Список цитирований

Список публикаций, цитирующих продукты Lumiprobe. Публикации можно отсортировать по дате или по продукту.

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по дате по продукту

1-Этинилпирен

  1. Vega, B.; Wondraczek, H.; Bretschneider, L.; Näreoja, T.; Fardim, P.; Heinze, T. Preparation of reactive fibre interfaces using multifunctional cellulose derivatives. Carbohydrate Polymers, 2015, 132, 261–273. doi: 10.1016/j.carbpol.2015.05.048

BDP 558/568 активированный эфир

  1. Tabe, H.; Sukenobe, K.; Kondo, T.; Sakurai, A.; Maruo, M.; Shimauchi, A.; Hirano, M.; Uno, S.-N.; Kamiya, M.; Urano, Y.; Matsushita, M.; Fujiyoshi, S. Cryogenic Fluorescence Localization Microscopy of Spectrally Selected Individual FRET Pairs in a Water Matrix. The Journal of Physical Chemistry B, 2018, 122(27), 6906–6911. doi: 10.1021/acs.jpcb.8b03977

BDP 581/591 активированный эфир

  1. Tabe, H.; Sukenobe, K.; Kondo, T.; Sakurai, A.; Maruo, M.; Shimauchi, A.; Hirano, M.; Uno, S.-N.; Kamiya, M.; Urano, Y.; Matsushita, M.; Fujiyoshi, S. Cryogenic Fluorescence Localization Microscopy of Spectrally Selected Individual FRET Pairs in a Water Matrix. The Journal of Physical Chemistry B, 2018, 122(27), 6906–6911. doi: 10.1021/acs.jpcb.8b03977

BDP 630/650 амин

  1. Zhang, Y.; Zhu, X.; Chen, X.; Chen, Q.; Zhou, W.; Guo, Q.; Lu, Y.; Li, C.; Zhang, Y.; Liang, D.; Sun, T.; Wei, X.; Jiang, C. Activated Platelets-Targeting Micelles with Controlled Drug Release for Effective Treatment of Primary and Metastatic Triple Negative Breast Cancer. Advanced Functional Materials, 2019, 29(13), 1806620. doi: 10.1002/adfm.201806620
  2. Zhang, Y.; Guo, Z.; Cao, Z.; Zhou, W.; Zhang, Y.; Chen, Q.; Lu, Y.; Chen, X.; Guo, Q.; Li, C.; Liang, D.; Sun, T.; Jiang, C. Endogenous albumin-mediated delivery of redox-responsive paclitaxel-loaded micelles for targeted cancer therapy. Biomaterials, 2018, 183, 243–257. doi: 10.1016/j.biomaterials.2018.06.002

BDP 630/650 карбоновая кислота

  1. Mitronova, G.Y.; Lukinavičius, G.; Butkevich, A.N.; Kohl, T.; Belov, V.N.; Lehnart, S.E.; Hell, S.W. High-Affinity Functional Fluorescent Ligands for Human β-Adrenoceptors. Scientific Reports, 2017, 7, 12319. doi: 10.1038/s41598-017-12468-3

BDP FL азид

  1. Nuhn, L.; Boli, E.; Massa, S.; Vandenberghe, I.; Movahedi, K.; Devreese, B.; Van Ginderachter, J.; De Geest, B.G. Targeting protumoral tumor-associated macrophages with nanobody-functionalized nanogels through SPAAC ligation. Bioconjugate Chemistry, 2018, 29(7), 2394–2405. doi: 10.1021/acs.bioconjchem.8b00319

BDP FL активированный эфир

  1. São Pedro, M.N.; Azevedo, A.M.; Aires-Barros, M.R.; Soares, R.R.G. Minimizing the influence of fluorescent tags on IgG partition in PEG-salt aqueous two-phase systems for rapid screening applications. Biotechnology Journal, in press. doi: 10.1002/biot.201800640
  2. Burla, F.; Tauber, J.; Dussi, S.; van der Gucht, J.; Koenderink, G.H. Stress management in composite biopolymer networks. Nature Physics, 2019, 15(6), 549–553. doi: 10.1038/s41567-019-0443-6
  3. Qi, T.; Chen, B.; Wang, Z.; Du, H.; Liu, D.; Yin, Q.; Liu, B.; Zhang, Q.; Wang, Y. A pH-Activatable nanoparticle for dual-stage precisely mitochondria-targeted photodynamic anticancer therapy. Biomaterials, 2019, 213, 119219. doi: 10.1016/j.biomaterials.2019.05.030
  4. Steinmetz, H.P.; Rudnick-Glick, S.; Natan, M.; Banin, E.; Margel, S. Poly(styryl bisphosphonate) nanoparticles with a narrow size distribution: Synthesis, characterization and antibacterial applications. European Polymer Journal, 2019, 116, 65–73. doi: 10.1016/j.eurpolymj.2019.04.007
  5. Reichart, F.; Maltsev, O.V.; Kapp, T.G.; Räder, A.F.B.; Weinmüller, M.; Marelli, U.K.; Notni, J.; Wurzer, A.; Beck, R.; Wester, H.-J.; Steiger, K.; Di Maro, S.; Di Leva, F.S.; Marinelli, L.; Nieberler, M.; Reuning, U.; Schwaiger, M.; Kessler, H. Selective Targeting of Integrin αvβ8 by a Highly Active Cyclic Peptide. Journal of Medicinal Chemistry, 2019, 62(4), 2024–2037. doi: 10.1021/acs.jmedchem.8b01588
  6. Alferova, V.A.; Shuvalov, M.V.; Suchkova, T.A.; Proskurin, G.V.; Aparin, I.O.; Rogozhin, E.A.; Novikov, R.A.; Solyev, P.N.; Chistov, A.A.; Ustinov, A.V.; Tyurin, A.P.; Korshun, V.A. 4-Chloro-L-kynurenine as fluorescent amino acid in natural peptides. Amino Acids, 2018, 50(12), 1697–1705. doi: 10.1007/s00726-018-2642-3
  7. Poreba, M.; Rut, W.; Vizovisek, M.; Groborz, K.; Kasperkiewicz, P.; Finlay, D.; Vuori, K.; Turk, D.; Turk, B.; Salvesen, G.; Drag, M. Selective imaging of human cathepsin L in breast cancer by fluorescent activity-based probes. Chemical Science, 2018, 9(8), 2113–2129. doi: 10.1039/C7SC04303A
  8. Grube, L.; Dellen, R.; Kruse, F.; Schwender, H.; Stuehler, K.; Poschmann, G. Mining the secretome of C2C12 muscle cells: Data dependent experimental approach to analyze protein secretion using label-free quantification and peptide based analysis. Journal of Proteome Research, 2018, 17(2), 879–890. doi: 10.1021/acs.jproteome.7b00684
  9. Wang, C.; Niederstrasser, H.; Douglas, P.M.; Lin, R.; Jaramillo, J.; Li, Y.; Olswald, N.W.; Zhou, A.; McMillan, E.A.; Mendiratta, S.; Wang, Z.; Zhao, T.; Lin, Z.; Luo, M.; Huang, G.; Brekken, R.A.; Posner, B.A.; MacMillan, J.B.; Gao, J.; White, M.A. Small-molecule TFEB pathway agonists that ameliorate metabolic syndrome in mice and extend C. elegans lifespan. Nature Communications, 2017, 8, 2270. doi: 10.1038/s41467-017-02332-3
  10. Gaspar, I.; Wippich, F.; Ephrussi, A. Enzymatic production of single molecule FISH and RNA capture probes. RNA, 2017, 23(10), 1582–1591. doi: 10.1261/rna.061184.117
  11. Perez-Anes, A.; Szarpak-Jankowska, A.; Jary, D.; Auzély-Velty, R. β-CD-Functionalized Microdevice for Rapid Capture and Release of Bacteria. ACS Applied Materials & Interfaces, 2017, 9(16), 13928–13938. doi: 10.1021/acsami.7b02194
  12. Löschmann, N.; Michaelis, M.; Rothweiler, F.; Voges, Y.; Balónová, B.; Blight, B.A.; Cinatl, J. ABCB1 as predominant resistance mechanism in cells with acquired SNS-032 resistance. Oncotarget, 2016, 7(36), 58051–58064. doi: 10.18632/oncotarget.11160
  13. Wang, C.; Wang, Y.; Li, Y.; Bodemann, B.; Zhao, T.; Ma, X.; Huang, G.; Hu, Z.; DeBerardinis, R.J.; White, M.A.; Gao, J. A nanobuffer reporter library for fine-scale imaging and perturbation of endocytic organelles. Nature Communications, 2015, 6, 8524. doi: 10.1038/ncomms9524

BDP FL алкин

  1. Daryaee, F.; Zhang, Z.; Gogarty, K.R.; Li, Y.; Merino, J.; Fisher, S.L.; Tonge, P.J. A quantitative mechanistic PK/PD model directly connects Btk target engagement and in vivo efficacy. Chemical Science, 2017, 8(5), 3434–3443. doi: 10.1039/c6sc03306g
  2. Kubota, T.; Durek, T.; Dang, B.; Finol-Urdaneta, R.K.; Craik, D.J.; Kent, S.B.H.; French, R.J.; Bezanilla, F.; Correa, A.M. Mapping of voltage sensor positions in resting and inactivated mammalian sodium channels by LRET. Proceedings of the National Academy of Sciences of the U.S.A., 2017, 114(10), E1857–1865. doi: 10.1073/pnas.1700453114

BDP FL амин

  1. Zhu, M.; Lu, D.; Wu, S.; Lian, Q.; Wang, W.; Lyon, A.; Wang, W.; Bartolo, P.; Saunders, B.R. Using green emitting pH-responsive nanogels to report environmental changes within hydrogels: A nanoprobe for versatile sensing. Nanoscale, in press. doi: 10.1039/c9nr00989b

BDP FL гидразид

  1. Liu, R.; Vairaprakash, P.; Lindsey, J.S. Self-assembly with fluorescence readout in a free base dipyrrin–polymer triggered by metal ion binding in aqueous solution. New Journal of Chemistry, 2019, 43(24), 9711–9724. doi: 10.1039/c9nj01787a

BDP FL малеимид

  1. São Pedro, M.N.; Azevedo, A.M.; Aires-Barros, M.R.; Soares, R.R.G. Minimizing the influence of fluorescent tags on IgG partition in PEG-salt aqueous two-phase systems for rapid screening applications. Biotechnology Journal, in press. doi: 10.1002/biot.201800640
  2. Doh, J.K.; White, J.D.; Zane, H.K.; Chang, Y.H.; López, C.S.; Enns, C.A.; Beatty, K.E. VIPER is a genetically encoded peptide tag for fluorescence and electron microscopy. Proceedings of the National Academy of Sciences of the United States of America, 2018, 115, 12961–12966. doi: 10.1073/pnas.1808626115
  3. Buecheler, J.W.; Winzer, M.; Tonillo, J.; Weber, C.A.; Gieseler, H. Impact of Payload Hydrophobicity on Stability of Antibody-Drug-Conjugates. Molecular Pharmaceutics, 2018, 15(7), 2656–2664. doi: 10.1021/acs.molpharmaceut.8b00177
  4. Mardirossian, M.; Pérébaskine, N.; Benincasa, M.; Gambato, S.; Hofmann, S.; Huter, P.; Müller, C.; Hilpert, K.; Innis, C.A.; Tossi, A.; Wilson, D.N. The Dolphin Proline-Rich Antimicrobial Peptide Tur1A Inhibits Protein Synthesis by Targeting the Bacterial Ribosome. Cell Chemical Biology, 2018, 25(5), 530–539.e7. doi: 10.1016/j.chembiol.2018.02.004

Coumarin 343 X активированный эфир

  1. Zheng, L.; Zhao, H.; Han, Y.; Qian, H.; Vukovic, L.; Mecinović, J.; Král, P.; Huck, W.T.S. Catalytic transport of molecular cargo using diffusive binding along a polymer track. Nature Chemistry, 2019, 11(4), 359–366. doi: 10.1038/s41557-018-0204-7

Cu(II)-TBTA комплекс, 10 мМ в 55% водном ДМСО

  1. Reyes-Ruiz, J.M.; Osuna-Ramos, J.F.; Bautista-Carbajal, P.; Jaworski, E.; Soto-Acosta, R.; Cervantes-Salazar, M.; Angel-Ambrocio, A.H.; Castillo-Munguía, J.P.; Chávez-Munguía, B.; De Nova-Ocampo, M.; Routh, A.; del Ángel, R.M.; Salas-Benito, J.S. Mosquito cells persistently infected with dengue virus produce viral particles with host-dependent replication. Virology, 2019, 531, 1–18. doi: 10.1016/j.virol.2019.02.018
  2. Elrod, N.R.; Jaworski, E.A.; Ji, P.; Wagner, E.J.; Routh, A. Development of Poly(A)-ClickSeq as a Tool Enabling Simultaneous Genome-wide Poly(A)-site identification and Differential Expression Analysis. Methods, 2019, 155, 20–29. doi: 10.1016/j.ymeth.2019.01.002
  3. Kuznetsov, A.E.; Komarova, N.V.; Kuznetsov, E.V.; Andrianova, M.S.; Grudtsov, V.P.; Rybachek, E.N.; Puchnin, K.V.; Ryazantsev, D.V.; Saurov, A.N. Integration of a field effect transistor-based aptasensor under a hydrophobic membrane for bioelectronic nose applications. Biosensors and Bioelectronics, 2019, 129, 29–35. doi: 10.1016/j.bios.2019.01.013
  4. Domljanovic, I.; Hansen, A.H.; Hansen, L.H.; Klitgaard, J.K.; Taskova, M.; Astakhova, K. Studies of Impending Oligonucleotide Therapeutics in Simulated Biofluids. Nucleic Acid Therapeutics, 2018, 28(6), 348–356. doi: 10.1089/nat.2017.0704
  5. van Hall-Beauvais, A.; Zhao, Y.; Urul, D.A.; Long, M.J.C.; Aye, Y. Single-Protein-Specific Redox Targeting in Live Mammalian Cells and C. elegans. Current Protocols in Chemical Biology, 2018, 10(3), e43. doi: 10.1002/cpch.43
  6. Schrand, B.; Clark, E.; Levay, A.; Capote, A.R.; Martinez, O.; Brenneman, R.; Castro, I.; Gilboa, E. Hapten-mediated recruitment of polyclonal antibodies to tumors engenders antitumor immunity. Nature Communications, 2018, 9, 3348. doi: 10.1038/s41467-018-05566-x
  7. Surya, S.L.; Long, M.J.C.; Urul, D.A.; Zhao, Y.; Mercer, E.J.; EIsaid, I.M.; Evans, T.; Aye, Y. Cardiovascular Small Heat Shock Protein HSPB7 Is a Kinetically Privileged Reactive Electrophilic Species (RES) Sensor. ACS Chemical Biology, 2018, 13(7), 1824–1831. doi: 10.1021/acschembio.7b00925
  8. Yang, J.; Jiang, Q.; He, L.; Zhan, P.; Liu, Q.; Liu, S.; Fu, M.; Liu, J.; Li, C.; Ding, B. Self-Assembled Double-Bundle DNA Tetrahedron for Efficient Antisense Delivery. ACS Applied Materials & Interfaces, 2018, 10(28), 23693–23699. doi: 10.1021/acsami.8b07889
  9. Long, M.J.C.; Urul, D.A.; Chawla, S.; Lin, H.-Y.; Zhao, Y.; Haegele, J.A.; Wang, Y.; Aye, Y. Precision Electrophile Tagging in Caenorhabditis elegans. Biochemistry, 2018, 57(2), 216–220. doi: 10.1021/acs.biochem.7b00642
  10. Andrianova, M.; Komarova, N.; Grudtsov, V.; Kuznetsov, E.; Kuznetsov, A. Amplified Detection of the Aptamer-Vanillin Complex with the Use of Bsm DNA Polymerase. Sensors, 2018, 18, 49. doi: 10.3390/s18010049
  11. Jaworski, E.; Routh, A. ClickSeq: Replacing Fragmentation and Enzymatic Ligation with Click-Chemistry to Prevent Sequence Chimeras. Methods in Molecular Biology, 2018, 1712, 71–85. doi: 10.1007/978-1-4939-7514-3_6
  12. Kuznetsov, A.; Komarova, N.; Andrianova, M.; Grudtsov, V.; Kuznetsov, E. Aptamer based vanillin sensor using an ion-sensitive field-effect transistor. Microchimica Acta, 2018, 185(1), 3. doi: 10.1007/s00604-017-2586-4
  13. Routh, A.; Ji, P.; Jaworski, E.; Xia, Z.; Li, W.; Wagner, E.J. Poly(A)-ClickSeq: click-chemistry for next-generation 3′-end sequencing without RNA enrichment or fragmentation. Nucleic Acids Research, 2017, 45(12), e112. doi: 10.1093/nar/gkx286
  14. Jaworski, E.; Routh, A. Parallel ClickSeq and Nanopore sequencing elucidates the rapid evolution of defective-interfering RNAs in Flock House virus. PLOS Pathogens, 2017, 13(5), e1006365. doi: 10.1371/journal.ppat.1006365
  15. Taskova, M.; Uhd, J.; Miotke, L.; Kubit, M.; Bell, J.; Ji, H.P.; Astakhova, K. Tandem Oligonucleotide Probe Annealing and Elongation To Discriminate Viral Sequence. Analytical Chemistry, 2017, 89(8), 4363–4366. doi: 10.1021/acs.analchem.7b00646
  16. Taskova, M.; Madsen, C.S.; Jensen, K.J.; Hansen, L.H.; Vester, B.; Astakhova, K. Antisense oligonucleotides internally labeled with peptides show improved target recognition and stability to enzymatic degradation. Bioconjugate Chemistry, 2017, 28(3), 768–774. doi: 10.1021/acs.bioconjchem.6b00567
  17. Long, M.J.C.; Parvez, S.; Zhao, Y.; Surya, S.L.; Wang, Y.; Zhang, S.; Aye, Y. Akt3 is a privileged first responder in isozyme-specific electrophile response. Nature Chemical Biology, 2017, 13(3), 333–338. doi: 10.1038/nchembio.2284
  18. Westergaard Mulberg, M.; Taskova, M.; Thomsen, R.P.; Okholm, A.H.; Kjems, J.; Astakhova, K. New Fluorescent Nanoparticles for Ultrasensitive Detection of Nucleic Acids by Optical Methods. Chembiochem, 2017, 18(16), 1599–1603. doi: 10.1002/cbic.201700125
  19. Shi, P.; Ju, E.; Yan, Z.; Gao, N.; Wang, J.; Hou, J.; Zhang, Y.; Ren, J.; Qu, X. Spatiotemporal control of cell-cell reversible interactions using molecular engineering. Nature communications, 2016, 7, 13088. doi: 10.1038/ncomms13088
  20. Samuelsen, S.V.; Maity, A.; Nybo, M.; Macaubas, C.; Lønstrup, L.; Balboni, I.M.; Mellins, E.D.; Astakhova, K. Novel Phospholipid-Protein Conjugates Allow Improved Detection of Antibodies in Patients with Autoimmune Diseases. PLoS One, 2016, 11(6), e0156125. doi: 10.1371/journal.pone.0156125
  21. Seo, K.-H.; Chu, H.-S.; Yoo, T.H.; Lee, S.-G.; Won, J.-I. Separation efficiency of free-solution conjugated electrophoresis with drag-tags incorporating a synthetic amino acid. Electrophoresis, 2016, 37(5–6), 818–825. doi: 10.1002/elps.201500506
  22. Li, Z.; Liu, Z.; Chen, Z.; Ju, E.; Li, W.; Ren, J.; Qu, X. Bioorthogonal chemistry for selective recognition, separation and killing bacteria over mammalian cells. Chemical Communications, 2016, 52(17), 3482–3485. doi: 10.1039/c5cc10625g
  23. Maity, A.; Macaubas, C.; Mellins, E.; Astakhova, K. Synthesis of Phospholipid-Protein Conjugates as New Antigens for Autoimmune Antibodies. Molecules, 2015, 20(6), 10253–10263. doi: 10.3390/molecules200610253
  24. Abel, G.R.; Cao, B.H.; Hein, J.E.; Ye, T. Covalent, sequence-specific attachment of long {DNA} molecules to a surface using DNA-templated click chemistry. Chemical Communications, 2014, 50(60), 8131–8133. doi: 10.1039/c4cc02900c
  25. Stuart, C.H.; Horita, D.A.; Thomas, M.J.; Salsbury, F.R.; Lively, M.O.; Gmeiner, W.H. Site-Specific DNA-Doxorubicin Conjugates Display Enhanced Cytotoxicity to Breast Cancer Cells. Bioconjugate Chemistry, 2014, 25(2), 406-413. doi: 10.1021/bc4005427
  26. Myung, J.-K.; Banuelos, C.A.; Fernandez, J.G.; Mawji, N.R.; Wang, J.; Tien, A.H.; Yang, Y.C.; Tavakoli, I.; Haile, S.; Watt, K.; McEwan, I.J.; Plymate, S.; Andersen, R.J.; Sadar, M.D. An androgen receptor N-terminal domain antagonist for treating prostate cancer. Journal of Clinical Investigation, 2013, 123(7), 2948–2960. doi: 10.1172/jci66398
  27. Astakhova, I.K.; Hansen, L.H.; Vester, B.; Wengel, J. Peptide-LNA oligonucleotide conjugates. Organic & Biomolecular Chemistry, 2013, 11(25), 4240-4240. doi: 10.1039/c3ob40786a
  28. Lu, X.; Song, C.-X.; Szulwach, K.; Wang, Z.; Weidenbacher, P.; Jin, P.; He, C. Chemical Modification-Assisted Bisulfite Sequencing (CAB-Seq) for 5-Carboxylcytosine Detection in DNA. Journal of the American Chemical Society, 2013, 135(25), 9315-9317. doi: 10.1021/ja4044856
  29. Kovacic, S.; Samii, L.; Woolfson, D.N.; Curmi, P.M.G.; Linke, H.; Forde, N.R.; Blab, G.A. Design and Construction of a One-Dimensional DNA Track for an Artificial Molecular Motor. Journal of Nanomaterials, 2012, 2012, ID-ID 109238. doi: 10.1155/2012/109238
  30. Meimetis, L.G.; Williams, D.E.; Mawji, N.R.; Banuelos, C.A.; Lal, A.A.; Park, J.J.; Tien, A.H.; Fernandez, J.G.; de Voogd, N.J.; Sadar, M.D. et al. Niphatenones, Glycerol Ethers from the Sponge Niphates digitalis Block Androgen Receptor Transcriptional Activity in Prostate Cancer Cells: Structure Elucidation, Synthesis, and Biological Activity . Journal of Medicinal Chemistry, 2012, 55(1), 503-514. doi: 10.1021/jm2014056

Cyanine2 для двумерного электрофореза

  1. Mildažienė, Vida and Aleknavičiūtė, V.; Žūkienė, R.; Paužaitė, G.; Naučienė, Z.; Filatova, I.; Lyushkevich, V.; Haimi, P.; Tamošiūnė, I.; Baniulis, D. Treatment of Common Sunflower (Helianthus annus L.) Seeds with Radio-frequency Electromagnetic Field and Cold Plasma Induces Changes in Seed Phytohormone Balance, Seedling Development and Leaf Protein Expression. Scientific Reports, 2019, 9, 6437. doi: 10.1038/s41598-019-42893-5
  2. Simon, Á.; Gulyás, G.; Mészár, Z.; Bhide, M.; Oláh, J.; Bai, P.; Csősz, É.; Jávor, A.; Komlósi, I.; Remenyik, J.; Czeglédi, L. Proteomics alterations in chicken jejunum caused by 24 h fasting. PeerJ, 2019, 7, e6588. doi: 10.7717/peerj.6588
  3. Laberge, A.; Ayoub, A.; Arif, S.; Larochelle, S.; Garnier, A.; Moulin, V.J. α-2-Macroglobulin induces the shedding of microvesicles from cutaneous wound myofibroblasts. Journal of Cellular Physiology, 2019, 234(7), 11369–11379. doi: 10.1002/jcp.27794
  4. Tesarova, B.; Charousova, M.; Dostalova, S.; Bienko, A.; Kopel, P.; Kruszyński, R.; Hynek, D.; Michalek, P.; Eckschlager, T.; Stiborova, M.; Adam, V.; Heger, Z. Folic acid-mediated re-shuttling of ferritin receptor specificity towards a selective delivery of highly cytotoxic nickel(II) coordination compounds. International Journal of Biological Macromolecules, 2019, 126, 1099–1111. doi: 10.1016/j.ijbiomac.2018.12.128
  5. Arevalo-Martin, A.; Grassner, L.; Garcia-Ovejero, D.; Paniagua-Torija, B.; Barroso-Garcia, G.; Arandilla, A.G.; Mach, O.; Turrero, A.; Vargas, E.; Alcobendas, M.; Rosell, C.; Alcaraz, M.A.; Ceruelo, S.; Casado, R.;Talavera, F.; Palazón, R.; Sanchez-Blanco, N.; Maier, D.; Esclarin, A.; Molina-Holgado, E. Elevated Autoantibodies in Subacute Human Spinal Cord Injury Are Naturally Occurring Antibodies. Frontiers in Immunology, 2018, 9, 2365. doi: 10.3389/fimmu.2018.02365
  6. Lu, J.; Tang, M.; Liu, Y.; Wang, J.; Wu, Z. Comparative Proteomics of Chromium-Transformed Beas-2B Cells by 2D-DIGE and MALDI-TOF/TOF MS. Biological Trace Element Research, 2018, 185(1), 78–88. doi: 10.1007/s12011-017-1222-9
  7. Tamošiūnė, I.; Stanienė, G.; Haimi, P.; Stanys, V.; Rugienius, R.; Baniulis, D. Endophytic Bacillus and Pseudomonas spp. Modulate Apple Shoot Growth, Cellular Redox Balance, and Protein Expression Under in Vitro Conditions. Frontiers in Plant Science, 2018, 9, 889. doi: 10.3389/fpls.2018.00889
  8. Tsikandelova, R.; Mladenov, P.; Planchon, S.; Kalenderova, S.; Praskova, M.; Mihaylova, Z.; Stanimirov, P.; Mitev, V.; Renaut, J.; Ishkitiev, N. Proteome response of dental pulp cells to exogenous FGF8. Journal of Proteomics, 2018, 183, 14–24. doi: 10.1016/j.jprot.2018.05.004
  9. Jun, D.; Minic, Z.; Bhat, S.V.; Vanderlinde, E.M.; Yost, C.K.; Babu, M.; Dahms, T.E.S. Metabolic Adaptation of a C-Terminal Protease A-Deficient Rhizobium leguminosarum in Response to Loss of Nutrient Transport. Frontiers in Microbiology, 2018, 8, 2617. doi: 10.3389/fmicb.2017.02617
  10. Shields, K.J.; Wu, C. Differential Adipose Tissue Proteomics. Methods in Molecular Biology, 2017, 1788, 243–250. doi: 10.1007/7651_2017_80
  11. Zhao, P.; George, J.V.; Li, B.; Amini, N.; Paluh, J.; Wang, J. Clickable Multifunctional Dumbbell Particles for In Situ Multiplex Single-Cell Cytokine Detection. ACS Applied Materials & Interfaces, 2017, 9(38), 32482–32488. doi: 10.1021/acsami.7b08338
  12. Merjaneh, M.; Langlois, A.; Larochelle, S.; Cloutier, C.B.; Ricard-Blum, S.; Moulin, V.J. Pro-angiogenic capacities of microvesicles produced by skin wound myofibroblasts. Angiogenesis, 2017, 20(3), 385–398. doi: 10.1007/s10456-017-9554-9
  13. Sikorskaite-Gudziuniene, S.; Haimi, P.; Gelvonauskiene, D.; Stanys, V. Nuclear proteome analysis of apple cultivar ‘Antonovka’ accessions in response to apple scab (Venturia inaequalis). European Journal of Plant Pathology, 2017, 148(4), 771–784. doi: 10.1007/s10658-016-1131-3
  14. Bian, Y.; Deng, X.; Yan, X.; Zhou, J.; Yuan, L.; Yan, Y. Integrated proteomic analysis of Brachypodium distachyon roots and leaves reveals a synergistic network in the response to drought stress and recovery. Scientific Reports, 2017, 7, 46183. doi: 10.1038/srep46183
  15. Nemethova, M.; Talian, I.; Danielisova, V.; Tkacikova, S.; Bonova, P.; Bober, P.; Matiasova, M.; Sabo, J.; Burda, J. Delayed bradykinin postconditioning modulates intrinsic neuroprotective enzyme expression in the rat CA1 region after cerebral ischemia: a proteomic study. Metabolic Brain Disease, 2016, 31(6), 1391–1403. doi: 10.1007/s11011-016-9859-1
  16. Lu, J.; Zhou, Z.; Zheng, J.; Zhang, Z.; Lu, R.; Liu, H.; Shi, H.; Tu, Z. 2D-DIGE and MALDI TOF/TOF MS analysis reveal that small GTPase signaling pathways may play an important role in cadmium-induced colon cell malignant transformation. Toxicology and Applied Pharmacology, 2015, 288(1), 106–113. doi: 10.1016/j.taap.2015.07.020
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  7. Burnham-Marusich, A.R.; Plechaty, A.M.; Berninsone, P.M. Size-matched alkyne-conjugated cyanine fluorophores to identify differences in protein glycosylation. Electrophoresis, 2014, 35(18), 2621-2625. doi: 10.1002/elps.201400241
  8. Hatzenpichler, R.; Scheller, S.; Tavormina, P.L.; Babin, B.M.; Tirrell, D.A.; Orphan, V.J. In situ visualization of newly synthesized proteins in environmental microbes using amino acid tagging and click chemistry. Environmental Microbiology, 2014, 16(8), 2568-2590. doi: 10.1111/1462-2920.12436

Cyanine3 амин

  1. van Herck, S.; Deswarte, K.; Nuhn, L.; Zhong, Z.; Portela Catani, J.P.; Li, Y.; Sanders, N.N.; Lienenklaus, S.; De Koker, S.; Lambrecht, B.N.; David, S.A.; De Geest, B.G. Lymph-Node-Targeted Immune Activation by Engineered Block Copolymer Amphiphiles-TLR7/8 Agonist Conjugates. Journal of the American Chemical Society, 2018, 140, 14300–14307. doi: 10.1021/jacs.8b08595
  2. Lufton, M.; Bustan, O.; Eylon, B.-h.; Shtifman-Segal, E.; Croitoru-Sadger, T.; Shagan, A.; Shabtay-Orbach, A.; Corem-Salkmon, E.; Berman, J.; Nyska, A.; Mizrahi, B. Living Bacteria in Thermoresponsive Gel for Treating Fungal Infections. Advanced Functional Materials, 2018, 28(40), 1801581. doi: 10.1002/adfm.201801581
  3. Huang, D.; Chen, Y.-S.; Green, C.R.; Rupenthal, I.D. Hyaluronic acid coated albumin nanoparticles for targeted peptide delivery in the treatment of retinal ischaemia. Biomaterials, 2018, 168, 10–23. doi: 10.1016/j.biomaterials.2018.03.034
  4. Murata, H.; Carmali, S.; Baker, S.L.; Matyjaszewski, K.; Russell, A.J. Solid-phase synthesis of protein-polymers on reversible immobilization supports. Nature Communications, 2018, 9, 845. doi: 10.1038/s41467-018-03153-8
  5. Huang, D.; Chen, Y.-S.; Xu, Q.; Hanes, J.; Rupenthal, I.D. Effects of enzymatic degradation on dynamic mechanical properties of the vitreous and intravitreal nanoparticle mobility. European Journal of Pharmaceutical Sciences, 2018, 118, 124–133. doi: 10.1016/j.ejps.2018.03.023
  6. Wollhofen, R.; Buchegger, B.; Eder, C.; Jacak, J.; Kreutzer, J.; Klar, T.A. Functional photoresists for sub-diffraction stimulated emission depletion lithography. Optical Materials Express, 2017, 7(7), 2538–2559. doi: 10.1364/ome.7.002538
  7. Wilson, D.R.; Mosenia, A.; Suprenant, M.P.; Upadhya, R.; Routkevitch, D.; Meyer, R.A.; Quinones-Hinojosa, A.; Green, J.J. Continuous Microfluidic Assembly of Biodegradable Poly(beta-amino ester)/DNA Nanoparticles for Enhanced Gene Delivery. Journal of Biomedical Materials Research. Part A, 2017, 105(6), 1813–1825. doi: 10.1002/jbm.a.36033
  8. Guldris, N.; Argibay, B.; Gallo, J.; Iglesias-Rey, R.; Carbó-Argibay, E.; Kolen'ko, Y.V.; Campos, F.; Sobrino, T.; Salonen, L.M.; Bañobre-López, M.; Castillo, J.; Rivas, J. Magnetite Nanoparticles for Stem Cell Labeling with High Efficiency and Long-Term in Vivo Tracking. Bioconjugate Chemistry, 2017, 28(2), 362–370. doi: 10.1021/acs.bioconjchem.6b00522
  9. Zhao, Y.; Houston, Z.H.; Simpson, J.D.; Chen, L.; Fletcher, N.L.; Fuchs, A.V.; Blakey, I.; Thurecht, K.J. Using Peptide Aptamer Targeted Polymers as a Model Nanomedicine for Investigating Drug Distribution in Cancer Nanotheranostics. Molecular Pharmaceutics, 2017, 14(10), 3539–3549. doi: 10.1021/acs.molpharmaceut.7b00560
  10. Guldris, N.; Argibay, B.; Kolen'ko, Y.V.; Carbó-Argibay, E.; Sobrino, T.; Campos, F.; Salonen, L.M.; Bañobre-López, M.; Castillo, J.; Rivas, J. Influence of the Separation Procedure on the Properties of Magnetic Nanoparticles: Gaining in vitro Stability and T1‐T2 Magnetic Resonance Imaging Performance. Journal of Colloid and Interface Science, 2016, 472, 229–236. doi: 10.1016/j.jcis.2016.03.040
  11. Gaitzsch, J.; Delahaye, M.; Poma, A.; Du Prez, F.; Battaglia, G. Comparison of metal free polymer-dye conjugation strategies in protic solvents. Polymer Chemistry, 2016, 7(17), 3046–3055;. doi: 10.1039/c6py00518g
  12. Demillo, V.G.; Zhu, X. Zwitterionic amphiphile coated magnetofluorescent nanoparticles – synthesis, characterization and tumor cell targeting. Journal of Materials Chemistry B, 2015, 3, 8328–8336. doi: 10.1039/C5TB01116G

Cyanine3 гидразид

  1. Zhang, J.; Chetnani, B.; Cormack, E.D.; Alonso, D.; Liu, W.; Mondragon, A.; Fei, J. Specific structural elements of the T-box riboswitch drive the two-step binding of the tRNA ligand. eLife, 2018, 7, e39518. doi: 10.7554/eLife.39518
  2. Cui, Z.; Wu, Y.; Mureev, S.; Alexandrov, K. Oligonucleotide-mediated tRNA sequestration enables one-pot sense codon reassignment in vitro. Nucleic Acids Research, 2018, 46(12), 6387–6400. doi: 10.1093/nar/gky365
  3. Porciani, D.; Cardwell, L.N.; Tawiah, K.d.; Alam, K.K.; Lange, M.J.; Daniels, M.A.; Burke, D.H. Modular cell-internalizing aptamer nanostructure enables targeted delivery of large functional RNAs in cancer cell lines. Nature Communications, 2018, 9(1), 2283. doi: 10.1038/s41467-018-04691-x
  4. Poudyal, R.R.; Nguyen, P.D.M.; Lokugamage, M.P.; Callaway, M.K.; Gavette, J.V.; Krishnamurthy, R.; Burke, D.H. Nucleobase modification by an RNA enzyme. Nucleic Acids Research, 2017, 45(3), 1345–1354. doi: 10.1093/nar/gkw1199
  5. Boone, C.; Grove, R.; Adamcova, D.; Braga, C.; Adamec, J. Revealing oxidative damage to enzymes of carbohydrate metabolism in yeast: An integration of 2D DIGE, quantitative proteomics and bioinformatics. Proteomics, 2016, 16(13), 1889–1903. doi: 10.1002/pmic.201500546

Cyanine3 для двумерного электрофореза

  1. Mildažienė, Vida and Aleknavičiūtė, V.; Žūkienė, R.; Paužaitė, G.; Naučienė, Z.; Filatova, I.; Lyushkevich, V.; Haimi, P.; Tamošiūnė, I.; Baniulis, D. Treatment of Common Sunflower (Helianthus annus L.) Seeds with Radio-frequency Electromagnetic Field and Cold Plasma Induces Changes in Seed Phytohormone Balance, Seedling Development and Leaf Protein Expression. Scientific Reports, 2019, 9, 6437. doi: 10.1038/s41598-019-42893-5
  2. Simon, Á.; Gulyás, G.; Mészár, Z.; Bhide, M.; Oláh, J.; Bai, P.; Csősz, É.; Jávor, A.; Komlósi, I.; Remenyik, J.; Czeglédi, L. Proteomics alterations in chicken jejunum caused by 24 h fasting. PeerJ, 2019, 7, e6588. doi: 10.7717/peerj.6588
  3. Laberge, A.; Ayoub, A.; Arif, S.; Larochelle, S.; Garnier, A.; Moulin, V.J. α-2-Macroglobulin induces the shedding of microvesicles from cutaneous wound myofibroblasts. Journal of Cellular Physiology, 2019, 234(7), 11369–11379. doi: 10.1002/jcp.27794
  4. Malheiros, J.M.; Braga, C.P.; Grove, R.A.; Ribeiro, F.A.; Calkins, C.R.; Adamec, J.; Chardulo, L.A.L. Influence of oxidative damage to proteins on meat tenderness using a proteomics approach. Meat Science, 2019, 148, 64–71. doi: 10.1016/j.meatsci.2018.08.016
  5. Jin, Y.N.; Schlueter, P.J.; Jurisch-Yaksi, N.; Lam, P.-Y.; Jin, S.; Hwang, W.Y.; Yeh, J.-R.J.; Yoshigi, M.; Ong, S.-E.; Schenone, M.; Hartigan, C.R.; Carr, S.A.; Peterson, R.T. Noncanonical translation via deadenylated 3' UTRs maintains primordial germ cells. Nature Chemical Biology, 2018, 14(9), 844–852. doi: 10.1038/s41589-018-0098-0
  6. Lu, J.; Tang, M.; Liu, Y.; Wang, J.; Wu, Z. Comparative Proteomics of Chromium-Transformed Beas-2B Cells by 2D-DIGE and MALDI-TOF/TOF MS. Biological Trace Element Research, 2018, 185(1), 78–88. doi: 10.1007/s12011-017-1222-9
  7. Tamošiūnė, I.; Stanienė, G.; Haimi, P.; Stanys, V.; Rugienius, R.; Baniulis, D. Endophytic Bacillus and Pseudomonas spp. Modulate Apple Shoot Growth, Cellular Redox Balance, and Protein Expression Under in Vitro Conditions. Frontiers in Plant Science, 2018, 9, 889. doi: 10.3389/fpls.2018.00889
  8. Tsikandelova, R.; Mladenov, P.; Planchon, S.; Kalenderova, S.; Praskova, M.; Mihaylova, Z.; Stanimirov, P.; Mitev, V.; Renaut, J.; Ishkitiev, N. Proteome response of dental pulp cells to exogenous FGF8. Journal of Proteomics, 2018, 183, 14–24. doi: 10.1016/j.jprot.2018.05.004
  9. Jun, D.; Minic, Z.; Bhat, S.V.; Vanderlinde, E.M.; Yost, C.K.; Babu, M.; Dahms, T.E.S. Metabolic Adaptation of a C-Terminal Protease A-Deficient Rhizobium leguminosarum in Response to Loss of Nutrient Transport. Frontiers in Microbiology, 2018, 8, 2617. doi: 10.3389/fmicb.2017.02617
  10. Shields, K.J.; Wu, C. Differential Adipose Tissue Proteomics. Methods in Molecular Biology, 2017, 1788, 243–250. doi: 10.1007/7651_2017_80
  11. Zhao, P.; George, J.V.; Li, B.; Amini, N.; Paluh, J.; Wang, J. Clickable Multifunctional Dumbbell Particles for In Situ Multiplex Single-Cell Cytokine Detection. ACS Applied Materials & Interfaces, 2017, 9(38), 32482–32488. doi: 10.1021/acsami.7b08338
  12. Haimi, P.; Vinskiene, J.; Stepulaitiene, I.; Baniulis, D.; Stanienė, G.; Šikšnianienė, J.B.; Rugienius, R. Patterns of low temperature-Induced accumulation of dehydrins in Rosaceae crops — Evidence for post-translational modification in apple. Journal of Plant Physiology, 2017, 218, 175–181. doi: 10.1016/j.jplph.2017.08.008
  13. Merjaneh, M.; Langlois, A.; Larochelle, S.; Cloutier, C.B.; Ricard-Blum, S.; Moulin, V.J. Pro-angiogenic capacities of microvesicles produced by skin wound myofibroblasts. Angiogenesis, 2017, 20(3), 385–398. doi: 10.1007/s10456-017-9554-9
  14. Sikorskaite-Gudziuniene, S.; Haimi, P.; Gelvonauskiene, D.; Stanys, V. Nuclear proteome analysis of apple cultivar ‘Antonovka’ accessions in response to apple scab (Venturia inaequalis). European Journal of Plant Pathology, 2017, 148(4), 771–784. doi: 10.1007/s10658-016-1131-3
  15. Heller, D.; Helmerhorst, E.J.; Oppenheim, F.G. Saliva and Serum Protein Exchange at the Tooth Enamel Surface. Journal of Dental Research, 2017, 96(4), 437–443. doi: 10.1177/0022034516680771
  16. Bian, Y.; Deng, X.; Yan, X.; Zhou, J.; Yuan, L.; Yan, Y. Integrated proteomic analysis of Brachypodium distachyon roots and leaves reveals a synergistic network in the response to drought stress and recovery. Scientific Reports, 2017, 7, 46183. doi: 10.1038/srep46183
  17. Kaux JF, Libertiaux V, Leprince P, Fillet M, Denoel V Wyss C, Lecut C, Gothot A, Le Goff C, Croisier JL, Crielaard JM, Drion P. Eccentric Training for Tendon Healing After Acute Lesion: A Rat Model. The American Journal of Sports Medicine, 2017, 45(6), 1440–1446. doi: 10.1177/0363546517689872
  18. Nemethova, M.; Talian, I.; Danielisova, V.; Tkacikova, S.; Bonova, P.; Bober, P.; Matiasova, M.; Sabo, J.; Burda, J. Delayed bradykinin postconditioning modulates intrinsic neuroprotective enzyme expression in the rat CA1 region after cerebral ischemia: a proteomic study. Metabolic Brain Disease, 2016, 31(6), 1391–1403. doi: 10.1007/s11011-016-9859-1
  19. Boone, C.; Grove, R.; Adamcova, D.; Braga, C.; Adamec, J. Revealing oxidative damage to enzymes of carbohydrate metabolism in yeast: An integration of 2D DIGE, quantitative proteomics and bioinformatics. Proteomics, 2016, 16(13), 1889–1903. doi: 10.1002/pmic.201500546
  20. Bertrand, A.; Bipfubusa, M.; Castonguay, Y.; Rocher, S.; Szopinska-Morawska, A.; Papadopoulos, Y.; Renaut, J. A proteome analysis of freezing tolerance in red clover (Trifolium pratense L.). BMC Plant Biology, 2016, 16, 65. doi: 10.1186/s12870-016-0751-2
  21. Bipfubusa, M.; Rocher, S.; Bertrand, A.; Castonguay, Y.; Renaut, J. Dataset of protein changes induced by cold acclimation in red clover (Trifolium pratense L.) populations recurrently selected for improved freezing tolerance. Data in Brief, 2016, 8, 570–574. doi: 10.1016/j.dib.2016.06.003
  22. Wang, Z.; Zourelias, L.; Wu, C.; Edwards, P.C.; Trombetta, M.; Passineau, M.J. Ultrasound-assisted nonviral gene transfer of AQP1 to the irradiated minipig parotid gland restores fluid secretion. Gene Therapy, 2015, 22, 739–749. doi: 10.1038/gt.2015.36
  23. Lu, J.; Zhou, Z.; Zheng, J.; Zhang, Z.; Lu, R.; Liu, H.; Shi, H.; Tu, Z. 2D-DIGE and MALDI TOF/TOF MS analysis reveal that small GTPase signaling pathways may play an important role in cadmium-induced colon cell malignant transformation. Toxicology and Applied Pharmacology, 2015, 288(1), 106–113. doi: 10.1016/j.taap.2015.07.020
  24. Printz, B.; Guerriero, G.; Sergeant, K.; Renaut, J.; Lutts, S.; Hausman, J.-F. Ups and downs in alfalfa: Proteomic and metabolic changes occurring in the growing stem. Plant Science, 2015, 238, 13–25. doi: 10.1016/j.plantsci.2015.05.014
  25. Ashoub, A.; Baeumlisberger, M.;Neupaertl, M.; Karas, M.; Brüggemann, W. Characterization of common and distinctive adjustments of wild barley leaf proteome under drought acclimation, heat stress and their combination. Plant Molecular Biology, 2015, 87(4–5), 459–471. doi: 10.1007/s11103-015-0291-4
  26. Feret, R.; Lilley, K.S. Protein Profiling Using Two-Dimensional Difference Gel Electrophoresis (2-D DIGE). Current Protocols in Protein Science, 2014, 22.2.1-22.2.17. doi: 10.1002/0471140864.ps2202s75
  27. Molinari, C.E.; Casadio, Y.S.; Hartmann, B.T.; Livk, A.; Bringans, S.; Arthur, P.G.; Hartmann, P.E. Proteome Mapping of Human Skim Milk Proteins in Term and Preterm Milk. Journal of Proteome Research, 2012, 11(3), 1696-1714. doi: 10.1021/pr2008797

Cyanine3 карбоновая кислота

  1. Deshmukh, R.; Biehs, S.-A.; Khwaja, E.; Galfsky, T.; Agarwal, G.S.; Menon, V.M. Long-range resonant energy transfer using optical topological transitions in metamaterials. ACS Photonics, 2018, 5(7), 2737–2741. doi: 10.1021/acsphotonics.8b00484
  2. Soni, K.S.; Lei, F.; Desale, S.S.; Marky, L.A.; Cohen, S.M.; Bronich, T.K. Tuning polypeptide-based micellar carrier for efficient combination therapy of ErbB2-positive breast cancer. Journal of Controlled Release, 2017, 264, 276–287. doi: 10.1016/j.jconrel.2017.08.038
  3. Melle, A.; Balaceanu, A.; Kather, M.; Wu, Y.; Gau, E.; Sun, W.; Huang, X.; Shi, X.; Karperien, M.; Pich, A. Stimuli-Responsive Poly(N}-vinylcaprolactam-co-2-methoxyethyl acrylate) Core-Shell Microgels: Facile Synthesis, Modulation of Surface Properties and Controlled Internalisation into Cells. Journal of Materials Chemistry B, 2016, 4(30), 5127–5137. doi: 10.1039/c6tb01196a
  4. Kwok, S.J.J.; Choi, M.; Bhayana, B.; Zhang, X.; Ran, C.; Yun, S.-H. Two-photon excited photoconversion of cyanine-based dyes. Scientific Reports, 2016, 6, 23866. doi: 10.1038/srep23866
  5. Xue, M.; Wei, W.; Su, Y.; Johnson, D.; Heath, J.R. Supramolecular Probes for Assessing Glutamine Uptake Enable Semi-Quantitative Metabolic Models in Single Cells. Journal of the American Chemical Society, 2016, 138(9), 3085–3093. doi: 10.1021/jacs.5b12187

Cyanine3 малеимид

  1. Singh, R.K.; Fan, J.; Gioacchini, N.; Watanabe, S.; Bilsel, O.; Peterson, C.L. Transient Kinetic Analysis of SWR1C-Catalyzed H2A.Z Deposition Unravels the Impact of Nucleosome Dynamics and the Asymmetry of Histone Exchange. Cell Reports, 2019, 27, 374–386.e4. doi: 10.1016/j.celrep.2019.03.035
  2. Gagni, P.; Romanato, A.; Bergamaschi, G.; Bettotti, P.; Vanna, R.; Piotto, C.; Morasso, C.F.; Chiari, M.; Cretich, M.; Gori, A. A self-assembling peptide hydrogel for ultrarapid 3D bioassays. Nanoscale Advances, 2019, 1(2), 490–497. doi: 10.1039/c8na00158h
  3. Wu, B.; Zhang, H.; Sun, R.; Peng, S.; Cooperman, B.S.; Goldman, Y.E.; Chen, C. Translocation kinetics and structural dynamics of ribosomes are modulated by the conformational plasticity of downstream pseudoknots. Nucleic Acids Research, 2018, 46(18), 9736–9748. doi: 10.1093/nar/gky636
  4. Liu, G.W.; Prossnitz, A.N.; Eng, D.G.; Cheng, Y.; Subrahmanyam, N.; Pippin, J.W.; Lamm, R.J.; Ngambenjawong, C.; Ghandehari, H.; Shankland, S.J.; Pun, S.H. Glomerular disease augments kidney accumulation of synthetic anionic polymers. Biomaterials, 2018, 178, 317–325. doi: 10.1016/j.biomaterials.2018.06.001
  5. Wojcik, F.; Dann, G.P.; Beh, L.Y.; Debelouchina, G.T.; Hofmann, R.; Muir, T.W. Functional crosstalk between histone H2B ubiquitylation and H2A modifications and variants. Nature Communications, 2018, 9, 1394. doi: 10.1038/s41467-018-03895-5
  6. Gadkari, V.V.; Harvey, S.R.; Raper, A.T.; Chu, W.-T.; Wang, J.; Wysocki, V.H.; Suo, Z. Investigation of sliding DNA clamp dynamics by single-molecule fluorescence, mass spectrometry and structure-based modeling. Nucleic Acids Research, 2018, 46(6), 3103–3118. doi: 10.1093/nar/gky125
  7. Raper, A.T.; Stephenson, A.A.; Suo, Z. Functional Insights Revealed by the Kinetic Mechanism of CRISPR/Cas9. Journal of the American Chemical Society, 2018, 140(8), 2971–2984. doi: 10.1021/jacs.7b13047
  8. Condon, S.G.F.; Mahbuba, D.-A.; Armstrong, C.R.; Díaz-Vázquez, G.; Craven, S.J.; LaPointe, L.M.; Khadria, A.S.; Chadda, R.; Crooks, J.A.; Rangarajan, N.; Weibel, D.B.; Hoskins, A.A.; Robertson, J.L.; Cui, Q.; Senes, A. The FtsLB sub-complex of the bacterial divisome is tetramer with an uninterrupted FtsL helix linking the transmembrane and periplasmic regions. Journal of Biological Chemistry, 2018, 293(5), 1623–1641. doi: 10.1074/jbc.RA117.000426
  9. Deyaert, E.; Wauters, L.; Guaitoli, G.; Konijnenberg, A.; Leemans, M.; Terheyden, S.; Petrovic, A.; Gallardo, R.; Nederveen-Schippers, L.M.; Athanasopoulos, P.S.; Pots, H.; Van Haastert, P.J.M.; Sobott, F.; Gloeckner, C.J.; Efremov, R.; Kortholt, A.; Versées, W. A homologue of the Parkinson's disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover. Nature Communications, 2017, 8(1), 1008. doi: 10.1038/s41467-017-01103-4
  10. Mateju, D.; Franzmann, T.M.; Patel, A.; Kopach, A.; Boczek, E.E.; Maharana, S.; Lee, H.O.; Carra, S.; Hyman, A.A.; Alberti, S. An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function. The EMBO Journal, 2017, 36(12), 1669–1687. doi: 10.15252/embj.201695957
  11. Maity, S.; Hashemi, M.; Lyubchenko, Y.L. Nano-assembly of amyloid β peptide: role of the hairpin fold. Scientific Reports, 2017, 7, 2344. doi: 10.1038/s41598-017-02454-0
  12. Wang, H.; Wu, J.; Xu, L.; Xie, K.; Chen, C.; Dong, Y. Albumin Nanoparticle Encapsulation of Potent Cytotoxic Therapeutics Shows Sustained Drug Release and Alleviates Cancer Drug Toxicity. Chemical Communications, 2017, 53(17), 2618–2621. doi: 10.1039/c6cc08978j
  13. Maity, S.; Viazovkina, E.; Gall, A.; Lyubchenko, Y.L. Single-molecule probing of amyloid nano-ensembles using the polymer nanoarray approach. Physical Chemistry Chemical Physics, 2017, 19(25), 16387–16394. doi: 10.1039/c7cp02691a
  14. Xue, C.; Whitis, N.R.; Sashital, D.G. Conformational Control of Cascade Interference and Priming Activities in CRISPR Immunity. Molecular Cell, 2016, 64(4), 826–834. doi: 10.1016/j.molcel.2016.09.033
  15. Chiu, H.-Y.; Deng, W.; Engelke, H.; Helma, J.; Leonhardt, H.; Bein, T. Intracellular chromobody delivery by mesoporous silica nanoparticles for antigen targeting and visualization in real time. Scientific Reports, 2016, 6, 25019. doi: 10.1038/srep25019
  16. Gaitzsch, J.; Delahaye, M.; Poma, A.; Du Prez, F.; Battaglia, G. Comparison of metal free polymer-dye conjugation strategies in protic solvents. Polymer Chemistry, 2016, 7(17), 3046–3055;. doi: 10.1039/c6py00518g
  17. Shrivastava, R.; Köster, D.; Kalme, S.; Mayor, S.; Neerathilingam, M. Tailor-made ezrin actin binding domain to probe its interaction with actin in-vitro. PLoS One, 2015, 10(4), e0123428. doi: 10.1371/journal.pone.0123428
  18. Schmidt, W.M.; Lehman, W.; Moore, J.R. Direct observation of tropomyosin binding to actin filaments. Cytoskeleton, 2015, 72(6), 292–303. doi: 10.1002/cm.21225
  19. Guo, Y.; Yuan, H.; Claudio, N.M.; Kura, S.; Shakerdge, N.; Mempel, T.R.; Bacskai, B.J.; Josephson, L. PEG-Like Nanoprobes: Multimodal, Pharmacokinetically and Optically Tunable Nanomaterials. PLoS ONE, 2014, 9(4), e95406. doi: 10.1371/journal.pone.0095406
  20. Graen, T.M.D.; Hoefling, M.; Grubmüller, H. AMBER-DYES: Characterization of Charge Fluctuations and Force Field Parameterization of Fluorescent Dyes for Molecular Dynamics Simulations. Journal of Chemical Theory and Computation, 2014, 10(12), 5505-5512. doi: 10.1021/ct500869p
  21. Schulze, R.J.; Komar, J.; Botte, M.; Allen, W.J.; Whitehouse, S.; Gold, V.A.M.; Lycklama a Nijeholt, J.A.; Huard, K.; Berger, I.; Schaffitzel, C. et al. Membrane protein insertion and proton-motive-force-dependent secretion through the bacterial holo-translocon SecYEG-SecDF-YajC-YidC. Proceedings of the National Academy of Sciences of the U.S.A., 2014, 111(13), 4844-4849. doi: 10.1073/pnas.1315901111

Cyanine3.5 азид

  1. Gaitzsch, J.; Delahaye, M.; Poma, A.; Du Prez, F.; Battaglia, G. Comparison of metal free polymer-dye conjugation strategies in protic solvents. Polymer Chemistry, 2016, 7(17), 3046–3055;. doi: 10.1039/c6py00518g
  2. Astakhova, I.K.; Wengel, J. Interfacing Click Chemistry with Automated Oligonucleotide Synthesis for the Preparation of Fluorescent DNA Probes Containing Internal Xanthene and Cyanine Dyes. Chemistry - a European Journal, 2013, 19(3), 1112-1122. doi: 10.1002/chem.201202621

Cyanine3.5 активированный эфир

  1. Wang, C.; Niederstrasser, H.; Douglas, P.M.; Lin, R.; Jaramillo, J.; Li, Y.; Olswald, N.W.; Zhou, A.; McMillan, E.A.; Mendiratta, S.; Wang, Z.; Zhao, T.; Lin, Z.; Luo, M.; Huang, G.; Brekken, R.A.; Posner, B.A.; MacMillan, J.B.; Gao, J.; White, M.A. Small-molecule TFEB pathway agonists that ameliorate metabolic syndrome in mice and extend C. elegans lifespan. Nature Communications, 2017, 8, 2270. doi: 10.1038/s41467-017-02332-3
  2. Massey, M.; Kim, H.; Conroy, E.M.; Algar, W.R. Expanded Quantum Dot-Based Concentric Förster Resonance Energy Transfer: Adding and Characterizing Energy-Transfer Pathways for Triply Multiplexed Biosensing. The Journal of Physical Chemistry C, 2017, 121(24), 13345–13356. doi: 10.1021/acs.jpcc.7b02739
  3. Wang, C.; Wang, Y.; Li, Y.; Bodemann, B.; Zhao, T.; Ma, X.; Huang, G.; Hu, Z.; DeBerardinis, R.J.; White, M.A.; Gao, J. A nanobuffer reporter library for fine-scale imaging and perturbation of endocytic organelles. Nature Communications, 2015, 6, 8524. doi: 10.1038/ncomms9524
  4. Fu, B.; Flynn, J.D.; Isaacoff, B.P.; Rowland, D.J.; Biteen, J.S. Super-Resolving the Distance-Dependent Plasmon-Enhanced Fluorescence of Single Dye and Fluorescent Protein Molecules. The Journal of Physical Chemistry C, 2015, 119(33), 19350–19358. doi: 10.1021/acs.jpcc.5b05154

Cyanine3.5 карбоновая кислота

  1. Kwok, S.J.J.; Choi, M.; Bhayana, B.; Zhang, X.; Ran, C.; Yun, S.-H. Two-photon excited photoconversion of cyanine-based dyes. Scientific Reports, 2016, 6, 23866. doi: 10.1038/srep23866

Cyanine5 ДБЦО

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Cyanine5 активированный эфир

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  130. Duellberg, C.; Trokter, M.; Jha, R.; Sen, I.; Steinmetz, M.O.; Surrey, T. Reconstitution of a hierarchical +TIP interaction network controlling microtubule end tracking of dynein. Nature Cell Biology, 2014, 16(8), 804-811. doi: 10.1038/ncb2999
  131. Geertsema, H.J.; Kulczyk, A.W.; Richardson, C.C.; van Oijen, A.M. Single-molecule studies of polymerase dynamics and stoichiometry at the bacteriophage T7 replication machinery. Proceedings of the National Academy of Sciences of the U.S.A., 2014, 111(11), 4073-4078. doi: 10.1073/pnas.1402010111
  132. Graen, T.M.D.; Hoefling, M.; Grubmüller, H. AMBER-DYES: Characterization of Charge Fluctuations and Force Field Parameterization of Fluorescent Dyes for Molecular Dynamics Simulations. Journal of Chemical Theory and Computation, 2014, 10(12), 5505-5512. doi: 10.1021/ct500869p
  133. Hu, X.; Wang, Q.; Liu, Y.; Liu, H.; Qin, C.; Cheng, K.; Robinson, W.; Gray, B.D.; Pak, K.Y.; Yu, A. et al. Optical imaging of articular cartilage degeneration using near-infrared dipicolylamine probes. Biomaterials, 2014, 35(26), 7511-7521. doi: 10.1016/j.biomaterials.2014.05.042
  134. Novo, L.; Rizzo, L.Y.; Golombek, S.K.; Dakwar, G.R.; Lou, B.; Remaut, K.; Mastrobattista, E.; van Nostrum, C.F.; Jahnen-Dechent, W.; Kiessling, F. et al. Decationized polyplexes as stable and safe carrier systems for improved biodistribution in systemic gene therapy. Journal of Controlled Release, 2014, 195, 162-175. doi: 10.1016/j.jconrel.2014.08.028
  135. Zhang, Y.; Ge, C.; Zhu, C.; Salaita, K. DNA-based digital tension probes reveal integrin forces during early cell adhesion. Nature Communications, 2014, 5, 5167-5167. doi: 10.1038/ncomms6167
  136. Chen, H.; Xiao, L.; Anraku, Y.; Mi, P.; Liu, X.; Cabral, H.; Inoue, A.; Nomoto, T.; Kishimura, A.; Nishiyama, N. et al. Polyion Complex Vesicles for Photoinduced Intracellular Delivery of Amphiphilic Photosensitizer. Journal of the American Chemical Society, 2014, 136(1), 157-163. doi: 10.1021/ja406992w
  137. Lee, S.; Ashizawa, A.T.; Kim, K.S.; Falk, D.J.; Notterpek, L. Liposomes to Target Peripheral Neurons and Schwann Cells. PLoS ONE, 2013, 8(11), e78724. doi: 10.1371/journal.pone.0078724
  138. Albertazzi, L.; Martinez-Veracoechea, F.J.; Leenders, C.M.A.; Voets, I.K.; Frenkel, D.; Meijer, E.W. Spatiotemporal control and superselectivity in supramolecular polymers using multivalency. Proceedings of the National Academy of Sciences of the U.S.A., 2013, 110(30), 12203-12208. doi: 10.1073/pnas.1303109110
  139. Cheng, M.-C.; Leske, A.T.; Matsuoka, T.; Kim, B.C.; Lee, J.; Burns, M.A.; Takayama, S.; Biteen, J.S. Super-Resolution Imaging of PDMS Nanochannels by Single-Molecule Micelle-Assisted Blink Microscopy. The Journal of Physical Chemistry B, 2013, 117(16), 4406-4411. doi: 10.1021/jp307635v
  140. Haller, A.; Altman, R.B.; Souliere, M.F.; Blanchard, S.C.; Micura, R. Folding and ligand recognition of the TPP riboswitch aptamer at single-molecule resolution. Proceedings of the National Academy of Sciences of the U.S.A., 2013, 110(11), 4188-4193. doi: 10.1073/pnas.1218062110
  141. He, H.; Chen, S.; Zhou, J.; Dou, Y.; Song, L.; Che, L.; Zhou, X.; Chen, X.; Jia, Y.; Zhang, J. et al. Cyclodextrin-derived pH-responsive nanoparticles for delivery of paclitaxel. Biomaterials, 2013, 34(21), 5344-5358. doi: 10.1016/j.biomaterials.2013.03.068
  142. Rimpelová, S.; Bříza, T.; Králová, J.; Záruba, K.; Kejík, Z.; Císařová, I.; Martásek, P.; Ruml, T.; Král, V. Rational Design of Chemical Ligands for Selective Mitochondrial Targeting. Bioconjugate Chemistry, 2013, 24(9), 1445-1454. doi: 10.1021/bc400291f
  143. Soulière, M.F.; Altman, R.B.; Schwarz, V.; Haller, A.; Blanchard, S.C.; Micura, R. Tuning a riboswitch response through structural extension of a pseudoknot. Proceedings of the National Academy of Sciences of the U.S.A., 2013, 110(35), E3256-E3264. doi: 10.1073/pnas.1304585110
  144. Yang, H.; Mao, H.; Wan, Z.; Zhu, A.; Guo, M.; Li, Y.; Li, X.; Wan, J.; Yang, X.; Shuai, X. et al. Micelles assembled with carbocyanine dyes for theranostic near-infrared fluorescent cancer imaging and photothermal therapy. Biomaterials, 2013, 34(36), 9124-9133. doi: 10.1016/j.biomaterials.2013.08.022
  145. Pecqueur, L.; Duellberg, C.; Dreier, B.; Jiang, Q.; Wang, C.; Pluckthun, A.; Surrey, T.; Gigant, B.; Knossow, M. A designed ankyrin repeat protein selected to bind to tubulin caps the microtubule plus end. Proceedings of the National Academy of Sciences of the U.S.A., 2012, 109(30), 12011-12016. doi: 10.1073/pnas.1204129109
  146. Sparks, J.; Slobodkin, G.; Matar, M.; Congo, R.; Ulkoski, D.; Rea-Ramsey, A.; Pence, C.; Rice, J.; McClure, D.; Polach, K.J. et al. Versatile cationic lipids for siRNA delivery. Journal of Controlled Release, 2012, 158(2), 269-276. doi: 10.1016/j.jconrel.2011.11.006

Cyanine5 алкин

  1. Mietlicki-Baase, E.G.; Liberini, C.G.; Workinger, J.L.; Bonaccorso, R.L.; Borner, T.; Reiner, D.J.; Koch-Laskowski, K.; McGrath, L.E.; Lhamo, R.; Stein, L.M.; De Jonghe, B.C.; Holz, G.G.; Roth, C.L.; Doyle, R.P.; Hayes, M.R. A Vitamin B12 Conjugate of Exendin-4 Improves Glucose Tolerance Without Associated Nausea or Hypophagia in Rodents. Diabetes, Obesity & Metabolism, 2018, 20(5), 1223–1234. doi: 10.1111/dom.13222
  2. Sacoman, J.L.; Dagda, R.Y.; Burnham-Marusich, A.R.; Dagda, R.K.; Berninsone, P.M. Mitochondrial O-GlcNAc transferase (mOGT) regulates mitochondrial structure, function and survival in HeLa cells. Journal of Biological Chemistry, 2017, 292(11), 4499–4518. doi: 10.1074/jbc.M116.726752
  3. Wallat, J.D.; Czapar, A.E.; Wang, C.; Wen, A.M.; Wek, K.S.; Yu, X.; Steinmetz, N.F.; Pokorski, J.K. Optical and Magnetic Resonance Imaging Using Fluorous Colloidal Nanoparticles. Biomacromolecules, 2017, 18(1), 103–112. doi: 10.1021/acs.biomac.6b01389
  4. Zhao, T.; Li, T.; Liu, Y. Silver nanoparticle plasmonic enhanced förster resonance energy transfer (FRET) imaging of protein-specific sialylation on the cell surface. Nanoscale, 2017, 9(28), 9841–9847. doi: 10.1039/c7nr01562c
  5. Ponomarenko, A.I.; Brylev, V.A.; Sapozhnikova, K.A.; Ustinov, A.V.; Prokhorenko, I.A.; Zatsepin, T.S.; Korshun, V.A. Tetrahedral DNA conjugates from pentaerythritol-based polyazides. Tetrahedron, 2016, 72(19), 2386–2391. doi: 10.1016/j.tet.2016.03.051
  6. Burnham-Marusich, A.R.; Plechaty, A.M.; Berninsone, P.M. Size-matched alkyne-conjugated cyanine fluorophores to identify differences in protein glycosylation. Electrophoresis, 2014, 35(18), 2621-2625. doi: 10.1002/elps.201400241
  7. Truong, F.; Yoo, T.H.; Lampo, T.J.; Tirrell, D.A. Two-Strain, Cell-Selective Protein Labeling in Mixed Bacterial Cultures. Journal of the American Chemical Society, 2012, 134(20), 8551-8556. doi: 10.1021/ja3004667

Cyanine5 амин

  1. Feczkó, T.; Merza, G.; Babos, G.; Varga, B.; Gyetvai, E.; Trif, L.; Kovács, E.; Tuba, R. Preparation of cubic-shaped sorafenib-loaded nanocomposite using well-defined poly(vinyl alcohol alt-propenylene) copolymer. International Journal of Pharmaceutics, 2019, 562, 333–341. doi: 10.1016/j.ijpharm.2019.03.008
  2. Wilson, D.R.; Rui, Y.; Siddiq, K.; Routkevitch, D.; Green, J.J. Differentially Branched Ester Amine Quadpolymers with Amphiphilic and pH Sensitive Properties for Efficient Plasmid DNA Delivery. Molecular Pharmaceutics, 2019, 16(2), 655–668. doi: 10.1021/acs.molpharmaceut.8b00963
  3. van Driessche, A; Kocere, A.; Everaert, H.; Nuhn, L.; van Herck, S.; Griffiths, G.; Fenaroli, F.; de Geest, B.G. pH-sensitive hydrazone-linked doxorubicin nanogels via polymeric activated ester scaffolds: synthesis, assembly, in vitro and in vivo evaluation in tumor bearing zebrafish. Chemistry of Materials, 2018, 30(23), 8587–8596. doi: 10.1021/acs.chemmater.8b03702
  4. Nuhn, L.; De Koker, S.; Van Lint, S.; Zhong, Z.; Catani, J.P.; Combes, F.; Deswarte, K.; Li, Y.; Lambrecht, B.N.; Lienenklaus, S.; Sanders, N.N.; David, S.A.; Tavernier, J.; De Geest, B.G. Nanoparticle-Conjugate TLR7/8 Agonist Localized Immunotherapy Provokes Safe Antitumoral Responses. Advanced Materials, 2018, 30(45), e1803397. doi: 10.1002/adma.201803397
  5. van Herck, S.; Deswarte, K.; Nuhn, L.; Zhong, Z.; Portela Catani, J.P.; Li, Y.; Sanders, N.N.; Lienenklaus, S.; De Koker, S.; Lambrecht, B.N.; David, S.A.; De Geest, B.G. Lymph-Node-Targeted Immune Activation by Engineered Block Copolymer Amphiphiles-TLR7/8 Agonist Conjugates. Journal of the American Chemical Society, 2018, 140, 14300–14307. doi: 10.1021/jacs.8b08595
  6. Babos, G.; Biró, E.; Meiczinger, M.; Feczkó, T. Dual Drug Delivery of Sorafenib and Doxorubicin from PLGA and PEG-PLGA Polymeric Nanoparticles. Polymers, 2018, 10(8), 895. doi: 10.3390/polym10080895
  7. Nuhn, L.; Van Hoecke, L.; Deswarte, K.; Schepens, B.; Li, Y.; Lambrecht, B.N.; De Koker, S.; David, S.A.; Saelens, X.; De Geest, B.G. Potent anti-viral vaccine adjuvant based on pH-degradable nanogels with covalently linked small molecule imidazoquinoline TLR7/8 agonist. Biomaterials, 2018, 178, 643–651. doi: 10.1016/j.biomaterials.2018.03.026
  8. Kongkatigumjorn, N.; Smith, S.A.; Chen, M.Z.; Fang, K.; Yang, S.; Gillies, E.R.; Johnston, A.P.R.; Such, G.K. Controlling Endosomal Escape Using pH Responsive Nanoparticles with Tunable Disassembly. Applied Nano Materials, 2018, 1(7), 3164–3173. doi: 10.1021/acsanm.8b00338
  9. Wang, B.; Chen, G.; Urabe, G.; Xie, R.; Wang, Y.; Shi, X.; Guo, L.-W.; Gong, S.; Kent, K.C. A paradigm of endothelium-protective and stent-free anti-restenotic therapy using biomimetic nanoclusters. Biomaterials, 2018, 178, 293–301. doi: 10.1016/j.biomaterials.2018.06.025
  10. Shih, T.-Y.; Blacklow, S.O.; Li, A.W.; Freedman, B.R.; Bencherif, S.; Koshy, S.T.; Darnell, M.C.; Mooney, D.J. Injectable, Tough Alginate Cryogels as Cancer Vaccines. Advanced Healthcare Materials, 2018, 7(10), 1701469. doi: 10.1002/adhm.201701469
  11. Raghupathi, K.; Skinner, M.; Chang, G.; Crawley, C.; Yoshida-Moriguchi, T.; Pipenhagen, P.; Zhu, Y.; Avila, L.Z.; Miller, R.J.; Dhal, P.K. Hyaluronic Acid Microgels as Intracellular Endosomolysis Reagents. ACS Biomaterials Science & Engineering, 2018, 4(2), 558–565. doi: 10.1021/acsbiomaterials.7b00966
  12. Pan, G.; Jia, T.-t.; Huang, Q.-x. Qiu, Y.-y.; Xu, J. Yin, P.-h.; Liu, T. Mesoporous Silica Nanoparticles (MSNs)-Based Organic/Inorganic Hybrid Nanocarriers Loading 5-Fluorouracil for the Treatment of Colon Cancer with Improved Anticancer Efficacy. Colloids and Surfaces, B: Biointerfaces, 2017, 159, 375–385. doi: 10.1016/j.colsurfb.2017.08.013
  13. Chen, G.; Wang, Y.; Xie, R.; Gong, S. Tumor-targeted pH/redox dual-sensitive unimolecular nanoparticles for efficient siRNA delivery. Journal of Controlled Release, 2017, 259, 105–114. doi: 10.1016/j.jconrel.2017.01.042
  14. Wilson, D.R.; Routkevitch, D.; Rui, Y.; Mosenia, A.; Wahlin, K.J.; Quinones-Hinojosa, A.; Zack, D.J.; Green, J.J. A Triple-Fluorophore Labeled Nucleic Acid pH Nanosensor to Investigate Non-Viral Gene Delivery. Molecular Therapy, 2017, 25(7), 1697–1709. doi: 10.1016/j.ymthe.2017.04.008
  15. Wang, Y.; Wang, L.; Chen, G.; Gong, S. Carboplatin-Complexed and cRGD-Conjugated Unimolecular Nanoparticles for Targeted Ovarian Cancer Therapy. Macromolecular Bioscience, 2017, 17(5), 1600292. doi: 10.1002/mabi.201600292
  16. Qu, J.-B.; Chapman, R.; Chen, F.; Lu, H.; Stenzel, M.H. Swollen Micelles for the Preparation of Gated, Squeezable, pH-Responsive Drug Carriers. ACS Applied Materials & Interfaces, 2017, 9(16), 13865–13874. doi: 10.1021/acsami.7b01120
  17. Yin, M.; Bao, Y.; Gao, X.; Wu, Y.; Sun, Y.; Zhao, X.; Xu, H.; Zhang, Z.; Tan, S. Redox/pH dual-sensitive hybrid micelles for targeting delivery and overcoming multidrug resistance of cancer. Journal of Materials Chemistry B, 2017, 5(16), 2964–2978. doi: 10.1039/c6tb03282f
  18. Glass, J.J.; Li, Y.; De Rose, R.; Johnston, A.P.R.; Czuba, E.I.; Khor, S.Y.; Quinn, J.F.; Whittaker, M.R.; Davis, T.P.; Kent, S.J. Thiol-Reactive Star Polymers Display Enhanced Association with Distinct Human Blood Components. ACS Applied Materials & Interfaces, 2017, 9(14), 12182-12194. doi: 10.1021/acsami.6b15942
  19. Zhang, R.; Yang, J.; Radford, D.C.; Fang, Y.; Kopeček, J. FRET Imaging of Enzyme-Responsive HPMA Copolymer Conjugate. Macromolecular Bioscience, 2017, 17(1), 1600125. doi: 10.1002/mabi.201600125
  20. Shalgunov, V.; Zaytseva-Zotova, D.; Zinchenko, A.; Levada, T.; Shilov, Y.; Andreyev, D.; Dzhumashev, D.; Metelkin, E.; Urusova, A.; Demin, O.; McDonnell, K.; Troiano, G.; Zale, S.; Safarovа, E. Comprehensive study of the drug delivery properties of poly(L-lactide)-poly(ethylene glycol) nanoparticles in rats and tumor-bearing mice. Journal of Controlled Release, 2017, 261, 31–42. doi: 10.1016/j.jconrel.2017.06.006
  21. Stefanello, T.; Couturaud, B.; Szarpak, A.; Fournier, D.; Louage, B.; Garcia, F.; Vataru Nakamura, C.; De Geest, B.; Woisel, P.; van der Sanden, B.; Auzely, R. Coumarin-containing thermoresponsive hyaluronic acid-based nanogels as delivery systems for anticancer chemotherapy. Nanoscale, 2017, 9(33), 12150–12162. doi: 10.1039/C7NR03964F
  22. Yang, W.; Xia, Y.; Zou, Y.; Meng, F.; Zhang, J.; Zhong, Z. Bioresponsive Chimaeric Nano-polymersomes Enable Targeted and Efficacious Protein Therapy for Human Lung Cancers in Vivo. Chemistry of Materials, 2017, 29(20), 8757–8765. doi: 10.1021/acs.chemmater.7b02953
  23. Pombo-García, K.; Weiss, S.; Zarschler, K.; Ang, C.-S.; Hübner, R.; Pufe, J.; Meister, S.; Seidel, J.; Pietzsch, J.; Spiccia, L.; Stephan, H.; Graham, B. Zwitterionic polymer-coated ultrasmall superparamagnetic iron oxide nanoparticles with low protein interaction and high biocompatibility. ChemNanoMat, 2016, 2(10), 959–971. doi: 10.1002/cnma.201600233
  24. Mann, S.K.; Dufour, A.; Glass, J.J.; De Rose, R.; Kent, S.J.; Such, G.K.; Johnston, A.P.R. Tuning the properties of pH responsive nanoparticles to control cellular interactions in vitro and ex vivo. Polymer Chemistry, 2016, 7(38), 6015–6024. doi: 10.1039/c6py01332e
  25. Mann, S.K.; Czuba, E.; Selby, L.I.; Such, G.K.; Johnston, A.P.R. Quantifying Nanoparticle Internalization Using a High Throughput Internalization Assay. Pharmaceutical Research, 2016, 33(10), 2421–2432. doi: 10.1007/s11095-016-1984-3
  26. Priwitaningrum, D.L.; Blonde, J.-B.; van Baarlen, J.; Hennink, W.E.; Storm, G.; Le Gac, S.; Prakash, J. Tumor stroma-containing 3D spheroid arrays: A tool to study nanoparticle penetration. Journal of Controlled Release, 2016, 244(Part B), 257–268. doi: 10.1016/j.jconrel.2016.09.004
  27. Zhu, Y.; Wang, X.; Chen, J.; Zhang, J.; Meng, F.; Deng, C.; Cheng, R.; Feijen, J.; Zhong, Z. Bioresponsive and fluorescent hyaluronic acid-iodixanol nanogels for targeted X-ray computed tomography imaging and chemotherapy of breast tumors. Journal of controlled release, 2016, 244(Part B), 229–239. doi: 10.1016/j.jconrel.2016.08.027
  28. Hartley, J.M.; Zhang, R.; Gudheti, M.; Yang, J.; Kopeček, J. Tracking and quantifying polymer therapeutic distribution on a cellular level using 3D dSTORM. Journal of Controlled Release, 2016, 231, 50–59. doi: 10.1016/j.jconrel.2016.02.005
  29. Bruckman, M.A.; Czapar, A.E.; VanMeter, A.; Randolph, L.N.; Steinmetz, N.F. Tobacco mosaic virus-based protein nanoparticles and nanorods for chemotherapy delivery targeting breast cancer. Journal of Controlled Release, 2016, 231, 103–113. doi: 10.1016/j.jconrel.2016.02.045
  30. Liu, T.; Yuan, X.; Jia, T.; and Liu, C.; Ni, Z.; Qin, Z.; Yuan, Y. Polymeric Prodrug of Bufalin for Increasing Solubility and Stability: Synthesis and Anticancer Study in Vitro and in Vivo. International Journal of Pharmaceutics, 2016, 506(1–2), 382–393. doi: 10.1016/j.ijpharm.2016.04.041
  31. Pan, G.; Bao, Y.-J.; Xu, J.; Liu, T.; Liu, C.; Qiu, Y.-Y.; Shi, X.-J.; Yu, H.; Jia, T.-T.; Yuan, X.; Yuan, Z.-T.; Yin, P.-H.; Cao, Y.-J. Esterase-responsive polymeric prodrug-based tumor targeting nanoparticles for improved anti-tumor performance against colon cancer. RSC Advances, 2016, 6(48), 42109–42119. doi: 10.1039/c6ra05236c
  32. Gao, D.; Zhang, P.; Liu, C.; Chen, C.; Gao, G.; Wu, Y.; Sheng, Z.; Song, L.; Cai, L. Compact chelator-free Ni-integrated CuS nanoparticles with tunable near-infrared absorption and enhanced relaxivity for in vivo dual-modal photoacoustic/MR imaging. Nanoscale, 2015, 7, 17631–17636. doi: 10.1039/C5NR05237H
  33. Yang, J.; Zhang, R.; Radford, D.C.; Kopeček, J. FRET-trackable biodegradable HPMA copolymer-epirubicin conjugates for ovarian carcinoma therapy. Journal of Controlled Release, 2015, 218, 36–44. doi: 10.1016/j.jconrel.2015.09.045
  34. Fuchs, A.V.; Tse, B.W.C.; Pearce, A.K.; Yeh, M.-C.; Fletcher, N.L.; Huang, S.S.; Heston, W.D.; Whittaker, A.K.; Russell, P.J.; Thurecht, K.J. Evaluation of Polymeric Nanomedicines Targeted to PSMA: Effect of Ligand on Targeting Efficiency. Biomacromolecules, 2015, 16(10), 3235–3247. doi: 10.1021/acs.biomac.5b00913
  35. Li, H.; Yang, Z.-Y.; Liu, C.; Zeng, Y.-P.; Hao, Y.-H. Gu, Y.; Wang, W.-D.; Li, R. PEGylated ceria nanoparticles used for radioprotection on Human liver cells under γ-ray irradiation. Free Radical Biology and Medicine, 2015, 87, 26–35. doi: 10.1016/j.freeradbiomed.2015.06.010
  36. Guo, Y.; Wang, D.; Song, Q.; Wu, T.; Zhuang, X.; Bao, Y.; Kong, M.; Qi, Y.; Tan, S.; Zhang, Z. Erythrocyte Membrane-Enveloped Polymeric Nanoparticles as Nanovaccine for Induction of Antitumor Immunity against Melanoma. ACS Nano, 2015, 9(7), 6918–6933. doi: 10.1021/acsnano.5b01042
  37. Ma, Y.; Fuchs, A.; Boase, N.R.B.; Rolfe, B.E.; Coombes, A.G.A.; Thurecht, K.J. The in vivo fate of nanoparticles and nanoparticle-loaded microcapsules after oral administration in mice: evaluation of their potential for colon-specific delivery. European Journal of Pharmaceutics and Biopharmaceutics, 2015, 94, 393–403. doi: 10.1016/j.ejpb.2015.06.014
  38. Zhang, R.; Yang, J.; Sima, M.; Zhou, Y.; Kopeček, J. Sequential combination therapy of ovarian cancer with degradable N-(2-hydroxypropyl)methacrylamide copolymer paclitaxel and gemcitabine conjugates. Proceedings of the National Academy of Sciences of the U.S.A., 2014, 111(33), 12181-12186. doi: 10.1073/pnas.1406233111

Cyanine5 гидразид

  1. Boone, C.; Grove, R.; Adamcova, D.; Braga, C.; Adamec, J. Revealing oxidative damage to enzymes of carbohydrate metabolism in yeast: An integration of 2D DIGE, quantitative proteomics and bioinformatics. Proteomics, 2016, 16(13), 1889–1903. doi: 10.1002/pmic.201500546
  2. Yoshimura, T.; Harashima, M.; Kurogi, K.; Suiko, M.; Liu, M.-C.; Sakakibara, Y. A novel procedure for the assessment of the antioxidant capacity of food components. Analytical Biochemistry, 2016, 507, 7–12. doi: 10.1016/j.ab.2016.05.002
  3. Huang, J.; Smith, F.; Panizzi, J.R.; Goodwin, D.C.; Panizzi, P. Inactivation of myeloperoxidase by benzoic acid hydrazide. Archives of Biochemistry and Biophysics, 2015, 570, 14–22. doi: 10.1016/j.abb.2015.01.028
  4. Einfalt, T.; Goers, R.; Dinu, I.A.; Najer, A.; Spulber, M.; Onaca-Fischer, O.; Palivan, C.G. Stimuli-triggered activity of nanoreactors by biomimetic engineering polymer membranes. Nano Letters, 2015, 15(11), 7596–7603. doi: 10.1021/acs.nanolett.5b03386
  5. Nienhaus, L.; Gross, D.E.; Xue, Z.; Moore, J.S.; Gruebele, M. Intramolecular energy transfer in a synthetic dendron-based light harvesting system. Journal of Photochemistry and Photobiology A: Chemistry, 2014, 295, 26-33. doi: 10.1016/j.jphotochem.2014.08.014
  6. Xie, M.; Xu, Y.; Shen, H.; Shen, S.; Ge, Y.; Xie, J. Negative-charge-functionalized mesoporous silica nanoparticles as drug vehicles targeting hepatocellular carcinoma. International Journal of Pharmaceutics, 2014, 474, 223-231. doi: 10.1016/j.ijpharm.2014.08.027
  7. Chang, Y.; Cai, C.; Li, L.; Miao, J.; Ucakturk, E.; Li, G.; Ly, M.; Linhardt, R.J. Ultrasensitive Detection and Quantification of Acidic Disaccharides Using Capillary Electrophoresis and Quantum Dot-Based Fluorescence Resonance Energy Transfer. Analytical Chemistry, 2013, 85(19), 9356-9362. doi: 10.1021/ac402242v
  8. Shen, H.; Shi, H.; Xie, M.; Ma, K.; Li, B.; Shen, S.; Wang, X.; Jin, Y. Biodegradable chitosan/alginate BSA-gel-capsules for pH-controlled loading and release of doxorubicin and treatment of pulmonary melanoma. Journal of Materials Chemistry B, 2013, 1(32), 3906-3906. doi: 10.1039/c3tb20330a
  9. Xie, M.; Shi, H.; Li, Z.; Shen, H.; Ma, K.; Li, B.; Shen, S.; Jin, Y. A multifunctional mesoporous silica nanocomposite for targeted delivery, controlled release of doxorubicin and bioimaging. Colloids and Surfaces B: Biointerfaces, 2013, 110, 138-147. doi: 10.1016/j.colsurfb.2013.04.009
  10. Xie, M.; Shi, H.; Ma, K.; Shen, H.; Li, B.; Shen, S.; Wang, X.; Jin, Y. Hybrid nanoparticles for drug delivery and bioimaging: Mesoporous silica nanoparticles functionalized with carboxyl groups and a near-infrared fluorescent dye. Journal of Colloid and Interface Science, 2013, 395, 306-314. doi: 10.1016/j.jcis.2013.01.001
  11. Xie, M.; Shi, H.; Ma, K.; Shen, H.; Li, B.; Shen, S.; Wang, X.; Jin, Y. Hybrid nanoparticles for drug delivery and bioimaging: Mesoporous silica nanoparticles functionalized with carboxyl groups and a near-infrared fluorescent dye. Journal of Colloid and Interface Science, 2013, 395, 306-314. doi: 10.1016/j.jcis.2013.01.001

Cyanine5 для разностного электрофореза

  1. Mildažienė, Vida and Aleknavičiūtė, V.; Žūkienė, R.; Paužaitė, G.; Naučienė, Z.; Filatova, I.; Lyushkevich, V.; Haimi, P.; Tamošiūnė, I.; Baniulis, D. Treatment of Common Sunflower (Helianthus annus L.) Seeds with Radio-frequency Electromagnetic Field and Cold Plasma Induces Changes in Seed Phytohormone Balance, Seedling Development and Leaf Protein Expression. Scientific Reports, 2019, 9, 6437. doi: 10.1038/s41598-019-42893-5
  2. Simon, Á.; Gulyás, G.; Mészár, Z.; Bhide, M.; Oláh, J.; Bai, P.; Csősz, É.; Jávor, A.; Komlósi, I.; Remenyik, J.; Czeglédi, L. Proteomics alterations in chicken jejunum caused by 24 h fasting. PeerJ, 2019, 7, e6588. doi: 10.7717/peerj.6588
  3. Laberge, A.; Ayoub, A.; Arif, S.; Larochelle, S.; Garnier, A.; Moulin, V.J. α-2-Macroglobulin induces the shedding of microvesicles from cutaneous wound myofibroblasts. Journal of Cellular Physiology, 2019, 234(7), 11369–11379. doi: 10.1002/jcp.27794
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  5. Jin, Y.N.; Schlueter, P.J.; Jurisch-Yaksi, N.; Lam, P.-Y.; Jin, S.; Hwang, W.Y.; Yeh, J.-R.J.; Yoshigi, M.; Ong, S.-E.; Schenone, M.; Hartigan, C.R.; Carr, S.A.; Peterson, R.T. Noncanonical translation via deadenylated 3' UTRs maintains primordial germ cells. Nature Chemical Biology, 2018, 14(9), 844–852. doi: 10.1038/s41589-018-0098-0
  6. Lu, J.; Tang, M.; Liu, Y.; Wang, J.; Wu, Z. Comparative Proteomics of Chromium-Transformed Beas-2B Cells by 2D-DIGE and MALDI-TOF/TOF MS. Biological Trace Element Research, 2018, 185(1), 78–88. doi: 10.1007/s12011-017-1222-9
  7. Tamošiūnė, I.; Stanienė, G.; Haimi, P.; Stanys, V.; Rugienius, R.; Baniulis, D. Endophytic Bacillus and Pseudomonas spp. Modulate Apple Shoot Growth, Cellular Redox Balance, and Protein Expression Under in Vitro Conditions. Frontiers in Plant Science, 2018, 9, 889. doi: 10.3389/fpls.2018.00889
  8. Tsikandelova, R.; Mladenov, P.; Planchon, S.; Kalenderova, S.; Praskova, M.; Mihaylova, Z.; Stanimirov, P.; Mitev, V.; Renaut, J.; Ishkitiev, N. Proteome response of dental pulp cells to exogenous FGF8. Journal of Proteomics, 2018, 183, 14–24. doi: 10.1016/j.jprot.2018.05.004
  9. Jun, D.; Minic, Z.; Bhat, S.V.; Vanderlinde, E.M.; Yost, C.K.; Babu, M.; Dahms, T.E.S. Metabolic Adaptation of a C-Terminal Protease A-Deficient Rhizobium leguminosarum in Response to Loss of Nutrient Transport. Frontiers in Microbiology, 2018, 8, 2617. doi: 10.3389/fmicb.2017.02617
  10. Shields, K.J.; Wu, C. Differential Adipose Tissue Proteomics. Methods in Molecular Biology, 2017, 1788, 243–250. doi: 10.1007/7651_2017_80
  11. Zhao, P.; George, J.V.; Li, B.; Amini, N.; Paluh, J.; Wang, J. Clickable Multifunctional Dumbbell Particles for In Situ Multiplex Single-Cell Cytokine Detection. ACS Applied Materials & Interfaces, 2017, 9(38), 32482–32488. doi: 10.1021/acsami.7b08338
  12. Haimi, P.; Vinskiene, J.; Stepulaitiene, I.; Baniulis, D.; Stanienė, G.; Šikšnianienė, J.B.; Rugienius, R. Patterns of low temperature-Induced accumulation of dehydrins in Rosaceae crops — Evidence for post-translational modification in apple. Journal of Plant Physiology, 2017, 218, 175–181. doi: 10.1016/j.jplph.2017.08.008
  13. Merjaneh, M.; Langlois, A.; Larochelle, S.; Cloutier, C.B.; Ricard-Blum, S.; Moulin, V.J. Pro-angiogenic capacities of microvesicles produced by skin wound myofibroblasts. Angiogenesis, 2017, 20(3), 385–398. doi: 10.1007/s10456-017-9554-9
  14. Sikorskaite-Gudziuniene, S.; Haimi, P.; Gelvonauskiene, D.; Stanys, V. Nuclear proteome analysis of apple cultivar ‘Antonovka’ accessions in response to apple scab (Venturia inaequalis). European Journal of Plant Pathology, 2017, 148(4), 771–784. doi: 10.1007/s10658-016-1131-3
  15. Heller, D.; Helmerhorst, E.J.; Oppenheim, F.G. Saliva and Serum Protein Exchange at the Tooth Enamel Surface. Journal of Dental Research, 2017, 96(4), 437–443. doi: 10.1177/0022034516680771
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  17. Kaux JF, Libertiaux V, Leprince P, Fillet M, Denoel V Wyss C, Lecut C, Gothot A, Le Goff C, Croisier JL, Crielaard JM, Drion P. Eccentric Training for Tendon Healing After Acute Lesion: A Rat Model. The American Journal of Sports Medicine, 2017, 45(6), 1440–1446. doi: 10.1177/0363546517689872
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Cyanine5 карбоновая кислота

  1. Santra, K.; Clark, K.D.; Maity, N.; Petrich, J.W.; Anderson, J.L. Exploiting Fluorescence Spectroscopy to Identify Magnetic Ionic Liquids Suitable for the Isolation of Oligonucleotides. The Journal of Physical Chemistry B, 2018, 122(31), 7747–7756. doi: 10.1021/acs.jpcb.8b05580
  2. Semkina, A.S.; Abakumov, M.A.; Skorikov, A.S.; Abakumova, T.O.; Melnikov, P.A.; Grinenko, N.F.; Cherepanov, S.A.; Vishnevskiy, D.A.; Naumenko, V.A.; Ionova, K.P.; Majouga, A.G.; Chekhonin, V.P. Multimodal doxorubicin loaded magnetic nanoparticles for {VEGF} targeted theranostics of breast cancer. Nanomedicine: Nanotechnology, Biology and Medicine, 2018, 14(5), 1733–1742. doi: 10.1016/j.nano.2018.04.019
  3. Kwok, S.J.J.; Choi, M.; Bhayana, B.; Zhang, X.; Ran, C.; Yun, S.-H. Two-photon excited photoconversion of cyanine-based dyes. Scientific Reports, 2016, 6, 23866. doi: 10.1038/srep23866
  4. Gupta, A.; Verma, N.C.; Khan, S.; Tiwari, S.; Chaudhary, A.; Nandi, C.K. Paper strip based and live cell ultrasensitive lead sensor using carbon dots synthesized from biological media. Sensors and Actuators B: Chemical, 2016, 232, 107–114. doi: 10.1016/j.snb.2016.03.110
  5. Deyle, K.M.; Farrow, B.; Hee, Y.Q.; Work, J.; Wong, M.; Lai, B.; Umeda, A.; Millward, S.W.; Nag, A.; Das, S.; Heath, J.R. A protein-targeting strategy used to develop a selective inhibitor of the E17K point mutation in the PH domain of Akt1. Nature Chemistry, 2015, 7, 455–462. doi: 10.1038/nchem.2223
  6. Rand, M.D.; Montgomery, S.L.; Prince, L.; Vorojeikina, D. Developmental Toxicity Assays Using the Drosophila Model. Current Protocols in Toxicology, 2014, 1.12.1-1.12.20. doi: 10.1002/0471140856.tx0112s59

Cyanine5 малеимид

  1. Ast, J.; Arvaniti, A.; Fine, N.H.F.; Nasteska, D.; Ashford, F.B.; Stamataki, Z.M Koszegi, Z.; Bacon, A.; Trapp, S.; Jones, B.J.; Hastoy, B.; Tomas, A.; Reissaus, C.; Linnemann, A.K.; D'Este, E.; Calebiro, D.; Johnsson, K.; Podewin, T.; Broichhagen, J.; Hodson, D.J. LUXendins reveal endogenous glucagon-like peptide-1 receptor distribution and dynamics. bioRxiv, preprint. doi: 10.1101/557132
  2. Singh, R.K.; Fan, J.; Gioacchini, N.; Watanabe, S.; Bilsel, O.; Peterson, C.L. Transient Kinetic Analysis of SWR1C-Catalyzed H2A.Z Deposition Unravels the Impact of Nucleosome Dynamics and the Asymmetry of Histone Exchange. Cell Reports, 2019, 27, 374–386.e4. doi: 10.1016/j.celrep.2019.03.035
  3. Gagni, P.; Romanato, A.; Bergamaschi, G.; Bettotti, P.; Vanna, R.; Piotto, C.; Morasso, C.F.; Chiari, M.; Cretich, M.; Gori, A. A self-assembling peptide hydrogel for ultrarapid 3D bioassays. Nanoscale Advances, 2019, 1(2), 490–497. doi: 10.1039/c8na00158h
  4. Doh, J.K.; White, J.D.; Zane, H.K.; Chang, Y.H.; López, C.S.; Enns, C.A.; Beatty, K.E. VIPER is a genetically encoded peptide tag for fluorescence and electron microscopy. Proceedings of the National Academy of Sciences of the United States of America, 2018, 115, 12961–12966. doi: 10.1073/pnas.1808626115
  5. Wu, B.; Zhang, H.; Sun, R.; Peng, S.; Cooperman, B.S.; Goldman, Y.E.; Chen, C. Translocation kinetics and structural dynamics of ribosomes are modulated by the conformational plasticity of downstream pseudoknots. Nucleic Acids Research, 2018, 46(18), 9736–9748. doi: 10.1093/nar/gky636
  6. Khor, S.Y.; Vu, M.N.; Pilkington, E.H.; Johnston, A.P.R.; Whittaker, M.R.; Quinn, J.F.; Truong, N.P.; Davis, T.P. Elucidating the Influences of Size, Surface Chemistry, and Dynamic Flow on Cellular Association of Nanoparticles Made by Polymerization-Induced Self-Assembly. Small, 2018, 14(34), e1801702. doi: 10.1002/smll.201801702
  7. Chambre, L.; Degirmenci, A.; Sanyal, R.; Sanyal, A. Multifunctional Nanogels as Theranostic Platforms: Exploiting Reversible and Non-reversible Linkages for Targeting, Imaging and Drug Delivery. Bioconjugate Chemistry, 2018, 29(6), 1885–1896. doi: 10.1021/acs.bioconjchem.8b00085
  8. Robinson, K.J.; Huynh, G.T.; Kouskousis, B.; Fletcher, N.L.; Houston, Z.H.; Thurecht, K.J.; Corrie, S.R. Modified organosilica core-shell nanoparticles for stable pH sensing in biological solutions. ACS Sensors, 2018, 3(5), 967–975. doi: 10.1021/acssensors.8b00034
  9. Gadkari, V.V.; Harvey, S.R.; Raper, A.T.; Chu, W.-T.; Wang, J.; Wysocki, V.H.; Suo, Z. Investigation of sliding DNA clamp dynamics by single-molecule fluorescence, mass spectrometry and structure-based modeling. Nucleic Acids Research, 2018, 46(6), 3103–3118. doi: 10.1093/nar/gky125
  10. Raper, A.T.; Stephenson, A.A.; Suo, Z. Functional Insights Revealed by the Kinetic Mechanism of CRISPR/Cas9. Journal of the American Chemical Society, 2018, 140(8), 2971–2984. doi: 10.1021/jacs.7b13047
  11. Jani, S.; Jackson, A.; Davies-Sala, C.; Chiem, K.; Soler-Bistué, A.; Zorreguieta, A.; Tolmasky, M.E. Assessment of External Guide Sequences' (EGS) Efficiency as Inducers of RNase P-Mediated Cleavage of mRNA Target Molecules. Methods in Molecular Biology, 2018, 1737, 89–98. doi: 10.1007/978-1-4939-7634-8_6
  12. Condon, S.G.F.; Mahbuba, D.-A.; Armstrong, C.R.; Díaz-Vázquez, G.; Craven, S.J.; LaPointe, L.M.; Khadria, A.S.; Chadda, R.; Crooks, J.A.; Rangarajan, N.; Weibel, D.B.; Hoskins, A.A.; Robertson, J.L.; Cui, Q.; Senes, A. The FtsLB sub-complex of the bacterial divisome is tetramer with an uninterrupted FtsL helix linking the transmembrane and periplasmic regions. Journal of Biological Chemistry, 2018, 293(5), 1623–1641. doi: 10.1074/jbc.RA117.000426
  13. Deyaert, E.; Wauters, L.; Guaitoli, G.; Konijnenberg, A.; Leemans, M.; Terheyden, S.; Petrovic, A.; Gallardo, R.; Nederveen-Schippers, L.M.; Athanasopoulos, P.S.; Pots, H.; Van Haastert, P.J.M.; Sobott, F.; Gloeckner, C.J.; Efremov, R.; Kortholt, A.; Versées, W. A homologue of the Parkinson's disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover. Nature Communications, 2017, 8(1), 1008. doi: 10.1038/s41467-017-01103-4
  14. Baranova, N.; Loose, M. Single-molecule measurements to study polymerization dynamics of FtsZ-FtsA copolymers. Methods in Cell Biology, 2017, 137, 355–370. doi: 10.1016/bs.mcb.2016.03.036
  15. Zhang, Z.; Yomo, D.; Gradinaru, C. Choosing the right fluorophore for single-molecule fluorescence studies in a lipid environment. Biochimica et Biophysica Acta – Biomembranes, 2017, 1859(7), 1242–1253. doi: 10.1016/j.bbamem.2017.04.001
  16. Chen, L.; Weinmeister, R.; Kralovicova, J.; Eperon, L.P.; Vorechovsky, I.; Hudson, A.J.; Eperon, I.C. Stoichiometries of U2AF35, U2AF65 and snRNP reveal new early spliceosome assembly pathways. Nucleic Acids Research, 2017, 45(4), 2051–2067. doi: 10.1093/nar/gkw860
  17. Hinde, E.; Thammasiraphop, K.; Duong, H.T.T.; Yeow, J.; Karagoz, B.; Boyer, C.; Gooding, J.J.; Gaus, K. Pair correlation microscopy reveals the role of nanoparticle shape in intracellular transport and site of drug release. Nature Nanotechnology, 2017, 12(1), 81–89. doi: 10.1038/nnano.2016.160
  18. Sahle, F.F.; Giulbudagian, M.; Bergueiro, J.; Lademann, J.; Calderón, M. Dendritic polyglycerol and N-isopropylacrylamide based thermoresponsive nanogels as smart carriers for controlled delivery of drugs through the hair follicle. Nanoscale, 2017, 9(1), 172–182. doi: 10.1039/c6nr06435c
  19. Qiu, Y.; Levendosky, R.F.; Chakravarthy, S.; Patel, A.; Bowman, G.D.; Myong, S. The Chd1 Chromatin Remodeler Shifts Nucleosomal DNA Bidirectionally as a Monomer. Molecular Cell, 2017, 68(1), 76–88.e6. doi: 10.1016/j.molcel.2017.08.018
  20. Jackson, A.; Jani, S.; Sala, C.D.; Soler-Bistué, A.J.C.; Zorreguieta, A.; Tolmasky, M.E. Assessment of configurations and chemistries of bridged nucleic acids-containing oligomers as external guide sequences: a methodology for inhibition of expression of antibiotic resistance genes. Biology Methods and Protocols, 2016, 1(1), bpw001. doi: 10.1093/biomethods/bpw001
  21. Yoshimura, T.; Kurogi, K.; Liu, M.-C.; Suiko, M.; Sakakibara, Y. A proteomic approach for the analysis of S-nitrosylated proteins using a fluorescence labeling technique. Journal of Electrophoresis, 2016, 60(1), 5–14. doi: 10.2198/jelectroph.60.5
  22. Xue, C.; Whitis, N.R.; Sashital, D.G. Conformational Control of Cascade Interference and Priming Activities in CRISPR Immunity. Molecular Cell, 2016, 64(4), 826–834. doi: 10.1016/j.molcel.2016.09.033
  23. Kollarigowda, R.H.; De Santo, I.; Rianna, C.; Fedele, C.; Manikas, A.C.; Cavalli, S.; Netti, P.A. Shedding light on azopolymer brush dynamics by fluorescence correlation spectroscopy. Soft Matter, 2016, 12(34), 7102–7111. doi: 10.1039/c6sm01482h
  24. Chadda, R.; Krishnamani, V.; Mersch, K.; Wong, J.; Brimberry, M.; Chadda, A.; Kolmakova-Partensky, L.; Friedman, L.J.; Gelles, J.; Robertson, J.L. The dimerization equilibrium of a ClC Cl/H+ antiporter in lipid bilayers. eLIFE, 2016, 5, e17438. doi: 10.7554/eLife.17438
  25. Zhao, Y.; Wei, Z.; Zhao, H.; Jia, J.; Chen, Z.; Zhang, S.; Ouyang, Z.; Ma, X.; Zhang, X. In situ Ion-Transmission Mass Spectrometry for Paper-Based Analytical Devices. Analytical Chemistry, 2016, 88(22), 10805–10810. doi: 10.1021/acs.analchem.6b03272
  26. Noriega, R.; Finley, D.T.; Haberstroh, J.; Geissler, P.L.; Francis, M.B.; Ginsberg, N.S. Manipulating Excited-State Dynamics of Individual Light-Harvesting Chromophores through Restricted Motions in a Hydrated Nanoscale Protein Cavity. The Journal of Physical Chemistry B, 2015, 119(23), 6963–6973. doi: 10.1021/acs.jpcb.5b03784
  27. Leonard, J.D.; Narlikar, G.J. A Nucleotide-Driven Switch Regulates Flanking DNA Length Sensing by a Dimeric Chromatin Remodeler. Molecular Cell, 2015, 57(5), 850–859. doi: 10.1016/j.molcel.2015.01.008
  28. Popp, M.W. Site-Specific Labeling of Proteins via Sortase: Protocols for the Molecular Biologist. Methods in Molecular Biology, 2015, 1266, 185–198. doi: 10.1007/978-1-4939-2272-7_13
  29. Lipchik, A.M.; Perez, M.; Cui, W.; Parker, L.L. Multicolored, Tb3+-Based Antibody-Free Detection of Multiple Tyrosine Kinase Activities. Analytical Chemistry, 2015, 87(15), 7555–7558. doi: 10.1021/acs.analchem.5b02233
  30. Graen, T.M.D.; Hoefling, M.; Grubmüller, H. AMBER-DYES: Characterization of Charge Fluctuations and Force Field Parameterization of Fluorescent Dyes for Molecular Dynamics Simulations. Journal of Chemical Theory and Computation, 2014, 10(12), 5505-5512. doi: 10.1021/ct500869p
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Cyanine5.5 азид

  1. Sun, H.; Yan, L.; Chang, M.Y.Z.; Carter, K.; Zhang, R.; Slyker, L.; Lovell, J.; Wu, Y.; Cheng, C. A multifunctional biodegradable brush polymer-drug conjugate for paclitaxel/gemcitabine co-delivery and tumor imaging. Nanoscale Advances, in press. doi: 10.1039/c9na00282k
  2. Al-Lawati, H.; Vakili, M.R.; Lavasanifar, A.; Ahmed, S.; Jamali, F. Delivery and biodistribution of traceable polymeric micellar diclofenac in the rat. Journal of Pharmaceutical Sciences, in press. doi: 10.1016/j.xphs.2019.03.016
  3. Carniato, F.; Alberti, D.; Lapadula, A.; Martinelli, J.; Isidoro, C.; Crich, S.G.; Tei, L. Multifunctional Gd-based mesoporous silica nanotheranostic for anticancer drug delivery. Journal of Materials Chemistry B, 2019, 7(19), 3143–3152. doi: 10.1039/c9tb00375d
  4. Zhang, H.; Wu, J.; Wu, J.; Fan, Q.; Zhou, J.; Wu, J.; Liu, S.; Zang, J.; Ye, J.; Xiao, M.; Tian, T.; Gao, J. Exosome-mediated targeted delivery of miR-210 for angiogenic therapy after cerebral ischemia in mice. Journal of Nanobiotechnology, 2019, 17, 29. doi: 10.1186/s12951-019-0461-7
  5. Sun, H.; Yan, L.; Carter, K.A.; Zhang, J.; Caserto, J.; Lovell, J.F.; Wu, Y.; Cheng, C. Zwitterionic Crosslinked Biodegradable Nanocapsules for Cancer Imaging. Langmuir, 2019, 35(5), 1440–1449. doi: 10.1021/acs.langmuir.8b01633
  6. Stefaniak, J.; Lewis, A.M.; Conole, D.; Galan, S.R.G.; Bataille, C.J.R.; Wynne, G.M.; Castaldi, M.P.; Lundbäck, T.; Russell, A.J.; Huber, K.V.M. Chemical Instability and Promiscuity of Arylmethylidenepyrazolinone-Based MDMX Inhibitors. ACS Chemical Biology, 2018, 13(10), 2849–2854. doi: 10.1021/acschembio.8b00665
  7. Tian, T.; Zhang, H.-X.; He, C.-P.; Fan, S.; Zhu, Y.-L.; Qi, C.; Huang, N.-P.; Xiao, Z.-D.; Lu, Z.-H.; Tannous, B.A.; Gao, J. Surface functionalized exosomes as targeted drug delivery vehicles for cerebral ischemia therapy. Biomaterials, 2018, 150, 137–149. doi: 10.1016/j.biomaterials.2017.10.012
  8. Cho, C.-F.; Wolfe, J.M.; Fadzen, C.M.; Calligaris, D.; Hornburg, K.; Chiocca, E.A.; Agar, N.Y.R.; Pentelute, B.L.; Lawler, S.E. Blood-brain-barrier spheroids as an in vitro screening platform for brain-penetrating agents. Nature Communications, 2017, 8, 15623. doi: 10.1038/ncomms15623
  9. Li, N.; Cai, H.; Jiang, L.; Hu, J.; Bains, A.; Hu, J.; Gong, Q.; Luo, K.; Gu, Z. Enzyme-Sensitive and Amphiphilic PEGylated Dendrimer-Paclitaxel Prodrug Based Nanoparticles for Enhanced Stability and Anticancer Efficacy. ACS Applied Materials & Interfaces, 2017, 9(8), 6865–6877. doi: 10.1021/acsami.6b15505
  10. Garg, S.M.; Paiva, I.M.; Vakili, M.R.; Soudy, R.; Agopsowicz, K.; Soleimani, A.; Hitt, M.; Kaur, K.; Lavasanifar, A. Traceable PEO-poly(ester) micelles for breast cancer targeting: The effect of core structure and targeting peptide on micellar tumor accumulation. Biomaterials, 2017, 144, 17–29. doi: 10.1016/j.biomaterials.2017.08.001
  11. Sun, Y.; Hong, S.; Ma, X.; Cheng, K.; Wang, J.; Zhang, Z.; Yang, M.; Jiang, Y.; Hong, X.; Cheng, Z. Recyclable Cu(I)/Melanin Dots for Cycloadditions, Bioconjugation and Cell Labeling. Chemical Science, 2016, 7(9), 5888–5892. doi: 10.1039/c6sc01536k
  12. Huang, R.; Conti, P.S.; Chen, K. In Vivo Tumor Angiogenesis Imaging Using Peptide-Based Near-Infrared Fluorescent Probes. Methods in Molecular Biology, 2016, 1444, 73–84. doi: 10.1007/978-1-4939-3721-9_8
  13. Puthenveetil, S.; Musto, S.; Loganzo, F.; Tumey, L.N.; O'Donnell, C.J.; Graziani, E.I. Development of solid-phase site-specific conjugation and its application towards generation of dual labeled antibody and Fab drug conjugates. Bioconjugate Chemistry, 2016, 27(4), 1030–1039. doi: 10.1021/acs.bioconjchem.6b00054
  14. Stone, R.C.; Fellows, B.D.; Qi, B.; Trebatowski, D.; Jenkins, B.; Raval, Y.; Tzeng, T.R.; Bruce, T.F.; Mcnealy, T.; Austin, M.J.; Monson, T.C.; Huber, D.L.; Mefford, O.T. Highly Stable Multi-Anchored Magnetic Nanoparticles for Optical Imaging within Biofilms. Journal of Colloid and Interface Science, 2015, 459, 175–182. doi: 10.1016/j.jcis.2015.08.012
  15. Zhong, J.; Li, L.; Zhu, X.; Guan, S.; Yang, Q.; Zhou, Z.; Zhang, Z.; Huang, Y. A smart polymeric platform for multistage nucleus-targeted anticancer drug delivery. Biomaterials, 2015, 65, 43–55. doi: 10.1016/j.biomaterials.2015.06.042
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Cyanine5.5 амин

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  11. Duret, D.; Grassin, A.; Henry, M.; Jacquet, T.; Thoreau, F.; Denis-Quanquin, S.; Coll, J.-L.; Boturyn, D.; Favier, A.; Charreyre, M.-T. "Polymultivalent" Polymer-Peptide Cluster Conjugates for an Enhanced Targeting of Cells Expressing αvβ3 Integrins. Bioconjugate Chemistry, 2017, 28(9), 2241–2245. doi: 10.1021/acs.bioconjchem.7b00362
  12. Luo, W.; Wen, G.; Yang, L.; Tang, J.; Wang, J.; Wang, J.; Zhang, S.; Zhang, L.; Ma, F.; Xiao, L.; Wang, Y.; Li, Y. Dual-targeted and pH-sensitive Doxorubicin Prodrug-Microbubble Complex with Ultrasound for Tumor Treatment. Theranostics, 2017, 7(2), 452–465
  13. Yang, X.; Wang, Z.; Zhang, F.; Zhu, G.; Song, J.; Teng, G.-J.; Niu, G.; Chen, X. Mapping Sentinel Lymph Node Metastasis by Dual-probe Optical Imaging. Theranostics, 2017, 7(1), 153–163. doi: 10.7150/thno.17085

Cyanine5.5 гидразид

  1. Machado, Y.; Duinkerken, S.; Hoepflinger, V.; Mayr, M.; Korotchenko, E.; Kurtaj, A.; Pablos, I.; Steiner, M.; Stoecklinger, A.; Lübbers, J.; Schmid, M.; Ritter, U.; Scheiblhofer, S.; Ablinger, M.; Wally, V.; Hochmann, S.; Raninger, A.M.; Strunk, D.; van Kooyk, Y.; Thalhamer, J.; Weiss, R. Synergistic effects of dendritic cell targeting and laser-microporation on enhancing epicutaneous skin vaccination efficacy. Journal of Controlled Release, 2017, 266, 87–99. doi: 10.1016/j.jconrel.2017.09.020
  2. Zhao, Y.; Wang, Y.; Ran, F.; Cui, Y.; Liu, C.; Zhao, Q.; Gao, Y.; Wang, D.; Wang, S. A comparison between sphere and rod nanoparticles regarding their in vivo biological behavior and pharmacokinetics. Scientific Reports, 2017, 7, 4131. doi: 10.1038/s41598-017-03834-2

Cyanine5.5 карбоновая кислота

  1. Zhao, C.; Liu, A.; Santamaria, C.M.; Shomorony, A.; Ji, T.; Wei, T.; Gordon, A.; Elofsson, H.; Mehta, M.; Yang, R.; Kohane, D.S. Polymer-tetrodotoxin conjugates to induce prolonged duration local anesthesia with minimal toxicity. Nature Communications, 2019, 10, 2566. doi: 10.1038/s41467-019-10296-9
  2. Ding, Y.; Liu, J.; Li, X.; Xu, L.; Li, C.; Ma, L.; Liu, J.; Ma, R.; An, Y.; Huang, F.; Liu, Y.; Shi, L. Rational design of drug delivery systems for potential programmable drug release and improved therapeutic effect. Materials Chemistry Frontiers, 2019, 3(6), 1159–1167. doi: 10.1039/c9qm00178f
  3. Islam, M.S.; Reineke, J.; Kaushik, R.S.; Woyengo, T.; Baride, A.; Alqahtani, M.S.; Perumal, O. Bioadhesive Food-Protein Nanoparticles as Pediatric Oral Drug Delivery system. ACS Applied Materials & Interfaces, 2019, 11(20), 18062–18073. doi: 10.1021/acsami.9b00152
  4. Yang, J.; Xu, J.; Gonzalez, R.; Lindner, T.; Kratochwil, C.; Miao, Y. 68Ga-DOTA-GGNle-CycMSHhex targets the melanocortin-1 receptor for melanoma imaging. Science Translational Medicine, 2018, 10(466), eaau4445. doi: 10.1126/scitranslmed.aau4445
  5. Zhang, L.; Yao, M.; Yan, W.; Liu, X.; Jiang, B.; Qian, Z.; Gao, Y.; Lu, X.-J.; Chen, X.; Wang, Q.-L. Delivery of a chemotherapeutic drug using novel hollow carbon spheres for esophageal cancer treatment. International Journal of Nanomedicine, 2017, 12, 6759–6769. doi: 10.2147/IJN.S142916
  6. Liu, M.; Richardson, R.R.; Mountford, S.J.; Zhang, L.; Tempone, M.H.; Herzog, H.; Holliday, N.D.; Thompson, P.E. Identification of a Cyanine-Dye Labelled Peptidic Ligand for Y1R and Y4R, based upon the Neuropeptide Y C-terminal analogue, BVD-15. Bioconjugate Chemistry, 2016, 27(9), 2166–2175. doi: 10.1021/acs.bioconjchem.6b00376
  7. Camerino, M.A.; Liu, M.; Moriya, S.; Kitahashi, T.; Mahgoub, A.; Mountford, S.J.; Chalmers, D.K.; Soga, T.; Parhar, I.S.; Thompson, P.E. Beta amino acid-modified and fluorescently labelled kisspeptin analogues with potent KISS1R activity. Journal of Peptide Science, 2016, 22(6), 406–414. doi: 10.1002/psc.2883
  8. Zhao, Y.; Fay, F.; Hak, S.; Manuel Perez-Aguilar, J.; Sanchez-Gaytan, B.L.; Goode, B.; Duivenvoorden, R.; de Lange Davies, C.; Bjørkøy, A.; Weinstein, H.; Fayad, Z.A.; Pérez-Medina, C.; Mulder, W.J.M. Augmenting drug-carrier compatibility improves tumour nanotherapy efficacy. Nature Communications, 2016, 7, 11221. doi: 10.1038/ncomms11221
  9. Kwok, S.J.J.; Choi, M.; Bhayana, B.; Zhang, X.; Ran, C.; Yun, S.-H. Two-photon excited photoconversion of cyanine-based dyes. Scientific Reports, 2016, 6, 23866. doi: 10.1038/srep23866
  10. Wang, X.; Wang, C.; Zhang, Q.; Cheng, Y. Near Infrared Light-responsive and Injectable Supramolecular Hydrogels for On-demand Drug Delivery. Chemical Communications, 2016, 52, 978–981. doi: 10.1039/c5cc08391e
  11. Kim, K.S.; Park, W.; Hu, J.; Bae, Y.H.; Na, K. A cancer-recognizable MRI contrast agents using pH-responsive polymeric micelle. Biomaterials, 2014, 35(1), 337-343. doi: 10.1016/j.biomaterials.2013.10.004
  12. Lee, B.-S.; Amano, T.; Wang, H.Q.; Pantoja, J.L.; Yoon, C.W.; Hanson, C.J.; Amatya, R.; Yen, A.; Black, K.L.; Yu, J.S. Reactive Oxygen Species Responsive Nanoprodrug to Treat Intracranial Glioblastoma. ACS Nano, 2013, 7(4), 3061-3077. doi: 10.1021/nn400347j

Cyanine5.5 малеимид

  1. Galstyan, A.; Chiechi, A.; Korman, A.J.; Sun, T.; Isreal, L.L.; Braubach, O.; Patil, R.; Shatalova, E.; Ljubimov, V.A.; Markman, J.; Grodzinski, Z.; Black, K.L.; Penichet, M.L.; Holler, E.; Ljubimov, A.V.; Ding, H.; Ljubimova, J.Y. Nano immunoconjugates crossing blood-brain barrier activate local brain tumor immune system for glioma treatment. bioRxiv, preprint. doi: 10.1101/466508
  2. Guo, S.; Xiao, X.; Wang, X.; Luo, Q.; Zhu, H.; Zhang, H.; Li, H.; Gong, Q.; Luo, K. Reductive microenvironment responsive gadolinium-based polymers as potential safe MRI contrast agents. Biomaterials Science, 2019, 7(5), 1919–1932. doi: 10.1039/c8bm01103f
  3. Vishnu Vardhan, G.P.; Hema, M.; Sushmitha, C.; Savithri, H.S.; Natraj, U.; Murthy, M.R.N. Development of sesbania mosaic virus nanoparticles for imaging. Archives of Virology, 2019, 164(2), 497–507. doi: 10.1007/s00705-018-4097-y
  4. Zhang, C.; Moonshi, S.S.; Wang, W.; Ta, H.T.; Han, Y.; Han, F.Y.; Peng, H.; Král, P.; Rolfe, B.E.; Gooding, J.J.; Gaus, K.; Whittaker, A.K. High F-Content Perfluoropolyether-Based Nanoparticles for Targeted Detection of Breast Cancer by 19F Magnetic Resonance and Optical Imaging. ACS Nano, 2018, 12(9), 9162–9176. doi: 10.1021/acsnano.8b03726
  5. Chung, S.W.; Choi, J.U.; Cho, Y.S.; Kim, H.R.; Won, T.H.; Dimitrion, P.; Jeon, O.-C.; Kim, S.W.; Kim, I.-S.; Kim, S.Y.; Byun, Y. Self-Triggered Apoptosis Enzyme Prodrug Therapy (STAEPT): Enhancing Targeted Therapies via Recurrent Bystander Killing Effect by Exploiting Caspase-Cleavable Linker. Advanced Science, 2018, 5(7), 1800368. doi: 10.1002/advs.201800368
  6. Cai, H.; Wang, X.; Zhang, H.; Sun, L.; Pan, D.; Gong, Q.; Gu, Z.; Luo, K. Enzyme-sensitive biodegradable and multifunctional polymeric conjugate as theranostic nanomedicine. Applied Materials Today, 2018, 11, 207–218. doi: 10.1016/j.apmt.2018.02.003
  7. Matsuoka, D.; Watanabe, H.; Shimizu, Y.; Kimura, H.; Yagi, Y.; Kawai, R.; Ono, M.; Saji, H. Structure–activity relationships of succinimidyl-Cys-C (O)-Glu derivatives with different near-infrared fluorophores as optical imaging probes for prostate-specific membrane antigen. Bioorganic & Medicinal Chemistry, 2018, 26(9), 2291–2301. doi: 10.1016/j.bmc.2018.03.015
  8. Zhang, C.; Moonshi, S.S.; Han, Y.; Puttick, S.; Peng, H.; Magoling, B.J.A.; Reid, J.C.; Bernardi, S.; Searles, D.J.; Král, P.; Whittaker, A.K. PFPE-Based Polymeric 19F MRI Agents: A New Class of Contrast Agents with Outstanding Sensitivity. Macromolecules, 2017, 50(15), 5953–5963. doi: 10.1021/acs.macromol.7b01285
  9. Masarapu, H.; Patel, B.K.; Chariou, P.L.; Hu, H.; Gulati, N.M.; Carpenter, B.L.; Ghiladi, R.A.; Shukla, S.; Steinmetz, N.F. Physalis Mottle Virus-Like Particles as Nanocarriers for Imaging Reagents and Drugs. Biomacromolecules, 2017, 18(12), 4141–4153. doi: 10.1021/acs.biomac.7b01196
  10. Wilks, M.Q.; Normandin, M.D.; Yuan, H.; Cho, H.; Guo, Y.; Herisson, F.; Ayata, C.; Wooten, D.W.; El Fakhri, G.; Josephson, L. Imaging PEG-Like Nanoprobes in Tumor, Transient Ischemia, and Inflammatory Disease Models. Bioconjugate Chemistry, 2015, 26(6), 1061–1069. doi: 10.1021/acs.bioconjchem.5b00213
  11. Cai, H.; Singh, A.N.; Sun, X.; Peng, F. Synthesis and Characterization of Her2-NLP Peptide Conjugates Targeting Circulating Breast Cancer Cells: Cellular Uptake and Localization by Fluorescent Microscopic Imaging. Journal of Fluorescence, 2015, 25(1), 113–117. doi: 10.1007/s10895-014-1486-9
  12. Graen, T.M.D.; Hoefling, M.; Grubmüller, H. AMBER-DYES: Characterization of Charge Fluctuations and Force Field Parameterization of Fluorescent Dyes for Molecular Dynamics Simulations. Journal of Chemical Theory and Computation, 2014, 10(12), 5505-5512. doi: 10.1021/ct500869p
  13. Park, S.; Kim, Y.-J.; Jon, S. A high-affinity peptide for nicotinic acetylcholine receptor-α1 and its potential use in pulmonary drug delivery. Journal of Controlled Release, 2014, 192, 141-147. doi: 10.1016/j.jconrel.2014.07.006
  14. Wang, X.; Yang, Y.; Jia, H.; Jia, W.; Miller, S.; Bowman, B.; Feng, J.; Zhan, F. Peptide decoration of nanovehicles to achieve active targeting and pathology-responsive cellular uptake for bone metastasis chemotherapy. Biomaterials Science, 2014, 2(7), 961-971. doi: 10.1039/c4bm00020j
  15. Fan, H.; Zhang, I.; Chen, X.; Zhang, L.; Wang, H.; Da Fonseca, A.; Manuel, E.R.; Diamond, D.J.; Raubitschek, A.; Badie, B. Intracerebral CpG Immunotherapy with Carbon Nanotubes Abrogates Growth of Subcutaneous Melanomas in Mice. Clinical Cancer Research, 2012, 18(20), 5628-5638. doi: 10.1158/1078-0432.ccr-12-1911
  16. Zhao, D.; Alizadeh, D.; Zhang, L.; Liu, W.; Farrukh, O.; Manuel, E.; Diamond, D.J.; Badie, B. Carbon Nanotubes Enhance CpG Uptake and Potentiate Antiglioma Immunity. Clinical Cancer Research, 2011, 17(4), 771–782. doi: 10.1158/1078-0432.ccr-10-2444

Cyanine7 азид

  1. Meka, R.R.; Venkatesha, S.H.; Moudgil, K.D. Peptide-directed liposomal delivery improves the therapeutic index of an immunomodulatory cytokine in controlling autoimmune arthritis. Journal of Controlled Release, 2018, 286, 279–288. doi: 10.1016/j.jconrel.2018.08.007
  2. Lyu, Z.; Kang, L.; Buuh, Z.Y.; Jiang, D.; McGuth, J.C.; Du, J.; Wissler, H.L.; Cai, W.; Wang, R.E. A Switchable Site-Specific Antibody Conjugate. ACS Chemical Biology, 2018, 13(4), 958–964. doi: 10.1021/acschembio.8b00107
  3. Maudens, P.; Seemayer, C.A.; Thauvin, C.; Gabay, C.; Jordan, O.; Allémann, E. Nanocrystal-Polymer Particles: Extended Delivery Carriers for Osteoarthritis Treatment. Small, 2018, 14(8), 1703108. doi: 10.1002/smll.201703108
  4. Morton, S.W.; Zhao, X.; Quadir, M.A.; Hammond, P.T. FRET-enabled biological characterization of polymeric micelles. Biomaterials, 2014, 35(11), 3489-3496. doi: 10.1016/j.biomaterials.2014.01.027

Cyanine7 активированный эфир

  1. Huang, C.; Zeng, T.; Li, J.; Tan, L.; Deng, X.; Pan, Y.; Chen, Q.; Li, A.; Hu, J. Folate Receptor-mediated Renal-targeting Nanoplatform for the Specific Delivery of Triptolide to Treat Renal Ischemia/Reperfusion Injury. ACS Biomaterials Science & Engineering, 2019, 5(6), 2877–2886. doi: 10.1021/acsbiomaterials.9b00119
  2. Dahanayake, V.; Pornrungroj, C.; Pablico-Lansigan, M.; Hickling, W.J.; Lyons, T.; Lah, D.; Lee, Y.-C.; Parasido, E.; Bertke, J.A.; Albanese, C.; Rodriguez, O.; Van Keuren, E.; Stoll, S.L. Paramagnetic Clusters of Mn3(O2CCH3)6(Bpy)2 in Polyacrylamide Nanobeads as a New Design Approach to T1-T2 Multi-Modal MRI Contrast Agent. ACS Applied Materials & Interfaces, 2019, 11(20), 18153–18164. doi: 10.1021/acsami.9b03216
  3. Crawford, B.M.; Strobbia, P.; Wang, H.-N.; Zentella, R.; Boyanov, M.; Odion, R.; Pei, Z.-M.; Sun, T.-P.; Kemner, K.M.; Vo-Dinh, T. In vivo nucleic acid detection and imaging within whole plants using plasmonic nanosensors. Advanced Environmental, Chemical, and Biological Sensing Technologies XV (Proceedings SPIE 11007), 2019, 11007, 1100708. doi: 10.1117/12.2524840
  4. Phillips, H.R.; Tolstyka, Z.P.; Hall, B.C.; Hexum, J.K.; Hackett, P.B.; Reineke, T.M. Glycopolycation-DNA Polyplex Formulation N/P Ratio Affects Stability, Hemocompatibility, and in Vivo Biodistribution. Biomacromolecules, 2019, 20(4), 1530–1544. doi: 10.1021/acs.biomac.8b01704
  5. Crawford, B.M.; Strobbia, P.; Wang, H.-N.; Zentella, R.; Boyanov, M.I.; Pei, Z.-M.; Sun, T.-P.; Kemner, K.M.; Vo-Dinh, T. Plasmonic nanoprobes for in vivo multimodal sensing and bioimaging of microRNA within plants. ACS Applied Materials & Interfaces, 2019, 11(8), 7743–7754. doi: 10.1021/acsami.8b19977
  6. Smith, W.J.; Wang, G.; Gaikwad, H.; Vu, V.P.; Groman, E.; Bourne, D.W.A.; Simberg, D. Accelerated Blood Clearance of Antibodies by Nanosized Click Antidotes. ACS Nano, 2018, 12(12), 12523–12532. doi: 10.1021/acsnano.8b07003
  7. Li, W.; Li, Y.; Liu, Z.; Kerdsakundee, N.; Zhang, M.; Zhang, F.; Liu, X.; Bauleth-Ramos, T.; Lian, W.; Mäkilä, E.; Kemell, M.; Ding, Y.; Sarmento, B.; Wiwattanapatapee, R.; Salonen, J.; Zhang, H.; Hirvonen, J.T.; Liu, D.; Deng, X.; Santos, H.A. Hierarchical structured and programmed vehicles deliver drugs locally to inflamed sites of intestine. Biomaterials, 2018, 185, 322–332. doi: 10.1016/j.biomaterials.2018.09.024
  8. Besford, Q.A.; Ju, Y.; Wang, T.-Y.; Yun, G.; Cherepanov, P.V.; Hagemeyer, C.E.; Cavalieri, F.; Caruso, F. Self-Assembled Metal-Phenolic Networks on Emulsions as Low-Fouling and pH-Responsive Particles. Small, 2018, 14(39), e1802342. doi: 10.1002/smll.201802342
  9. Etrych, T.; Daumová, L.; Pokorná, E.; Tušková, D.; Lidický, O.; Kolářová, V.; Pankrác, J.; Šefc, L.; Chytil, P.; Klener, P. Effective doxorubicin-based nano-therapeutics for simultaneous malignant lymphoma treatment and lymphoma growth imaging. Journal of Controlled Release, 2018, 289, 44–55. doi: 10.1016/j.jconrel.2018.09.018
  10. Bonnard, T.; Jayapadman, A.; Putri, J.A.; Cui, J.; Ju, Y.; Carmichael, C.; Angelovich, T.A.; Cody, S.H.; French, S.; Pascaud, K.; Pearce, H.A.; Jagdale, S.; Caruso, F.; Hagemeyer, C.E. Low-Fouling and Biodegradable Protein-Based Particles for Thrombus Imaging. ACS Nano, 2018, 12(7), 6988–6996. doi: 10.1021/acsnano.8b02588
  11. Moroz, P.; Jin, Z.; Sugiyama, Y.; Lara, D'A.; Razgoniaeva, N.; Yang, M.; Kholmicheva, N.; Khon, D.; Mattoussi, H.; Zamkov, M. The Competition of Charge and Energy Transfer Processes in Donor-Acceptor Fluorescence Pairs: Calibrating the Spectroscopic Ruler. ACS Nano, 2018, 12(6), 5657–5665. doi: 10.1021/acsnano.8b01451
  12. Gusliakova, O.; Atochina-Vasserman, E.N.; Sindeeva, O.; Sindeev, S.; Pinyaev, S.; Pyataev, N.; Revin, V.; Sukhorukov, G.B.; Gorin, D.; Gow, A.J. Use of Submicron Vaterite Particles Serves as an Effective Delivery Vehicle to the Respiratory Portion of the Lung. Frontiers in Pharmacology, 2018, 9, 559. doi: 10.3389/fphar.2018.00559
  13. Ashwanikumar, N.; Plaut, J.S.; Mostofian, B.; Patel, S.; Kwak, P.; Sun, C.; McPhail, K.; Zuckerman, D.M.; Esener, S.C.; Sahay, G. Supramolecular self assembly of nanodrill-like structures for intracellular delivery. Journal of Controlled Release, 2018, 282, 76–89. doi: 10.1016/j.jconrel.2018.02.041
  14. Zhang, X.; He, F.; Xiang, K.; Zhang, J.; Xu, M.; Long, P.; Su, H.; Gan, Z.; Yu, Q. CD44-targeted Facile Enzymatic Activatable Chitosan Nanoparticles for Efficient Antitumor Therapy and Reversal of Multidrug Resistance. Biomacromolecules, 2018, 19(3), 883–895. doi: 10.1021/acs.biomac.7b01676
  15. Tal, N.; Rudnick-Glick, S.; Grinberg, I.; Natan, M.; Banin, E.; Margel, S. Engineering of a New Bisphosphonate Monomer and Nanoparticles of Narrow Size Distribution for Antibacterial Applications. ACS Omega, 2018, 3(2), 1458–1469. doi: 10.1021/acsomega.7b01686
  16. Newman, M.R.; Russell, S.G.; Schmitt, C.S.; Marozas, I.A.; Sheu, T.-J.; Puzas, J.E.; Benoit, D.S.W. Multivalent Presentation of Peptide Targeting Groups Alters Polymer Biodistribution to Target Tissues. Biomacromolecules, 2018, 19(1), 71–84. doi: 10.1021/acs.biomac.7b01193
  17. Suleimanov, I.; Gabor, M.; Lionel, S.; Bousseksou, A. Near-infrared luminescence switching in a spin-crossover polymer nanocomposite. European Journal of Inorganic Chemistry, 2017, 28, 3446–3451. doi: 10.1002/ejic.201700426
  18. Wang, Y.; Malcolm, D.W.; Benoit, D.S.W. Controlled and sustained delivery of siRNA/NPs from hydrogels expedites bone fracture healing. Biomaterials, 2017, 139, 127–138. doi: 10.1016/j.biomaterials.2017.06.001
  19. Zhang, R.; Yang, J.; Radford, D.C.; Fang, Y.; Kopeček, J. FRET Imaging of Enzyme-Responsive HPMA Copolymer Conjugate. Macromolecular Bioscience, 2017, 17(1), 1600125. doi: 10.1002/mabi.201600125
  20. Shen, T.; Xu, X.; Guo, L.; Tang, H.; Diao, T.; Gan, Z.; Zhang, G.; Yu, Q. Efficient Tumor Accumulation, Penetration and Tumor Growth Inhibition Achieved by Polymer Therapeutics: The Effect of Polymer Architectures. Biomacromolecules, 2017, 18(1), 217–230. doi: 10.1021/acs.biomac.6b01533
  21. Kilic, E.; Novoselova, M.V.; Lim, S.H.; Pyataev, N.A.; Pinyaev, S.I.; Kulikov, O.A.; Sindeeva, O.A.; Mayorova, O.A.; Murney, R.; Antipina, M.N.; Haigh, B.; Sukhorukov, G.B.; Kiryukhin, M.V. Formulation for Oral Delivery of Lactoferrin Based on Bovine Serum Albumin and Tannic Acid Multilayer Microcapsules. Scientific Reports, 2017, 7, 44159. doi: 10.1038/srep44159
  22. Beldman, T.J.; Senders, M.L.; Alaarg, A.; Perez-Medina, C.; Tang, J.; Zhao, Y.; Fay, F.; Deichmöller, J.; Born, B.; Desclos, E.; van der Wel, N.N.; Hoebe, R.A.; Kohen, F.; Kartvelishvily, E.; Neeman, M.; Reiner, T.; Calcagno, C.; Fayad, Z.A.; de Winther, M.P.J.; Lutgens, E.; Mulder, W.J.M.; Kluza, E. Hyaluronan Nanoparticles Selectively Target Plaque-Associated Macrophages and Improve Plaque Stability in Atherosclerosis. ACS Nano, 2017, 11(6), 5785–5799. doi: 10.1021/acsnano.7b01385
  23. Rudnick-Glick, S.; Corem-Salkmon, E.; Grinberg, I.; Margel, S. Targeted drug delivery of near IR fluorescent doxorubicin-conjugated poly(ethylene glycol) bisphosphonate nanoparticles for diagnosis and therapy of primary and metastatic bone cancer in a mouse model. Journal of Nanobiotechnology, 2016, 14, 80. doi: 10.1186/s12951-016-0233-6
  24. Xu, X.; Xu, Z.; Liu, J.; Zhang, Z.; Chen, H.; Li, X.; Shi, S. Visual tracing of diffusion and biodistribution for amphiphilic cationic nanoparticles using photoacoustic imaging after ex vivo intravitreal injections. International Journal of Nanomedicine, 2016, 11, 5079–5086. doi: 10.2147/IJN.S109986
  25. Gera, L.; Charest-Morin, X.; Jean, M.; Bachelard, H.; Marceau, F. Infrared-emitting, peptidase-resistant fluorescent ligands of the bradykinin B2 receptor: application to cytofluorometry and imaging. BMC Research Notes, 2016, 9, 452. doi: 10.1186/s13104-016-2258-1
  26. Zhao, L.; Ma, S.; Pan, Y.; Zhang, Q.; Wang, K.; Song, D.; Wang, X.; Feng, G.; Liu, R.; Xu, H.; Zhang, J.; Qiao, M.; Kong, D. Functional Modification of Fibrous PCL Scaffolds with Fusion Protein VEGF-HGFI Enhanced Cellularization and Vascularization. Advanced Healthcare Materials, 2016, 5(18), 2376–2385. doi: 10.1002/adhm.201600226
  27. Sui, B.; Zhong, G.; Sun, J. Drug-loadable Mesoporous Bioactive Glass Nanospheres: Biodistribution, Clearance, BRL Cellular Location and Systemic Risk Assessment via 45Ca Labelling and Histological Analysis. Scientific Reports, 2016, 6, 33443. doi: 10.1038/srep33443
  28. Su, S.; Wang, J.; Vargas, E.; Wei, J.; Martinez-Zaguilan, R.; Sennoune, S.R.; Pantoya, M.L.; Wang, S.; Chaudhuri, J.; Qiu, J. Porphyrin Immobilized Nano-Graphene Oxide for Enhanced and Targeted Photothermal Therapy of Brain Cancer. ACS Biomaterials Science & Engineering, 2016, 2(8), 1357–1366. doi: 10.1021/acsbiomaterials.6b00290
  29. Zhang, L.; Navaratna, T.; Thurber, G.M. A Helix-Stabilizing Linker Improves Subcutaneous Bioavailability of a Helical Peptide Independent of Linker Lipophilicity , 2016, 27(7), 1663–1672. doi: 10.1021/acs.bioconjchem.6b00209
  30. Pérez-Medina, C.; Abdel-Atti, D.; Tang, J.; Zhao, Y.; Fayad, Z.A.; Lewis, J.S.; Mulder, W.J.M.; Reiner, T. Nanoreporter PET predicts the efficacy of anti-cancer nanotherapy. Nature Communications, 2016, 7, 11838. doi: 10.1038/ncomms11838
  31. Zhao, Y.; Fay, F.; Hak, S.; Manuel Perez-Aguilar, J.; Sanchez-Gaytan, B.L.; Goode, B.; Duivenvoorden, R.; de Lange Davies, C.; Bjørkøy, A.; Weinstein, H.; Fayad, Z.A.; Pérez-Medina, C.; Mulder, W.J.M. Augmenting drug-carrier compatibility improves tumour nanotherapy efficacy. Nature Communications, 2016, 7, 11221. doi: 10.1038/ncomms11221
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  33. Kim, J.B.; Park, K.; Ryu, Ji.; Lee, J.J.; Lee, M.W.; Cho, H.S.; Nam, H.S.; Park, O.K.; Song, J.W.; Kim, T.S.; Oh, D.J.; Gweon, D.; Oh, W.-Y.; Yoo, H.; Kim, J.W. Intravascular optical imaging of high-risk plaques in vivo by targeting macrophage mannose receptors. Scientific Reports, 2016, 6, 22608. doi: 10.1038/srep22608
  34. Tolstyka, Z.P.; Phillips, H.; Cortez, M.; Wu, Y.; Ingle, N.; Bell, J.B.; Hackett, P.B.; Reineke, T.M. Trehalose-Based Block Copolycations Promote Polyplex Stabilization for Lyophilization and in Vivo pDNA Delivery. ACS Biomaterials Science & Engineering, 2016, 2(1), 43–55. doi: 10.1021/acsbiomaterials.5b00312
  35. Turcheniuk, K.; Dumych, T.; Bilyy, R.; Turcheniuk, V.; Bouckaert, J.; Vovk, V.; Chopyak, V.; Zaitsev, V.; Mariot, P.; Prevarskaya, N.; Boukherrouba, R.; Szunerits, S. Plasmonic photothermal cancer therapy with gold nanorods/reduced graphene oxide core/shell nanocomposites. RSC Advances, 2016, 6(2), 1600–1610. doi: 10.1039/c5ra24662h
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  41. Shi, Y.; van der Meel, R.; Theek, B.; Oude Blenke, E.; Pieters, E.H.E.; Fens, M.H.A.M.; Ehling, J.; Schiffelers, R.M.; Storm, G.; van Nostrum, C.F.; Lammers, T.; Hennink, W.E. Complete Regression of Xenograft Tumors upon Targeted Delivery of Paclitaxel via Π–Π Stacking Stabilized Polymeric Micelles. ACS Nano, 2015, 9(4), 3740–3752. doi: 10.1021/acsnano.5b00929
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  45. Graen, T.M.D.; Hoefling, M.; Grubmüller, H. AMBER-DYES: Characterization of Charge Fluctuations and Force Field Parameterization of Fluorescent Dyes for Molecular Dynamics Simulations. Journal of Chemical Theory and Computation, 2014, 10(12), 5505-5512. doi: 10.1021/ct500869p
  46. Lin, X.; Zhu, H.; Luo, Z.; Hong, Y.; Zhang, H.; Liu, X.; Ding, H.; Tian, H.; Yang, Z. Near-Infrared Fluorescence Imaging of Non-Hodgkin's Lymphoma CD20 Expression Using Cy7-Conjugated Obinutuzumab. Molecular Imaging and Biology, 2014. doi: 10.1007/s11307-014-0742-3
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Cyanine7 алкин

  1. Tang, H.; Zhang, J.; Tang, J.; Shen, Y.; Guo, W.; Zhou, M.; Wang, R.; Jiang, N.; Gan, Z.; Yu, Q. Tumor specific and renal excretable star-like tri-block polymer-doxorubicin conjugates for safe and efficient anticancer therapy. Biomacromolecules, 2018, 19(7), 2849–2862. doi: 10.1021/acs.biomac.8b00425
  2. Smith, A.A.A.; Zuwala, K.; Pilgram, O.; Johansen, K.S.; Tolstrup, M.; Dagnæs-Hansen, F.; Zelikin, A.N. Albumin-Polymer-Drug Conjugates: Long Circulating, High Payload Drug Delivery Vehicles. ACS Macro Letters, 2016, 5, 1089–1094. doi: 10.1021/acsmacrolett.6b00544
  3. Zhang, L.; Thurber, G.M. Quantitative Impact of Plasma Clearance and Down-regulation on GLP-1 Receptor Molecular Imaging. Molecular Imaging and Biology, 2016, 18(1), 79–89. doi: 10.1007/s11307-015-0880-2

Cyanine7 амин

  1. Pola, R.; Parnica, J.; Zuska, K.; Böhmová, E.; Filipová, M.; Pechar, M.; Pankrác, J.; Mucksová, J.; Trefil, P.; Kalina, J.; Šefc, L.; Větvička, D.; Poučková, P.; Bouček, J.; Janoušková, O.; Etrych, T. Oligopeptide-targeted polymer nanoprobes for fluorescence-guided endoscopic surgery. Multifunctional Materials, in press. doi: 10.1088/2399-7532/ab159e
  2. Nuhn, L.; De Koker, S.; Van Lint, S.; Zhong, Z.; Catani, J.P.; Combes, F.; Deswarte, K.; Li, Y.; Lambrecht, B.N.; Lienenklaus, S.; Sanders, N.N.; David, S.A.; Tavernier, J.; De Geest, B.G. Nanoparticle-Conjugate TLR7/8 Agonist Localized Immunotherapy Provokes Safe Antitumoral Responses. Advanced Materials, 2018, 30(45), e1803397. doi: 10.1002/adma.201803397
  3. Joo, J.; Poon, C.; Yoo, S.P.; Chung, E.J. Shape Effects of Peptide Amphiphile Micelles for Targeting Monocytes. Molecules, 2018, 23(11), 2786. doi: 10.3390/molecules23112786
  4. Melgar-Asensio, I.; Kandela, I.; Aird, F.; Darjatmoko, S.R.; de Los Rios, C.; Sorenson, C.M.; Albert, D.M.; Sheibani, N.; Henkin, J. Extended Intravitreal Rabbit Eye Residence of Nanoparticles Conjugated With Cationic Arginine Peptides for Intraocular Drug Delivery: In Vivo Imaging. Investigative Ophthalmology & Visual Science, 2018, 59(10), 4071–4081. doi: 10.1167/iovs.18-24087
  5. Segura-Ibarra, V.; Cara, F.E.; Wu, S.; Iruegas-Nunez, D.A.; Wang, S.; Ferrari, M.; Ziemys, A.; Valderrabano, M.; Blanco, E. Nanoparticles administered intrapericardially enhance payload myocardial distribution and retention. Journal of Controlled Release, 2017, 262, 18–27. doi: 10.1016/j.jconrel.2017.07.012
  6. Cheng, L.; Ji, K.; Shih, T. Y.; Haddad, A.; Giatsidis, G.; Mooney, D.J.; Orgill, D.P.; Nabzdyk, C.S. Injectable Shape-Memorizing Three-Dimensional Hyaluronic Acid Cryogels for Skin Sculpting and Soft Tissue Reconstruction. Tissue Engineering Part A, 2017, 23(5–6), 243–251. doi: 10.1089/ten.tea.2016.0263

Cyanine7 карбоновая кислота

  1. Svenskaya, Y.I.; Genina, E.A.; Parakhonskiy, B.V.; Lengert, E.; Talnikova, E.E.; Terentyuk, G.S.; Utz, S.R.; Gorin, D.A.; Tuchin, V.V.; Sukhorukov, G. A simple non-invasive approach towards efficient transdermal drug delivery based on biodegradable particulate system. ACS Applied Materials & Interfaces, 2019, 11(19), 17270–17282. doi: 10.1021/acsami.9b04305
  2. Yang, C.; Liu, D.; Renny, A.; Kuttipillai, P.S.; Lunt, R.R. Integration of near-infrared harvesting transparent luminescent solar concentrators onto arbitrary surfaces. Journal of Luminescence, 2019, 210, 239–246. doi: 10.1016/j.jlumin.2019.02.042
  3. Luthman, A.S. Wide-Field fHSI with a Linescan SRDA. In: Spectrally Resolved Detector Arrays for Multiplexed Biomedical Fluorescence Imaging (Springer Thesis), 2018, 51–85. doi: 10.1007/978-3-319-98255-7_3
  4. Luthman, A.S.; Dumitru, S.; Quiros-Gonzalez, I.; Joseph, J.; Bohndiek, S.E. Fluorescence hyperspectral imaging (fHSI) using a spectrally resolved detector array. Journal of Biophotonics, 2017, 10(6–7), 840–853. doi: 10.1002/jbio.201600304
  5. Zhao, Y.; Fay, F.; Hak, S.; Manuel Perez-Aguilar, J.; Sanchez-Gaytan, B.L.; Goode, B.; Duivenvoorden, R.; de Lange Davies, C.; Bjørkøy, A.; Weinstein, H.; Fayad, Z.A.; Pérez-Medina, C.; Mulder, W.J.M. Augmenting drug-carrier compatibility improves tumour nanotherapy efficacy. Nature Communications, 2016, 7, 11221. doi: 10.1038/ncomms11221
  6. Ma, X.; Cheng, Z.; Jin, Y.; Liang, X.; Yang, X.; Dai, Z.; Tian, J. SM5-1-Conjugated PLA nanoparticles loaded with 5-fluorouracil for targeted hepatocellular carcinoma imaging and therapy. Biomaterials, 2014, 35(9), 2878-2889. doi: 10.1016/j.biomaterials.2013.12.045

Cyanine7 малеимид

  1. Melgar-Asensio, I.; Kandela, I.; Aird, F.; Darjatmoko, S.R.; de Los Rios, C.; Sorenson, C.M.; Albert, D.M.; Sheibani, N.; Henkin, J. Extended Intravitreal Rabbit Eye Residence of Nanoparticles Conjugated With Cationic Arginine Peptides for Intraocular Drug Delivery: In Vivo Imaging. Investigative Ophthalmology & Visual Science, 2018, 59(10), 4071–4081. doi: 10.1167/iovs.18-24087
  2. Matsuoka, D.; Watanabe, H.; Shimizu, Y.; Kimura, H.; Yagi, Y.; Kawai, R.; Ono, M.; Saji, H. Structure–activity relationships of succinimidyl-Cys-C (O)-Glu derivatives with different near-infrared fluorophores as optical imaging probes for prostate-specific membrane antigen. Bioorganic & Medicinal Chemistry, 2018, 26(9), 2291–2301. doi: 10.1016/j.bmc.2018.03.015
  3. Tondera, C.; Wieduwild, R.; Röder, E.; Werner, C.; Zhang, Y.; Pietzsch, J. In Vivo Examination of an Injectable Hydrogel System Crosslinked by Peptide-Oligosaccharide Interaction in Immunocompetent Nude Mice. In Vivo Examination of an Injectable Hydrogel System Crosslinked by Peptide-Oligosaccharide Interaction in Immunocompetent Nude Mice, 2017, 27(15), 1605189. doi: 10.1002/adfm.201605189
  4. Wang, T.; Tang, Y.; He, X.; Yan, J.; Wang, C.; Feng, X. Self-Assembled Raspberry-Like Core/Satellite Nanoparticles for Anti-Inflammatory Protein Delivery. ACS Applied Materials & Interfaces, 2017, 9(8), 6902–6907. doi: 10.1021/acsami.6b16277
  5. Schwarz, B.; Madden, P.; Avera, J.; Gordon, B.; Larson, K.; Miettinen, H.; Uchida, M.; LaFrance, B.; Basu, G.; Rynda-Apple, A.; Douglas, T. Symmetry Controlled, Genetic Presentation of Bio-Active Proteins on the P22 Virus-Like Particle Using an External Decoration Protein. ACS Nano, 2015, 9(9), 9134–9147. doi: 10.1021/acsnano.5b03360

Cyanine7.5 азид

  1. Kong, J.-N.; Zhu, Z.; Itokazu, Y.; Wang, G.; Dinkins, M.B.; Zhong, L.; Lin, H.-P.; Elsherbini, A.; Leanhart, S.; Jiang, X.; Qin, H.; Zhi, W.; Spassieva, S.D.; Bieberich, E. Novel function of ceramide for regulation of mitochondrial ATP release in astrocytes. Journal of Lipid Research, 2018, 59(3), 488–506. doi: 10.1194/jlr.M081877
  2. van der Steen, S.C.H.A.; Raavé, R.; Langerak, S.; van Houdt, L.; van Duijnhoven, S.M.J.; van Lith, S.A.M.; Massuger, L.F.A.G.; Daamen, W.F.; Leenders, W.P.; van Kuppevelt, T.H. Targeting the extracellular matrix of ovarian cancer using functionalized, drug loaded lyophilisomes. European Journal of Pharmaceutics and Biopharmaceutics, 2017, 113, 229–239. doi: 10.1016/j.ejpb.2016.12.010
  3. Junker, M.; Rapoport, T.A. Involvement of VAT-1 in phosphatidylserine transfer from the endoplasmic reticulum to mitochondria. Traffic, 2015, 16(12), 1306–1317. doi: 10.1111/tra.12336

Cyanine7.5 активированный эфир

  1. Vinciguerra, D.; Degrassi, A.; Mancini, L.; Mura, S.; Mougin, J.; Couvreur, P.; Nicolas, J. Drug-Initiated Synthesis of Heterotelechelic Polymer Prodrug Nanoparticles for in Vivo Imaging and Cancer Cell Targeting. Biomacromolecules, in press. doi: 10.1021/acs.biomac.9b00148
  2. Qi, T.; Chen, B.; Wang, Z.; Du, H.; Liu, D.; Yin, Q.; Liu, B.; Zhang, Q.; Wang, Y. A pH-Activatable nanoparticle for dual-stage precisely mitochondria-targeted photodynamic anticancer therapy. Biomaterials, 2019, 213, 119219. doi: 10.1016/j.biomaterials.2019.05.030
  3. Mo, Y.; Du, H.; Chen, B.; Liu, D.; Yin, Q.; Yan, Y.; Wang, Z.; Wan, F.; Qi, T.; Wang, Y.; Zhang, Q.; Wang, Y. Quick-Responsive Polymer-Based Thermo-Sensitive Liposomes for Controlled Doxorubicin Release and Chemotherapy. ACS Biomaterials Science & Engineering, 2019, 5(5), 2316–2329. doi: 10.1021/acsbiomaterials.9b00343
  4. He, Z.; Hu, Y.; Gui, Z.; Zhou, Y.; Nie, T.; Zhu, J.; Liu, Z.; Chen, K.; Liu, L.; Leong, K.W.; Cao, P.; Chen, Y.; Mao, H.-Q. Sustained release of exendin-4 from tannic acid/Fe (III) nanoparticles prolongs blood glycemic control in a mouse model of type II diabetes. Journal of Controlled Release, 2019, 301, 119–128. doi: 10.1016/j.jconrel.2019.03.014
  5. Näkki, S.; Wang, J.T.-W.; Wu, J.; Fan, L.; Rantanen, J.; Nissinen, T.; Kettunen, M.I.; Backholm, M.; Ras, R.H.A.; Al-Jamal, K.T.; Lehto, V.-P.; Xu, W. Designed inorganic porous nanovector with controlled release and MRI features for safe administration of doxorubicin. International Journal of Pharmaceutics, 2019, 554, 327–336. doi: 10.1016/j.ijpharm.2018.10.074
  6. Xu, H.; Bandari, R.; Lee, L.E.; Li, R.; Yu, P.; Smith, C.J.; Ma, L. Design, Synthesis, and In Vitro and In Vivo Evaluation of High Affinity and Specificity Near-Infrared Fluorescent Bombesin Antagonists for Tumor Imaging. Journal of Medicinal Chemistry, 2018, 61(17), 7657–7670. doi: 10.1021/acs.jmedchem.8b00614
  7. Jones, J.E.; Busi, S.B.; Mitchem, J.B.; Amos-Landgraf, J.M.; Lewis, M.R. Evaluation of a Tumor-Targeting, Near-Infrared Fluorescent Peptide for Early Detection and Endoscopic Resection of Polyps in a Rat Model of Colorectal Cancer. Molecular Imaging, 2018, 17, 1536012118790065. doi: 10.1177/1536012118790065
  8. He, S.; Li, C.; Zhang, Q.; Ding, J.; Liang, X.-J.; Chen, X.; Xiao, H.; Chen, X.; Zhou, D.; Huang, Y. Tailoring Platinum(IV) Amphiphiles for Self-Targeting All-in-One Assemblies as Precise Multimodal Theranostic Nanomedicine. ACS Nano, 2018, 12(7), 7272–7281. doi: 10.1021/acsnano.8b03476
  9. Xue, F.; Wang, Y.; Zhang, Q.; Han, S.; Zhang, F.; Jin, T.; Li, C.; Hu, H.; Zhang, J. Self-assembly of affinity-controlled nanoparticles via host-guest interactions for drug delivery. Nanoscale, 2018, 10(26), 12364–12377. doi: 10.1039/C8NR01518J
  10. Li, H.; Li, K.; Dai, Y.; Xu, X.; Cao, X.; Zeng, Q.; He, H.; Pang, L.; Liang, J.; Chen, X.; Zhan, Y. In vivo near infrared fluorescence imaging and dynamic quantification of pancreatic metastatic tumors using folic acid conjugated biodegradable mesoporous silica nanoparticles. Nanomedicine: Nanotechnology, Biology and Medicine, 2018, 14(6), 1867–1877. doi: 10.1016/j.nano.2018.04.018
  11. Malhotra, M.; Sekar, T.V.; Ananta, J.S.; Devulapally, R.; Afjei, R.; Babikir, H.A.; Paulmurugan, R.; Massoud, T.F. Targeted nanoparticle delivery of therapeutic antisense microRNAs presensitizes glioblastoma cells to lower effective doses of temozolomide in vitro and in a mouse model. Oncotarget, 2018, 9(30), 21478–21494. doi: 10.18632/oncotarget.25135
  12. Shi, F.; Li, M.; Wang, J.; Wu, D.; Pan, M.; Guo, M.; Dou, J. Induction of multiple myeloma cancer stem cell apoptosis using conjugated anti-ABCG2 antibody with epirubicin-loaded microbubbles. Stem Cell Research & Therapy, 2018, 9, 144. doi: 10.1186/s13287-018-0885-2
  13. Loebel, C.; Rodell, C.B.; Chen, M.H.; Burdick, J.A. Shear-thinning and self-healing hydrogels as injectable therapeutics and for 3D-printing. Nature Protocols, 2017, 12(8), 1521–1541. doi: 10.1038/nprot.2017.053
  14. O'Mary, H.L.; Aldayel, A.M.; Valdes, S.A.; Naguib, Y.W.; Li, X.; Salvady, K.; Cui, Z. Acid-sensitive sheddable PEGylated, mannose-modified nanoparticles increase the delivery of betamethasone to chronic inflammation sites in a mouse model. Molecular Pharmaceutics, 2017, 14(6), 1929–1937. doi: 10.1021/acs.molpharmaceut.7b00024
  15. Sivak, L.; Subr, V.; Tomala, J.; Rihova, B.; Strohalm, J.; Etrych, T.; Kovar, M. Overcoming multidrug resistance via simultaneous delivery of cytostatic drug and P-glycoprotein inhibitor to cancer cells by HPMA copolymer conjugate. Biomaterials, 2017, 115, 65–80. doi: 10.1016/j.biomaterials.2016.11.013
  16. Lin, S.; Shah, A.; Hernández-Gil, J.; Stanziola, A.; Harriss, B.I.; Matsunaga, T.O.; Long, N.; Bamber, J.; Tang, M.-X. Optically and acoustically triggerable sub-micron phase-change contrast agents for enhanced photoacoustic and ultrasound imaging. Photoacoustics, 2017, 6, 26–36. doi: 10.1016/j.pacs.2017.04.001
  17. Cheng, J.; Feng, S.; Han, S.; Zhang, X.; Chen, Y.; Zhou, X.; Wang, R.; Li, X.; Hu, H.; Zhang, J. Facile Assembly of Cost-Effective and Locally Applicable or Injectable Nanohemostats for Hemorrhage Control. ACS Nano, 2016, 10(11), 9957&ndash9973. doi: 10.1021/acsnano.6b04124
  18. Zhang, Q.; Tao, H.; Lin, Y.; Hu, Y.; An, H.; Zhang, D.; Feng, S.; Hu, H.; Wang, R.; Li, X.; Zhang, J. A superoxide dismutase/catalase mimetic nanomedicine for targeted therapy of inflammatory bowel disease. Biomaterials, 2016, 105, 206–221. doi: 10.1016/j.biomaterials.2016.08.010
  19. Feng, S.; Hu, Y.; Peng, S.; Han, S.; Tao, H.; Zhang, Q.; Xu, X.; Zhang, J.; Hu, H. Nanoparticles responsive to the inflammatory microenvironment for targeted treatment of arterial restenosis. Biomaterials, 2016, 105, 167–184. doi: 10.1016/j.biomaterials.2016.08.003
  20. Dou, Y.; Guo, J.; Chen, Y.; Han, S.; Xu, X.; Shi, Q.; Jia, Y.; Liu, Y.; Deng, Y.; Wang, R.; Li, X.; Zhang, J. Sustained delivery by a cyclodextrin material-based nanocarrier potentiates antiatherosclerotic activity of rapamycin via selectively inhibiting mTORC1 in mice. Journal of Controlled Release, 2016, 235, 48–62. doi: 10.1016/j.jconrel.2016.05.049
  21. Markovic, S.; Belz, J.; Kumar, R.; Cormack, R.A.; Sridhar, S.; Niedre, M. Near-infrared fluorescence imaging platform for quantifying in vivo nanoparticle diffusion from drug loaded implants. International Journal of Nanomedicine, 2016, 11, 1213–1223. doi: 10.2147/IJN.S93324
  22. Zhang, Z.; Cai, H.; Liu, Z.; Yao, P. Effective Enhancement of Hypoglycemic Effect of Insulin by Liver-targeted Nanoparticles Containing Cholic Acid-modified Chitosan Derivative. Molecular Pharmaceutics, 2016, 13(7), 2433–2442. doi: 10.1021/acs.molpharmaceut.6b00188
  23. Han, F.Y.; Thurecht, K.J.; Lam, A.-L.; Whittaker, A.K.; Smith, M.T. Novel Polymeric Bioerodable Microparticles for Prolonged-Release Intrathecal Delivery of Analgesic Agents for Relief of Intractable Cancer-Related Pain. Journal of Pharmaceutical Sciences, 2015, 104(7), 2334–2344. doi: 10.1002/jps.24497
  24. Duong, H.T.T.; Dong, Z.; Su, L; Boyer, C.; George, J.; Davis, T.P.; Wang, J. The Use of Nanoparticles to Deliver Nitric Oxide to Hepatic Stellate Cells for Treating Liver Fibrosis and Portal Hypertension. Small, 2015, 11(19), 2291–2304. doi: 10.1002/smll.201402870
  25. Chen, K.; Xu, X.; Guo, J.W.; Zhang, X.; Han, S.; Wang, R.; Li, X.; Zhang, J. Enhanced Intracellular Delivery and Tissue Retention of Nanoparticles by Mussel-Inspired Surface Chemistry. Biomacromolecules, 2015, 16(11), 3574–3583. doi: 10.1021/acs.biomac.5b01056
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Cyanine7.5 алкин

  1. Chan, P.S.; Xian, J.W.; Li, Q.; Chan, C.W.; Leung, S.S.Y.; To, K.K.W. Biodegradable Thermosensitive PLGA-PEG-PLGA Polymer for Non-irritating and Sustained Ophthalmic Drug Delivery. AAPS Journal, 2019, 21, 59. doi: 10.1208/s12248-019-0326-x

Cyanine7.5 амин

  1. Hauser-Kawaguchi, A.; Milne, M.; Li, F.; Lee, T.Y.; Luyt, L.G. The development of a near infrared inulin optical probe for measuring glomerular filtration rate. International Journal of Biological Macromolecules, 2019, 123, 255–260. doi: 10.1016/j.ijbiomac.2018.11.034
  2. Li, Y.; Xiao, Y.; Lin, H.-P.; Reichel, D.; Bae, Y.; Lee, E.Y.; Jiang, Y.; Huang, X.; Yang, C.; Wang, Z. In vivo β-catenin attenuation by the integrin α5-targeting nano-delivery strategy suppresses triple negative breast cancer stemness and metastasis. Biomaterials, 2019, 188, 160–172. doi: 10.1016/j.biomaterials.2018.10.019
  3. Gurnani, Pratik and Sanchez-Cano, C.; Abraham, K.; Xandri-Monje, H.; Cook, A.B.; Hartlieb, M.; Lévi, F.; Dallmann, R.; Perrier, S. RAFT Emulsion Polymerization as a Platform to Generate Well-Defined Biocompatible Latex Nanoparticles. Macromolecular Bioscience, 2018, 18(10), e1800213. doi: 10.1002/mabi.201800213
  4. Tabe, H.; Sukenobe, K.; Kondo, T.; Sakurai, A.; Maruo, M.; Shimauchi, A.; Hirano, M.; Uno, S.-N.; Kamiya, M.; Urano, Y.; Matsushita, M.; Fujiyoshi, S. Cryogenic Fluorescence Localization Microscopy of Spectrally Selected Individual FRET Pairs in a Water Matrix. The Journal of Physical Chemistry B, 2018, 122(27), 6906–6911. doi: 10.1021/acs.jpcb.8b03977
  5. Souchek, J.J.; Wojtynek, N.E.; Payne, W.M.; Holmes, M.B.; Dutta, S.; Qi, B.; Datta, K.; LaGrange, C.A.; Mohs, A.M. Hyaluronic acid formulation of near infrared fluorophores optimizes surgical imaging in a prostate tumor xenograft. Acta Biomaterialia, 2018, 75, 323–333. doi: 10.1016/j.actbio.2018.06.016
  6. Mondal, G.; Almawash, S.; Chaudhary, A.K.; Mahato, R.I. EGFR-Targeted Cationic Polymeric Mixed Micelles for Co-delivery of Gemcitabine and miR-205 for treating Advanced Pancreatic Cancer. Molecular Pharmaceutics, 2017, 14(9), 3121–3133. doi: 10.1021/acs.molpharmaceut.7b00355
  7. Payne, W.M.; Hill, T.K.; Svechkarev, D.; Holmes, M.B.; Sajja, B.R.; Mohs, A.M. Multimodal Imaging Nanoparticles Derived from Hyaluronic Acid for Integrated Preoperative and Intraoperative Cancer Imaging. Contrast Media & Molecular Imaging, 2017, 2017, Article ID 9616791. doi: 10.1155/2017/9616791
  8. Ta, H.T.; Li, Z.; Hagemeyer, C.E.; Cowin, G.; Zhang, S.; Palasubramaniam, J.; Alt, K.; Wang, X.; Peter, K.; Whittaker, A.K. Molecular imaging of activated platelets via antibody-targeted ultra-small iron oxide nanoparticles displaying unique dual MRI contrast. Biomaterials, 2017, 134, 31–42. doi: 10.1016/j.biomaterials.2017.04.037
  9. Cheng, J.; Feng, S.; Han, S.; Zhang, X.; Chen, Y.; Zhou, X.; Wang, R.; Li, X.; Hu, H.; Zhang, J. Facile Assembly of Cost-Effective and Locally Applicable or Injectable Nanohemostats for Hemorrhage Control. ACS Nano, 2016, 10(11), 9957&ndash9973. doi: 10.1021/acsnano.6b04124
  10. Hill, T.K.; Kelkar, S.S.; Wojtynek, N.E.; Souchek, J.J:; Payne, W.M.; Stumpf, K.; Marini, F.C.; Mohs, A.M. Near Infrared Fluorescent Nanoparticles Derived from Hyaluronic Acid Improve Tumor Contrast for Image-Guided Surgery. Theranostics, 2016, 6(13), 2314–2328. doi: 10.7150/thno.16514
  11. Kelkar, S.S.; Hill, T.K.; Marini, F.C.; Mohs, A.M. Near infrared fluorescent nanoparticles based on hyaluronic acid: self-assembly, optical properties, and cell interaction. Acta Biomaterialia, 2016, 36, 112–121. doi: 10.1016/j.actbio.2016.03.024
  12. Saadat, E.; Shakor, N.; Gholami, M.; Dorkoosh, F.A. Hyaluronic acid based micelle for articular delivery of triamcinolone, preparation, in vitro and in vivo evaluation. International Journal of Pharmaceutics, 2015, 489(1–2), 218–225. doi: 10.1016/j.ijpharm.2015.05.001

Cyanine7.5 гидразид

  1. Liu, S.; Dozois, M.D.; Chang, C.N.; Ahmad, A.; Ng, D.L.T.; Hileeto, D.; Liang, H.; Reyad, M.-M.; Boyd, S.; Jones, L.W.; Gu, F.X. Prolonged Ocular Retention of Mucoadhesive Nanoparticle Eye Drop Formulation Enables Treatment of Eye Diseases Using Significantly Reduced Dosage. Molecular Pharmaceutics, 2016, 13(9), 2897–2905. doi: 10.1021/acs.molpharmaceut.6b00445

Cyanine7.5 карбоновая кислота

  1. Howard, G.P.; Verma, G.; Ke, X.; Thayer, W.M.; Hamerly, T.; Baxter, V.K.; Lee, J.E.; Dinglasan, R.R.; Mao, H.-Q. Critical size limit of biodegradable nanoparticles for enhanced lymph node trafficking and paracortex penetration. Nano Research, 2019, 12(4), 837–844. doi: 10.1007/s12274-019-2301-3
  2. Luthman, A.S. Wide-Field fHSI with a Linescan SRDA. In: Spectrally Resolved Detector Arrays for Multiplexed Biomedical Fluorescence Imaging (Springer Thesis), 2018, 51–85. doi: 10.1007/978-3-319-98255-7_3
  3. Nunes, R.; Araújo, F.; Tavares, J.; Sarmento, B.; das Neves, J. Surface modification with polyethylene glycol enhances colorectal distribution and retention of nanoparticles. European Journal of Pharmaceutics and Biopharmaceutics, 2018, 130, 200–206. doi: 10.1016/j.ejpb.2018.06.029
  4. Roberts, S.; Andreou, C.; Choi, C.; Donabedian, P.; Jayaraman, M.; Pratt, E.C.; Tang, J.; Pérez-Medina, C.; de la Cruz, M.J.; Mulder, W.J.M.; Grimm, J.; Kircher, M.; Reiner, T. Sonophore-enhanced nanoemulsions for optoacoustic imaging of cancer. Chemical Science, 2018, 9(25), 5646–5657. doi: 10.1039/C8SC01706A
  5. Luthman, A.S.; Dumitru, S.; Quiros-Gonzalez, I.; Joseph, J.; Bohndiek, S.E. Fluorescence hyperspectral imaging (fHSI) using a spectrally resolved detector array. Journal of Biophotonics, 2017, 10(6–7), 840–853. doi: 10.1002/jbio.201600304
  6. Shen, T.; Guan, S.; Gan, Z.; Zhang, G.; Yu, Q. Polymeric Micelles with Uniform Surface Properties and Tunable Size and Charge: Positive Charges Improve Tumor Accumulation. Biomacromolecules, 2016, 17(5), 1801–1810. doi: 10.1021/acs.biomac.6b00234
  7. Ravar, F.; Saadat, E.; Gholami, M.; Dehghankelishady, P.; Mahdavi, M.; Azami, S.; Dorkoosh, F.A. Hyaluronic acid-coated liposomes for targeted delivery of paclitaxel, in-vitro characterization and in-vivo evaluation. Journal of Controlled Release, 2016, 229, 10–22. doi: 10.1016/j.jconrel.2016.03.012
  8. Du, N.; Guo, W.; Yu, Q.; Guan, S.; Guo, L.; Shen, T.; Tang, H.; Gan, Z. Poly(D,L-lactic acid)-block-poly(N-(2-hydroxypropyl)methacrylamide) nanoparticles for overcoming accelerated blood clearance and achieving efficient anti-tumor therapy. Polymer Chemistry, 2016, 7(36), 5719–5729. doi: 10.1039/c6py01113f
  9. Rodell, C.B.; Rai, R.; Faubel, S.; Burdick, J.A.; Soranno, D.E. Local Immunotherapy via Delivery of Interleukin-10 and Transforming Growth Factor β Antagonist for Treatment of Chronic Kidney Disease. Journal of Controlled Release, 2015, 206, 131–139. doi: 10.1016/j.jconrel.2015.03.025
  10. Rodell, C.B.; Wade, R.J.; Purcell, B.P.; Dusaj, N.N.; Burdick, J.A. Selective Proteolytic Degradation of Guest–Host Assembled, Injectable Hyaluronic Acid Hydrogels. ACS Biomaterials Science & Engineering, 2015, 1(4), 277–286. doi: 10.1021/ab5001673
  11. Wade, R.J.; Bassin, E.J.; Rodell, C.B.; Burdick, J.A. Protease-degradable electrospun fibrous hydrogels. Nature Communications, 2015, 6, 6639. doi: 10.1038/ncomms7639

Cyanine7.5 малеимид

  1. Men, Y.; Peng, S.; Yang, P.; Jiang, Q.; Zhang, Y.; Shen, B.; Dong, P.; Pang, Z.; Yang, W. Biodegradable Zwitterionic Nanogels with Long Circulation for Antitumor Drug Delivery. ACS Applied Materials & Interfaces, 2018, 10(28), 23509–23521. doi: 10.1021/acsami.8b03943

DMS(O)MT аминолинк C6

  1. Aparin, I.O.; Farzan, V.M.; Veselova, O.A.; Chistov, A.A.; Podkolzin, A.T.; Ustinov, A.V.; Shipulin, G.A.; Formanovsky, A.A.; Korshun, V.A.; Zatsepin, T.S. 1-Phenylethynylpyrene (PEPy) as a novel blue-emitting dye for qPCR assay. Analyst, 2016, 141, 1331–1338. doi: 10.1039/c5an01767j

EdU (5-этинил-2'-дезоксиуридин)

  1. Hernandez-Segura, A.; Brandenburg, S.; Demaria, M. Induction and Validation of Cellular Senescence in Primary Human Cells. Journal of Visualized Experiments, 2018, 136, e57782. doi: 10.3791/57782

FAM (флуоресцеин) азид, 5-изомер

  1. Haider, N.; Dutt, P.; van de Kooij, B.; Yaffe, M.B.; Stambolic, V. NEK10 tyrosine phosphorylates p53 and controls its transcriptional activity. bioRxiv, preprint. doi: 10.1101/516971
  2. Feltes, M.; Moores, S.; Gale, S.E.; Krishnan, K.; Mydock-McGrane, L.; Covey, D.F.; Ory, D.S.; Schaffer, J.E. Synthesis and characterization of diazirine alkyne probes for the study of intracellular cholesterol trafficking. Journal of Lipid Research, 2019, 60(3), 707–716. doi: 10.1194/jlr.D091470
  3. Delasoie, J.; Rossier, J.; Haeni, L.; Rothen-Rutishauser, B.; Zobi, F. Slow-targeted release of a ruthenium anticancer agent from vitamin B12 functionalized marine diatom microalgae. Dalton Transactions, 2018, 47(48), 17221–17232. doi: 10.1039/c8dt02914h
  4. Ta, D.T.; Vanella, R.; Nash, M.A. Bioorthogonal Elastin-like Polypeptide Scaffolds for Immunoassay Enhancement. ACS Applied Materials & Interfaces, 2018, 10(36), 30147–30154. doi: 10.1021/acsami.8b10092
  5. Dutta, D.; Lai, K.-Y.; Reyes-Ordoñez, A.; Chen, J.; van der Donk, W.A. Lanthionine synthetase C-like protein 2 (LanCL2) is Important for Adipogenic Differentiation. Journal of Lipid Research, 2018, 59(8), 1433–1445. doi: 10.1194/jlr.M085274
  6. Ganapathy, U.S.; Bai, L.; Wei, L.; Eckartt, K.A.; Lett, C.M.; Previti, M.L.; Carrico, I.S.; Seeliger, J.C. Compartment-Specific Labeling of Bacterial Periplasmic Proteins by Peroxidase-Mediated Biotinylation. ACS Infectious Diseases, 2018, 4(6), 918–925. doi: 10.1021/acsinfecdis.8b00044
  7. Su, H.; Liu, Z.; Liu, Y.; Ma, V.P.-Y.; Blanchard, A.; Zhao, J.; Galior, K.; Dyer, R.B.; Salaita, K. Light-Responsive Polymer Particles as Force Clamps for the Mechanical Unfolding of Target Molecules. Nano Letters, 2018, 18(4), 2630–2636. doi: 10.1021/acs.nanolett.8b00459
  8. Long, M.J.C.; Urul, D.A.; Chawla, S.; Lin, H.-Y.; Zhao, Y.; Haegele, J.A.; Wang, Y.; Aye, Y. Precision Electrophile Tagging in Caenorhabditis elegans. Biochemistry, 2018, 57(2), 216–220. doi: 10.1021/acs.biochem.7b00642
  9. Penn, C.; Yang, K.; Zong, H.; Lim, J.-Y.; Cole, A.; Yang, D.; Baker, J.; Goonewardena, S.N.; Buckanovich, R.J. Therapeutic Impact of Nanoparticle Therapy Targeting Tumor Associated Macrophages. Molecular Cancer Therapeutics, 2018, 17(1), 96–106. doi: 10.1158/1535-7163.MCT-17-0688
  10. Fatona, A.; Berry, R.M.; Brook, M.A.; Moran-Mirabal, J.M. Versatile Surface Modification of Cellulose Fibres and Cellulose Nanocrystals through Modular Triazinyl Chemistry. Chemistry of Materials, 2018, 30(7), 2424–2435. doi: 10.1021/acs.chemmater.8b00511
  11. Pink, M.; Verma, N.; Zerries, A.; Schmitz-Spanke, S. Dose-dependent response to 3-nitrobenzanthrone exposure in human urothelial cancer cells. Chemical Research in Toxicology, 2017, 30(10), 1855–1864. doi: 10.1021/acs.chemrestox.7b00174
  12. Guttenplan, A.P.M.; Young, L.J.; Matak-Vinkovic, D.; Kaminski, C.F.; Knowles, T.P.J.; Itzhaki, L.S. Nanoscale click-reactive scaffolds from peptide self-assembly. Journal of Nanobiotechnology, 2017, 15, 70. doi: 10.1186/s12951-017-0300-7
  13. Ruhl, K.E; Rovis, T. Visible Light-Gated Cobalt Catalysis for a Spatially and Temporally Resolved [2+2+2] Cycloaddition. Journal of the American Chemical Society, 2016, 138(48), 15527–15530. doi: 10.1021/jacs.6b08792
  14. Berte, N.; Piee-Staffa, A.; Piecha, N.; Wang, M.; Borgmann, K.; Kaina, B.; Nikolova, T. Targeting homologous recombination by pharmacological inhibitors enhances the killing response of glioblastoma cells treated with alkylating drugs. Molecular Cancer Therapeutics, 2016, 15(11), 2665–2678. doi: 10.1158/1535-7163.mct-16-0176
  15. Ngo, J.T.; Adams, S.R.; Deerinck, T.J.; Boassa, D.; Rodriguez-Rivera, F.; Palida, S.F.; Bertozzi, C.R.; Ellisman, M.H.; Tsien, R.Y. Click-EM for imaging metabolically tagged nonprotein biomolecules. Nature Chemical Biology, 2016, 12(6), 459–465. doi: 10.1038/nchembio.2076
  16. Li, Z.; Liu, Z.; Chen, Z.; Ju, E.; Li, W.; Ren, J.; Qu, X. Bioorthogonal chemistry for selective recognition, separation and killing bacteria over mammalian cells. Chemical Communications, 2016, 52(17), 3482–3485. doi: 10.1039/c5cc10625g

FAM (флуоресцеин) азид, 6-изомер

  1. Haider, N.; Dutt, P.; van de Kooij, B.; Yaffe, M.B.; Stambolic, V. NEK10 tyrosine phosphorylates p53 and controls its transcriptional activity. bioRxiv, preprint. doi: 10.1101/516971
  2. Feltes, M.; Moores, S.; Gale, S.E.; Krishnan, K.; Mydock-McGrane, L.; Covey, D.F.; Ory, D.S.; Schaffer, J.E. Synthesis and characterization of diazirine alkyne probes for the study of intracellular cholesterol trafficking. Journal of Lipid Research, 2019, 60(3), 707–716. doi: 10.1194/jlr.D091470
  3. Ruhl, K.E; Rovis, T. Visible Light-Gated Cobalt Catalysis for a Spatially and Temporally Resolved [2+2+2] Cycloaddition. Journal of the American Chemical Society, 2016, 138(48), 15527–15530. doi: 10.1021/jacs.6b08792
  4. Berte, N.; Piee-Staffa, A.; Piecha, N.; Wang, M.; Borgmann, K.; Kaina, B.; Nikolova, T. Targeting homologous recombination by pharmacological inhibitors enhances the killing response of glioblastoma cells treated with alkylating drugs. Molecular Cancer Therapeutics, 2016, 15(11), 2665–2678. doi: 10.1158/1535-7163.mct-16-0176
  5. Ngo, J.T.; Adams, S.R.; Deerinck, T.J.; Boassa, D.; Rodriguez-Rivera, F.; Palida, S.F.; Bertozzi, C.R.; Ellisman, M.H.; Tsien, R.Y. Click-EM for imaging metabolically tagged nonprotein biomolecules. Nature Chemical Biology, 2016, 12(6), 459–465. doi: 10.1038/nchembio.2076
  6. Kryvalap, Y.; Lo, C.-W.; Manuylova, E.; Baldzizhar, R.; Jospe, N.; Czyzyk, J. Antibody Response to Serpin B13 Induces Adaptive Changes in Mouse Pancreatic Islets and Slows Down the Decline in the Residual Beta Cell Function in Children with Recent Onset of Type 1 Diabetes Mellitus. Journal of Biological Chemistry, 2016, 291(1), 266–278. doi: 10.1074/jbc.M115.687848

FAM (флуоресцеин) алкин, 5-изомер

  1. Rojas-Sánchez, L.; Sokolova, V.; Riebe, S.; Voskuhl, J.; Epple, M. Covalent Surface Functionalization of Calcium Phosphate Nanoparticles with Fluorescent Dyes by Copper-Catalysed and by Strain-Promoted Azide-Alkyne Click Chemistry. ChemNanoMat, 2019, 5(4), 436–446. doi: 10.1002/cnma.201800509
  2. Liang, S.; Guan, Y.; Zhang, Y. Layer-by-Layer Assembly of Microgel Colloidal Crystals via Photoinitiated Alkyne–Azide Click Reaction. ACS Omega, 2019, 4(3), 5650–5660. doi: 10.1021/acsomega.9b00354
  3. Ganapathy, U.S.; Bai, L.; Wei, L.; Eckartt, K.A.; Lett, C.M.; Previti, M.L.; Carrico, I.S.; Seeliger, J.C. Compartment-Specific Labeling of Bacterial Periplasmic Proteins by Peroxidase-Mediated Biotinylation. ACS Infectious Diseases, 2018, 4(6), 918–925. doi: 10.1021/acsinfecdis.8b00044
  4. Stadler, D.; Siribbal, S.M.; Gessner, I.; Öz, S.; Ilyas, S.; Mathur, S. Asymmetric attachment and functionalization of plasmonic nanoparticles on ceramic interfaces. Journal of Nanostructure in Chemistry, 2018, 8(1), 33–44. doi: 10.1007/s40097-018-0252-y
  5. Shi, P.; Ju, E.; Yan, Z.; Gao, N.; Wang, J.; Hou, J.; Zhang, Y.; Ren, J.; Qu, X. Spatiotemporal control of cell-cell reversible interactions using molecular engineering. Nature communications, 2016, 7, 13088. doi: 10.1038/ncomms13088
  6. Lu, X.; Jia, F.; Tan, X.; Wang, D.; Cao, X.; Zheng, J.; Zhang, K. Effective Antisense Gene Regulation via Noncationic, Polyethylene Glycol Brushes. Journal of the American Chemical Society, 2016, 138(29), 9097–9100. doi: 10.1021/jacs.6b05787
  7. Ilnitskaya, E.V.; Kononevich, Y.N.; Muzafarov, A.M.; Rzhevskiy, S.A.; Shadrin, I.A.; Babaev, E.V.; Martynov, V.I.; Pakhomov, A.A. Preparation and application of a BODIPY-labeled probe for a real-time polymerase chain reaction. Russian Journal of Bioorganic Chemistry, 2015, 41(4), 451–453. doi: 10.1134/S1068162015040068

FAM (флуоресцеин) алкин, 6-изомер

  1. Machado, Y.; Duinkerken, S.; Hoepflinger, V.; Mayr, M.; Korotchenko, E.; Kurtaj, A.; Pablos, I.; Steiner, M.; Stoecklinger, A.; Lübbers, J.; Schmid, M.; Ritter, U.; Scheiblhofer, S.; Ablinger, M.; Wally, V.; Hochmann, S.; Raninger, A.M.; Strunk, D.; van Kooyk, Y.; Thalhamer, J.; Weiss, R. Synergistic effects of dendritic cell targeting and laser-microporation on enhancing epicutaneous skin vaccination efficacy. Journal of Controlled Release, 2017, 266, 87–99. doi: 10.1016/j.jconrel.2017.09.020
  2. Shi, P.; Ju, E.; Yan, Z.; Gao, N.; Wang, J.; Hou, J.; Zhang, Y.; Ren, J.; Qu, X. Spatiotemporal control of cell-cell reversible interactions using molecular engineering. Nature communications, 2016, 7, 13088. doi: 10.1038/ncomms13088

FAM активированный эфир, 6-изомер

  1. Evans, L.E.; Jones, K.; Cheeseman, M.D. Targeting secondary protein complexes in drug discovery: studying the druggability and chemical biology of the HSP70/BAG1 complex. Chemical Communications, 2017, 53(37), 5167–5170. doi: 10.1039/c7cc01376k
  2. Warminski, M.; Sikorski, P.J.; Warminska, Z.; Lukaszewicz, M.; Kropiwnicka, A.; Zuberek, J.; Darzynkiewicz, E.; Kowalska, J.; Jemielity, J. Amino-functionalized 5' cap analogs as tools for site-specific sequence-independent labeling of messenger RNA. Bioconjugate Chemistry, 2017, 28(7), 1978–1992. doi: 10.1021/acs.bioconjchem.7b00291
  3. Horning, D.P.; Joyce, G.F. Amplification of RNA by an RNA polymerase ribozyme. Proceedings of the National Academy of Sciences of the United States of America, 2016, 113(35), 9786–9791. doi: 10.1073/pnas.1610103113

FAM малеимид, 6-изомер

  1. Nojoumi, S.; Ma, Y.; Schwagerus, S.; Hackenberger, C.P.R.; Budisa, N. In-Cell Synthesis of Bioorthogonal Alkene Tag S-Allyl-Homocysteine and Its Coupling with Reprogrammed Translation. International Journal of Molecular Sciences, 2019, 20(9), 2299. doi: 10.3390/ijms20092299
  2. Yu, C.; Tang, J.; Loredo, A.; Chen, Y.; Jung, S.Y.; Jain, A.; Gordon, A.; Xiao, H. Proximity-Induced Site-Specific Antibody Conjugation. Bioconjugate Chemistry, 2018, 29(11), 3522–3526. doi: 10.1021/acs.bioconjchem.8b00680

FAM фосфорамидит, 6-изомер

  1. Zhou, Z.; Liu, S.; Zhang, Y.; Yang, X.; Ma, Y.; Guan, Z.; Wu, Y.; Zhang, L.; Yang, Z. Reductive nanocomplex encapsulation of cRGD-siRNA conjugates for enhanced targeting to cancer cells. International Journal of Nanomedicine, 2017, 12, 7255–7272. doi: 10.2147/ijn.S136726

JOE азид, 5- изомер

  1. Nåbo, L.J.; Madsen, C.S.; Jensen, K.J.; Kongsted, J.; Astakhova, K. Ultramild Protein-Mediated Click Chemistry Creates Efficient Oligonucleotide Probes for Targeting and Detecting Nucleic Acids. ChemBioChem, 2015, 16(8), 1163–1167. doi: 10.1002/cbic.201500145

R110 азид, 5-изомер

  1. Nåbo, L.J.; Madsen, C.S.; Jensen, K.J.; Kongsted, J.; Astakhova, K. Ultramild Protein-Mediated Click Chemistry Creates Efficient Oligonucleotide Probes for Targeting and Detecting Nucleic Acids. ChemBioChem, 2015, 16(8), 1163–1167. doi: 10.1002/cbic.201500145
  2. Shieh, P.; Siegrist, M.S.; Cullen, A.J.; Bertozzi, C.R. Imaging bacterial peptidoglycan with near-infrared fluorogenic azide probes. Proceedings of the National Academy of Sciences of the U.S.A., 2014, 111(15), 5456–5461. doi: 10.1073/pnas.1322727111
  3. Okholm, A.; Kjems, J.; Astakhova, K. Fluorescence detection of natural RNA using rationally designed "clickable" oligonucleotide probes. RSC Advances, 2014, 4(86), 45653–45656. doi: 10.1039/c4ra07165d

R110 азид, 6-изомер

  1. Shieh, P.; Siegrist, M.S.; Cullen, A.J.; Bertozzi, C.R. Imaging bacterial peptidoglycan with near-infrared fluorogenic azide probes. Proceedings of the National Academy of Sciences of the U.S.A., 2014, 111(15), 5456–5461. doi: 10.1073/pnas.1322727111

ROX активированный эфир, 5-изомер

  1. Konopka, C.J.; Wozniak, M.; Hedhli, J.; Ploska, A.; Schwartz-Duval, A.; Siekierzycka, A.; Pan, D.; Munirathinam, G.; Dobrucki, I.T.; Kalinowski, L.; Dobrucki, L.W. Multimodal imaging of the receptor for advanced glycation end-products with molecularly targeted nanoparticles. Theranostics, 2018, 8(18), 5012–5024. doi: 10.7150/thno.24791

ROX активированный эфир, 6-изомер

  1. Konopka, C.J.; Wozniak, M.; Hedhli, J.; Ploska, A.; Schwartz-Duval, A.; Siekierzycka, A.; Pan, D.; Munirathinam, G.; Dobrucki, I.T.; Kalinowski, L.; Dobrucki, L.W. Multimodal imaging of the receptor for advanced glycation end-products with molecularly targeted nanoparticles. Theranostics, 2018, 8(18), 5012–5024. doi: 10.7150/thno.24791

ROX референсный краситель

  1. Schmidt, N.; Kollewe, A.; Constantin, C.E.; Henrich, S.; Ritzau-Jost, A.; Bildl, W.; Saalbach, A.; Hallermann, S.; Kulik, A.; Fakler, B.; Schulte, U. Neuroplastin and Basigin Are Essential Auxiliary Subunits of Plasma Membrane Ca2+-ATPases and Key Regulators of Ca2+ Clearance. Neuron, 2017, 96(4), 827–838.e9. doi: 10.1016/j.neuron.2017.09.038

ROX-азид, 5-изомер

  1. Feltes, M.; Moores, S.; Gale, S.E.; Krishnan, K.; Mydock-McGrane, L.; Covey, D.F.; Ory, D.S.; Schaffer, J.E. Synthesis and characterization of diazirine alkyne probes for the study of intracellular cholesterol trafficking. Journal of Lipid Research, 2019, 60(3), 707–716. doi: 10.1194/jlr.D091470
  2. Verardi, R.; Kim, J.-S.; Ghirlando, R.; Banerjee, A. Structural Basis for Substrate Recognition by the Ankyrin Repeat Domain of Human DHHC17 Palmitoyltransferase. Structure, 2017, 25(9), 1337–1347. doi: 10.1016/j.str.2017.06.018
  3. Bak, D.W.; Pizzagalli, M.D.; Weerapana, E. Identifying Functional Cysteine Residues in the Mitochondria. ACS Chemical Biology, 2017, 12(4), 947–957. doi: 10.1021/acschembio.6b01074
  4. Nåbo, L.J.; Madsen, C.S.; Jensen, K.J.; Kongsted, J.; Astakhova, K. Ultramild Protein-Mediated Click Chemistry Creates Efficient Oligonucleotide Probes for Targeting and Detecting Nucleic Acids. ChemBioChem, 2015, 16(8), 1163–1167. doi: 10.1002/cbic.201500145
  5. Astakhova, I.K.; Wengel, J. Interfacing Click Chemistry with Automated Oligonucleotide Synthesis for the Preparation of Fluorescent DNA Probes Containing Internal Xanthene and Cyanine Dyes. Chemistry - a European Journal, 2013, 19(3), 1112-1122. doi: 10.1002/chem.201202621
  6. Liboska, R.; Ligasová, A.; Strunin, D.; Rosenberg, I.; Koberna, K. Most Anti-BrdU Antibodies React with 2'-Deoxy-5-Ethynyluridine ‒ The Method for the Effective Suppression of This Cross-Reactivity. PLoS ONE, 2012, 7(12), e51679. doi: 10.1371/journal.pone.0051679

SYBR Green I для ПЦР реального времени, 100x

  1. Yang, F.; Teoh, F.; Tan, A.S.M.; Cao, Y.; Pavelka, N.; Berman, J. Aneuploidy enables cross-adaptation to unrelated drugs. Molecular Biology and Evolution, in press. doi: 10.1093/molbev/msz104
  2. Segal, E.S.; Gritsenko, V.; Levitan, A.; Yadav, B.; Dror, N.; Steenwyk, J.L.; Silberberg, Y.; Mielich, K.; Rokas, A.; Gow, N.A.R.; Kunze, R.; Sharan, R.; Berman, J. Gene Essentiality Analyzed by In Vivo Transposon Mutagenesis and Machine Learning in a Stable Haploid Isolate of Candida albicans. mBio, 2018, 9(5), e02048-18. doi: 10.1128/mBio.02048-18
  3. Maximova, N.; Koroleva, A.; Sitnikova, T.; Khanaev, I.; Bukin, Y.; Kirilchik, S. Age Dynamics of Telomere Length of Baikal Gastropods is Sex Specific and Multidirectional. Folia Biologica (Kraków), 2017, 65(4), 187–197. doi: 10.3409/fb65_4.187
  4. Schmidt, N.; Kollewe, A.; Constantin, C.E.; Henrich, S.; Ritzau-Jost, A.; Bildl, W.; Saalbach, A.; Hallermann, S.; Kulik, A.; Fakler, B.; Schulte, U. Neuroplastin and Basigin Are Essential Auxiliary Subunits of Plasma Membrane Ca2+-ATPases and Key Regulators of Ca2+ Clearance. Neuron, 2017, 96(4), 827–838.e9. doi: 10.1016/j.neuron.2017.09.038
  5. Sharangdhar, T.; Sugimoto, Y.; Heraud-Farlow, J.; Fernández-Moya, S.M.; Ehses, J.; Ruiz de Los Mozos, I.; Ule, J.; Kiebler, M.A. A retained intron in the 3'-UTR of Calm3 mRNA mediates its Staufen2- and activity-dependent localization to neuronal dendrites. EMBO Reports, 2017, 18(10), 1762–1774. doi: 10.15252/embr.201744334
  6. Revalde, J.L.; Li, Y.; Wijeratne, T.S.; Bugde, P.; Hawkins, B.C.; Rosengren, R.J.; Paxton, J.W. Curcumin and its cyclohexanone analogue inhibited human Equilibrative nucleoside transporter 1 (ENT1) in pancreatic cancer cells. European Journal of Pharmacology, 2017, 803, 167–173. doi: 10.1016/j.ejphar.2017.03.055
  7. Wu, Z.-G.; Jiang, W.; Chen, S.-L.; Mantri, N.; Tao, Z.-M.; Jiang, C.-X. Insights from the Cold Transcriptome and Metabolome of Dendrobium officinale: Global Reprogramming of Metabolic and Gene Regulation Networks during Cold Acclimation. Frontiers in Plant Science, 2016, 7, 1653. doi: 10.3389/fpls.2016.01653
  8. Brauer, V.S.; Stomp, M.; Bouvier, T.; Fouilland, E.; Leboulanger, C.; Confurius-Guns, V.; Weissing, F.J.; Stal, L.J.; Huisman, J. Competition and facilitation between the marine nitrogen-fixing cyanobacterium Cyanothece and its associated bacterial community. Frontiers in Microbiology, 2015, 5, 795. doi: 10.3389/fmicb.2014.00795

SYBR Green I раствор для прокраски гелей, 10000x

  1. Komarova, N.; Andrianova, M.; Glukhov, S.; Kuznetsov, A. Selection, Characterization, and Application of {ssDNA} Aptamer against Furaneol. Molecules, 2018, 23(12), 3159. doi: 10.3390/molecules23123159
  2. Zietzer, A.; Buschmann, E.E.; Janke, D.; Li, L.; Brix, M.; Meyborg, H.; Stawowy, P.; Jungk, C.; Buschmann, I.; Hillmeister, P. Acute Physical Exercise and Long-Term Individual Shear Rate Therapy Increase Telomerase Activity in Human Peripheral Blood Mononuclear Cells. Acta Physiologica, 2017, 220(2), 251–262. doi: 10.1111/apha.12820
  3. Diaz-Romero, J.; Kürsener, S.; Kohl, S.; Nesic, D. S100B+A1 CELISA: A Novel Potency Assay and Screening Tool for Redifferentiation Stimuli of Human Articular Chondrocytes. Journal of Cellular Physiology, 2017, 232(6), 1559–1570. doi: 10.1002/jcp.25682
  4. Richter-Heitmann, T.; Eickhorst, T.; Knauth, S.; Friedrich, M.W.; Schmidt, H. Evaluation of Strategies to Separate Root-Associated Microbial Communities: A Crucial Choice in Rhizobiome Research. Frontiers in Microbiology, 2016, 7, 773. doi: 10.3389/fmicb.2016.00773
  5. Jain, D.; Siede, W. Rad5 Template Switch Pathway of DNA Damage Tolerance Determines Synergism between Cisplatin and NSC109268 in Saccharomyces cerevisiae. PLoS ONE, 2013, 8(10), e77666. doi: 10.1371/journal.pone.0077666
  6. Song, C.-X.; Sun, Y.; Dai, Q.; Lu, X.-Y.; Yu, M.; Yang, C.-G.; He, C. Detection of 5-Hydroxymethylcytosine in DNA by Transferring a Keto-Glucose by Using T4 Phage beta-Glucosyltransferase. ChemBioChem, 2011, 12(11), 1682-1685. doi: 10.1002/cbic.201100278
  7. Song, C.-X.; Yu, M.; Dai, Q.; He, C. Detection of 5-hydroxymethylcytosine in a combined glycosylation restriction analysis (CGRA) using restriction enzyme Taq[alpha]I. Bioorganic & Medicinal Chemistry Letters, 2011, 21(17), 5075-5077. doi: 10.1016/j.bmcl.2011.03.118

Sulfo-Cyanine3 азид

  1. Doll, F.; Steimbach, R.; Zumbusch, A. Direct Imaging of Protein-Specific Methylation in Mammalian Cells. Chembiochem, 2019, 20(10), 1315–1325. doi: 10.1002/cbic.201800787
  2. Cohen, J.; Raviv, S.; Adir, O.; Padmanabhan, K.; Soffer, A.; Luxenburg, C. The Wave complex controls epidermal morphogenesis and proliferation by suppressing Wnt-Sox9 signaling. Journal of Cell Biology, 2019, 218(4), 1390–1406. doi: 10.1083/jcb.201807216
  3. Melnychuk, N.; Klymchenko, A.S. DNA-Functionalized Dye-Loaded Polymeric Nanoparticles: Ultrabright FRET Platform for Amplified Detection of Nucleic Acids. Journal of the American Chemical Society, 2018, 140(34), 10856–10865. doi: 10.1021/jacs.8b05840
  4. Hernandez-Segura, A.; Brandenburg, S.; Demaria, M. Induction and Validation of Cellular Senescence in Primary Human Cells. Journal of Visualized Experiments, 2018, 136, e57782. doi: 10.3791/57782
  5. Wong, S.Z.H.; Scott, E.P.; Mu, W.; Guo, X.; Borgenheimer, E.; Freeman, M.; Ming, G.-L.; Wu, Q.-F.; Song, H.; Nakagawa, Y. In vivo clonal analysis reveals spatiotemporal regulation of thalamic nucleogenesis. PLoS Biology, 2018, 16, e2005211. doi: 10.1371/journal.pbio.2005211
  6. Konishcheva, E.V.; Zhumaev, U.E.; Meier, W.P. PEO-b-PCL-b-PMOXA Triblock Copolymers: From Synthesis to Microscale Polymersomes with Asymmetric Membrane. Macromolecules, 2017, 50(4), 1512–1520. doi: 10.1021/acs.macromol.6b02743
  7. Sun, L.; Gai, Y.; Anderson, C.J.; Zeng, D. Highly-efficient and versatile fluorous-tagged Cu(I)-catalyzed azide–alkyne cycloaddition ligand for preparing bioconjugates. Chemical Communications, 2015, 51, 17072–17075. doi: 10.1039/C5CC06858D
  8. Haller, A.; Altman, R.B.; Souliere, M.F.; Blanchard, S.C.; Micura, R. Folding and ligand recognition of the TPP riboswitch aptamer at single-molecule resolution. Proceedings of the National Academy of Sciences of the U.S.A., 2013, 110(11), 4188-4193. doi: 10.1073/pnas.1218062110

Sulfo-Cyanine3 активированный эфир

  1. Huang, S.; Qi, J.; deQuilettes, D.W.; Huang, M.; Lin, C.-W.; Bardhan, N.M.; Dang, X.; Bulović, V.; Belcher, A.M. M13 Virus-Based Framework for High Fluorescence Enhancement. Small, in press. doi: 10.1002/smll.201901233
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  3. Umakoshi, T.; Fukuda, S.; Iino, R.; Uchihashi, T.; Ando, T. High-speed near-field fluorescence microscopy combined with high-speed atomic force microscopy for biological studies. Biochimica et Biophysica Acta, in press. doi: 10.1016/j.bbagen.2019.03.011
  4. Kam, A.; Loo, S.; Dutta, B.; Sze, S.K.; Tam, J.P. Plant-derived mitochondria-targeting cysteine-rich peptide modulates cellular bioenergetics. Journal of Biological Chemistry, 2019, 294(11), 4000–4011. doi: 10.1074/jbc.RA118.006693
  5. Cao, P.; Wei, X.; Awal, R.P.; Müller, R.; Wall, D. A Highly Polymorphic Receptor Governs Many Distinct Self-Recognition Types within the Myxococcales Order. mBio, 2019, 10, e02751-18. doi: 10.1128/mBio.02751-18
  6. Meena, G.G.; Jain, A.; Parks, J.; Stambaugh, A.; Patterson, J.; Hawkins, A.; Schmidt, H. Integration of sample preparation and analysis on an optofluidic chip for multi-target disease detection. Lab on a Chip, 2018, 18(23), 3678–3686. doi: 10.1039/c8lc00966j
  7. Zadeh, P.S.N.; do Valle Gomes, M.Z.; Abrahamsson, M.; Palmqvist, A.; Åkerman, B. Measuring Viscosity inside Mesoporous Silica Using Protein-Bound Molecular Rotor Probe. Physical Chemistry Chemical Physics, 2018, 20(36), 23202–23213. doi: 10.1039/C8CP01063C
  8. Gu, R.; Oweida, T.; Yingling, Y.G.; Chilkoti, A.; Zauscher, S. Enzymatic synthesis of nucleobase-modified single-stranded DNA offers tunable resistance to nuclease degradation. Biomacromolecules, 2018, 19(8), 3525–3535. doi: 10.1021/acs.biomac.8b00816
  9. Zadeh, P.S.N.; do Valle Gomes, M.Z.; Åkerman, B.; Palmqvist, A.E.C. Förster resonance energy transfer study of the improved biocatalytic conversion of CO2 to formaldehyde by co-immobilization of enzymes in siliceous mesostructured cellular foams. ACS Catalysis, 2018, 8(8), 7251–7260. doi: 10.1021/acscatal.8b01806
  10. Stambaugh, A.; Parks, J.W.; Stott, M.A.; Meena, G.G.; Hawkins, A.R.; Schmidt, H. Optofluidic detection of Zika nucleic acid and protein biomarkers using multimode interference multiplexing. Biomedical Optics Express, 2018, 9(8), 3725–3730. doi: 10.1364/BOE.9.003725
  11. Selnihhin, D.; Sparvath, S.M.; Preus, S.; Birkedal, V.; Andersen, E.S. Multi-Fluorophore DNA Origami Beacon as a Biosensing Platform. ACS Nano, 2018, 12(6), 5699–5708. doi: 10.1021/acsnano.8b01510
  12. Sallada, N.D.; Dunn, K.J.; Berger, B.W. A structural and functional role for disulfide bonds in a class II hydrophobin. Biochemistry, 2018, 57(5), 645–653. doi: 10.1021/acs.biochem.7b01166
  13. Zabara, A.; Meikle, T.G.; Trenker, R.; Yao, S.; Newman, J.; Peat, T.S.; Separovic, F.; Conn, C.E.; Call, M.J.; Call, M.E.; Landau, E.M.; Drummond, C.J. Lipidic Cubic Phase-Induced Membrane Protein Crystallization: Interplay Between Lipid Structure, Mesophase Properties, and Crystallogenesis. Crystal Growth and Design, 2017, 17(11), 5667–5674. doi: 10.1021/acs.cgd.7b00519
  14. Ozcelik, D.; Jain, A.; Stambaugh, A.; Stott, M.A.; Parks, J.W.; Hawkins, A.; Schmidt, H. Scalable Spatial-Spectral Multiplexing of Single-Virus Detection Using Multimode Interference Waveguides. Scientific Reports, 2017, 7, 12199. doi: 10.1038/s41598-017-12487-0
  15. Shi, X.; Yu, C.Y.Y.; Su, H.; Kwok, R.T.K.; Jiang, M.; He, Z.; Lam, J.W.Y.; Tang, B.Z. A Red-emissive antibody–AIEgen conjugate for turn-on and wash-free imaging of specific cancer cells. Chemical Science, 2017, 8(10), 7014–7024. doi: 10.1039/C7SC01054K
  16. Schneider, J.R.; Carias, A.M.; Bastian, A.R.; Cianci, G.C.; Kiser, P.F.; Veazey, R.S.; Hope, T.J. Long-term direct visualization of passively transferred fluorophore-conjugated antibodies. Journal of Immunological Methods, 2017, 450, 66–72. doi: 10.1016/j.jim.2017.07.009
  17. Huang, T.-Y.; Chang, C.-K.; Kao, Y.-F.; Chin, C.-H.; Ni, C.-W.; Hsu, H.-Y.; Hu, N.-J.; Hsieh, L.-C.; Chou, S.-H.; Lee, I.-R.; Hou, M.-H. Parity-dependent hairpin configurations of repetitive DNA sequence promote slippage associated with DNA expansion. Proceedings of the National Academy of Sciences of the USA, 2017, 114(36), 9535–9540. doi: 10.1073/pnas.1708691114
  18. Barnett, D.; Liu, Y.; Partyka, K.; Huang, Y.; Tang, H.; Hostetter, G.; Brand, R.E.; Singhi, A.D.; Drake, R.R.; Haab, B.B. The CA19-9 and Sialyl-TRA Antigens Define Separate Subpopulations of Pancreatic Cancer Cells. Scientific Reports, 2017, 7, 4020. doi: 10.1038/s41598-017-04164-z
  19. Korkmaz, E.; Friedrich, E.E.; Ramadan, M.H.; Erdos, G.; Mathers, A.R.; Ozdoganlar, O.B.; Washburn, N.R.; Falo, Jr, L.D. Tip-Loaded Dissolvable Microneedle Arrays Effectively Deliver Polymer-Conjugated Antibody Inhibitors of Tumor-Necrosis-Factor-Alpha Into Human Skin. Journal of Pharmaceutical Sciences, 2016, 105(11), 3453–3457. doi: 10.1016/j.xphs.2016.07.008
  20. Zhou, L.; Wang, K.; Wu, Z.; Dong, H.; Sun, H.; Cheng, X.; Zhang, H.; Zhou, H.; Jia, C.; Jin, Q.; Mao, H.; Coll, J.-L.; Zhao, J. Investigation of Controllable Nanoscale Heat-Denatured Bovine Serum Albumin Films on Graphene. Langmuir, 2016, 32(48), 12623–12631. doi: 10.1021/acs.langmuir.6b03296
  21. Zhang, X.; MIn, L.; Jia, C. Application of Wavelet Transform Algorithm and Rolling Ball Algorithm in Single Molecule Fluorescence Resonance Energy Transfer Images. Progress in Biochemistry and Biophysics, 2016, 43(10), 997–1003. doi: 10.16476/j.pibb.2016.0218
  22. Søndergaard, S.; Aznauryan, M.; Haustrup, E.K.; Schiøtt, B.; Birkedal, V.; Corry, B. Dynamics of Fluorescent Dyes Attached to G-Quadruplex DNA and their Effect on FRET Experiments. ChemPhysChem, 2015, 16(12), 2562–2570. doi: 10.1002/cphc.201500271
  23. Wang, W.; Kapur, A.; Ji, X.; Safi, M.; Palui, G.; Palomo, V.; Dawson, P.E.; Mattoussi, H. Photoligation of an Amphiphilic Polymer with Mixed Coordination Provides Compact and Reactive Quantum Dots. Journal of the American Chemical Society, 2015, 137(16), 5438–5451. doi: 10.1021/jacs.5b00671
  24. Reid, D.A.; Keegan, S.; Leo-Macias, A.; Watanabe, G.; Strande, N.T.; Chang, H.H.; Oksuz, B.A.; Fenyo, D.; Lieber, M.R.; Ramsden, D.A.; Rothenberg, E. Organization and dynamics of the nonhomologous end-joining machinery during DNA double-strand break repair. Proceedings of the National Academy of Sciences of the U.S.A., 2015, 112(20), E2575–E2584. doi: 10.1073/pnas.1420115112
  25. Glembockyte, V.; Lincoln, R.; Cosa, G. Cy3 Photoprotection Mediated by Ni2+ for Extended Single-Molecule Imaging: Old Tricks for New Techniques. Journal of the American Chemical Society, 2015, 137(3), 1116–1122. doi: 10.1021/ja509923e
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  28. Wang, W.; Ji, X.; Na, H.B.; Safi, M.; Smith, A.; Palui, G.; Perez, J.M.; Mattoussi, H. Design of a Multi-Dopamine-Modified Polymer Ligand Optimally Suited for Interfacing Magnetic Nanoparticles with Biological Systems. Langmuir, 2014, 30(21), 6197-6208. doi: 10.1021/la500974r
  29. Aldeek, F.; Muhammed, M.A.H.; Palui, G.; Zhan, N.; Mattoussi, H. Growth of Highly Fluorescent Polyethylene Glycol- and Zwitterion-Functionalized Gold Nanoclusters. ACS Nano, 2013, 7(3), 2509-2521. doi: 10.1021/nn305856t
  30. Zhan, N.; Palui, G.; Safi, M.; Ji, X.; Mattoussi, H. Multidentate Zwitterionic Ligands Provide Compact and Highly Biocompatible Quantum Dots. Journal of the American Chemical Society, 2013, 135(37), 13786-13795. doi: 10.1021/ja405010v
  31. Kim, W.-J.; Kim, A.; Huh, C.; Park, C.W.; Ah, C.S.; Kim, B.K.; Yang, J.-H.; Chung, K.H.; Choi, Y.H.; Hong, J. et al. Photo selective protein immobilization using bovine serum albumin. Applied Surface Science, 2012, 261, 880-889. doi: 10.1016/j.apsusc.2012.08.111

Sulfo-Cyanine3 алкин

  1. Tobola, F.; Sylvander, E.; Gafko, C.; Wiltschi, B. `Clickable lectins': bioorthogonal reactive handles facilitate the directed conjugation of lectins in a modular fashion. Interface Focus, 2019, 9(2), 20180072. doi: 10.1098/rsfs.2018.0072
  2. Rambarran, T.; Gonzaga, F.; Fatona, A.; Coulson, M.; Saem, S.; Moran-Mirabal, J.; Brook, M.A. Bonding and in-channel microfluidic functionalization using the huisgen cyclization. ournal of Polymer Science Part A: Polymer Chemistry, 2018, 56(6), 589–597. doi: 10.1002/pola.28930
  3. Konishcheva, E.V.; Zhumaev, U.E.; Meier, W.P. PEO-b-PCL-b-PMOXA Triblock Copolymers: From Synthesis to Microscale Polymersomes with Asymmetric Membrane. Macromolecules, 2017, 50(4), 1512–1520. doi: 10.1021/acs.macromol.6b02743

Sulfo-Cyanine3 амин

  1. Zhang, Q.; Scigliano, A.; Biver, T.; Pucci, A.; Swager, T.M. Interfacial Bioconjugation on Emulsion Droplet for Biosensors. Bioorganic & Medicinal Chemistry, 2018, 26(19), 5307–5313. doi: 10.1016/j.bmc.2018.04.020
  2. Sobotzki, N.; Schafroth, M.A.; Rudnicka, A.; Koetemann, A.; Marty, F.; Goetze, S.; Yamauchi, Y.; Carreira, E.M.; Wollscheid, B. HATRIC-based identification of receptors for orphan ligands. Nature Communications, 2018, 9, 1519. doi: 10.1038/s41467-018-03936-z

Sulfo-Cyanine3 карбоновая кислота

  1. Cho, U.; Riordan, D.P.; Ciepla, P.; Kocherlakota, K.S.; Chen, J.K.; Harbury, P.B. Ultrasensitive optical imaging with lanthanide lumiphores. Nature Chemical Biology, 2018, 14(1), 15–21. doi: 10.1038/nchembio.2513
  2. Spears, B.R.; Marin, M.A.; Chaker, A.N.; Lampley, M.W.; Harth, E. Precise Microscale Polymeric Networks through Piezoelectronic Inkjet Printing. ACS Biomaterials Science & Engineering, 2016, 2(8), 1265–1272. doi: 10.1021/acsbiomaterials.6b00175

Sulfo-Cyanine3 малеимид

  1. Tischer, D.K.; Weiner, O.D. Light-based tuning of ligand half-life supports kinetic proofreading model of T cell signaling. eLIFE, 2019, 8, e42489. doi: 10.7554/eLife.42498
  2. Ni, Y.; Arts, R.; Merkx, M. Ratiometric bioluminescent sensor proteins based on intramolecular split luciferase complementation. ACS Sensors, 2019, 4(1), 20–25. doi: 10.1021/acssensors.8b01381
  3. Agrawalla, B.K.; Wang, T.; Riegger, A.; Domogalla, M.P.; Steinbrink, K.; Dörfler, T.; Chen, X.; Boldt, F.; Lamla, M.; Michaelis, J.; Kuan, S.L.; Weil, T. Chemoselective Dual and Triple Labelling of Native and Recombinant Proteins. Bioconjugate Chemistry, 2018, 29(1), 29–34. doi: 10.1021/acs.bioconjchem.7b00675
  4. Yao, L.; Li, Q.; Guan, Y.; Zhu, X.X.; Zhang, Y. Tetrahedral, Octahedral, and Triangular Dipyramidal Microgel Clusters with Thermosensitivity Fabricated from Binary Colloidal Crystals Template and Thiol–Ene Reaction. ACS Macro Letters, 2018, 7, 80–84. doi: 10.1021/acsmacrolett.7b00935
  5. Steffen, W.; Ko, F.C.; Patel, J.; Lyamichev, V.; Albert, T.; Benz, J.; Rudolph, M.G.; Bergmann, F.; Streidl, T.; Kratzsch, P.; Boenitz-Dulat, M.; Oelschlaegel, T.; Schraeml, M. Discovery of a microbial transglutaminase enabling highly site-specific labeling of proteins. Journal of Biological Chemistry, 2017, 292(38), 15622–15635. doi: 10.1074/jbc.M117.797811
  6. Allen, C.D.; Chen, M.Y.; Trick, A.Y.; Le, D.T.; Ferguson, A.L.; Link, A.J. Thermal Unthreading of the Lasso Peptides Astexin-2 and Astexin-3. ACS Chemical Biology, 2016, 11(11), 3043–3051. doi: 10.1021/acschembio.6b00588
  7. Shebl, B., Menke, D.E.; Pennella, M.; Poudyal, R.R.; Burke, D.H.; Cornish, P.V. Preparation of ribosomes for smFRET studies: A simplified approach. Archives of Biochemistry and Biophysics, 2016, 603, 118–130. doi: 10.1016/j.abb.2016.05.010

Sulfo-Cyanine5 азид

  1. Chariou, P.L.; Dogan, A.B.; Welsh, A.G.; Saidel, G.M.; Baskaran, H.; Steinmetz, N.F. Soil mobility of synthetic and virus-based model nanopesticides. Nature Nanotechnology, in press. doi: 10.1038/s41565-019-0453-7
  2. Yang, Z.; Joyner, A.L. YAP is involved in replenishment of granule cell progenitors following injury to the neonatal cerebellum. bioRxiv, preprint. doi: 10.1101/558742
  3. De France, K.J.; Badv, M.; Dorogin, J.; Siebers, E.; Panchal, V.; Babi, M.; Moran-Mirabal, J.; Lawlor, M.; Cranston, E.D.; Hoare, T. Tissue Response and Biodistribution of Injectable Cellulose Nanocrystal Composite Hydrogels. ACS Biomaterials Science & Engineering, 2019, 5(5), 2235–2246. doi: 10.1021/acsbiomaterials.9b00522
  4. Zemella, A.; Richter, T.; Thoring, L.; Kubick, S. A Combined Cell-Free Protein Synthesis and Fluorescence-Based Approach to Investigate GPCR Binding Properties. Methods in Molecular Biology, 2019, 1947, 57–77. doi: 10.1007/978-1-4939-9121-1_4
  5. Liang, S.; Guan, Y.; Zhang, Y. Layer-by-Layer Assembly of Microgel Colloidal Crystals via Photoinitiated Alkyne–Azide Click Reaction. ACS Omega, 2019, 4(3), 5650–5660. doi: 10.1021/acsomega.9b00354
  6. De France, K.J.; Babi, M.; Vapaavuori, J.; Hoare, T.; Moran-Mirabal, J.M.; Cranston, E.D. 2.5D Hierarchical Structuring of Nanocomposite Hydrogel Films Containing Cellulose Nanocrystals. ACS Applied Materials & Interfaces, 2019, 11(6), 6325–6335. doi: 10.1021/acsami.8b16232
  7. Maerle, A.V.; Simonova, M.A.; Pivovarov, V.D.; Voronina, D.V.; Drobyazina, P.E.; Trofimov, D.Y.; Alekseev, L.P.; Zavriev, S.K.; Ryazantsev, D.Y. Development of the covalent antibody-DNA conjugates technology for detection of IgE and IgM antibodies by immuno-PCR. PloS One, 2019, 14(1), e0209860. doi: 10.1371/journal.pone.0209860
  8. Marín-Caba, L.; Chariou, P.L.; Pesquera, C.; Correa-Duarte, M.A.; Steinmetz, N.F. Tobacco Mosaic Virus-Functionalized Mesoporous Silica Nanoparticles, a Wool-Ball-like Nanostructure for Drug Delivery. Langmuir, 2019, 35(1), 203–211. doi: 10.1021/acs.langmuir.8b03337
  9. Pitek, A.S.; Hu, H.; Shukla, S.; Steinmetz, N.F. Cancer Theranostic Applications of Albumin-Coated Tobacco Mosaic Virus Nanoparticles. ACS Applied Materials & Interfaces, 2018, 10(46), 39468–39477. doi: 10.1021/acsami.8b12499
  10. van Hall-Beauvais, A.; Zhao, Y.; Urul, D.A.; Long, M.J.C.; Aye, Y. Single-Protein-Specific Redox Targeting in Live Mammalian Cells and C. elegans. Current Protocols in Chemical Biology, 2018, 10(3), e43. doi: 10.1002/cpch.43
  11. Karas, J.; Turner, B.J.; Shabanpoor, F. The Assembly of Fluorescently Labeled Peptide-Oligonucleotide Conjugates via Orthogonal Ligation Strategies. Methods in Molecular Biology, 2018, 1282, 355–363. doi: 10.1007/978-1-4939-8651-4_22
  12. Lomakin, Y.; Kudriaeva, A.; Kostin, N.; Terekhov, S.; Kaminskaya, A.; Chernov, A.; Zakharova, M.; Ivanova, M.; Simaniv, T.; Telegin, G.; Gabibov, A.; Belogurov, A. Diagnostics of autoimmune neurodegeneration using fluorescent probing. Scientific Reports, 2018, 8, 12679. doi: 10.1038/s41598-018-30938-0
  13. Franke, C.E.; Czapar, A.E.; Patel, R.B.; Steinmetz, N.F. Tobacco Mosaic Virus-Delivered Cisplatin Restores Efficacy in Platinum-Resistant Ovarian Cancer Cells. Molecular Pharmaceutics, 2018, 15(8), 2922–2931. doi: 10.1021/acs.molpharmaceut.7b00466
  14. Gupta, S.; M-Redmond, T; Meng, F.; Tidball, A.; Akil, H.; Watson, S.; Parent, J.M.; Uhler, M.; others. Fibroblast Growth Factor 2 Regulates Activity and Gene Expression of Human Postmitotic Excitatory Neuron. Journal of Neurochemistry, 2018, 145(3), 188–203. doi: 10.1111/jnc.14255
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  61. Han, Z.; Zhou, Z.; Shi, X.; Wang, J.; Wu, X.; Sun, D.; Chen, Y.; Zhu, H.; Magi-Galluzzi, C.; Lu, Z.-R. EDB fibronectin specific peptide for prostate cancer targeting. Bioconjugate Chemistry, 2015, 26(5), 830–838. doi: 10.1021/acs.bioconjchem.5b00178
  62. Aldeek, F.; Hawkins, D.; Palomo, V.; Safi, M.; Palui, G.; Dawson, P.E.; Alabugin, I.V.; Mattoussi, H. UV and Sunlight Driven Photoligation of Quantum Dots: Understanding the Photochemical Transformation of the Ligands. Journal of the American Chemical Society, 2015, 137(7), 2704–2714. doi: 10.1021/ja512802x
  63. Wen, A.M.; Infusino, M.; De Luca, A.; Kernan, D.L.; Czapar, A.E.; Strangi, G.; Steinmetz, N.F. Interface of Physics and Biology: Engineering Virus-Based Nanoparticles for Biophotonics. Bioconjugate Chemistry, 2015, 26(1), 51–62. doi: 10.1021/bc500524f
  64. Nakamura, T.; Sugihara, F.; Matsushita, H.; Yoshioka, Y.; Mizukami, S.; Kikuchi, K. Mesoporous silica nanoparticles for 19F magnetic resonance imaging, fluorescence imaging, and drug delivery. Chemical Science, 2015, 6, 1986–1990. doi: 10.1039/c4sc03549f
  65. Hsueh, P.-Y.; Edman, M.C.; Sun, G.; Shi, P.; Xu, S.; Lin, Y.-a.; Cui, H.; Hamm-Alvarez, S.F.; MacKay, J.A. Tear-mediated delivery of nanoparticles through transcytosis of the lacrimal gland. Journal of Controlled Release, 2015, 208, 2–13. doi: 10.1016/j.jconrel.2014.12.017
  66. Geertsema, H.J.; Duderstadt, K.E.; van Oijen, A.M. Single-molecule observation of prokaryotic DNA replication. Methods in Molecular Biology, 2015, 1300, 219–238. doi: 10.1007/978-1-4939-2596-4_14
  67. Nooney, R.I.; White, A.; O’Mahony, C.; O’Connell, C.; Kelleher, S.M.; Daniels, S.; McDonagh, C. Investigating the colloidal stability of fluorescent silica nanoparticles under isotonic conditions for biomedical applications. Journal of Colloid and Interface Science, 2015, 456, 50–58. doi: 10.1016/j.jcis.2015.05.051
  68. Santangelo, M.F.; Sciuto, E.L.; Busacca, A.C.; Petralia, S.; Conoci, S.; Libertino, S. SiPM as miniaturised optical biosensor for DNA-microarray applications. Sensing and Bio-Sensing Research, 2015, 6, 95–98. doi: 10.1016/j.sbsr.2015.08.003
  69. Sciuto, E.L.; Santangelo, M.F.; Villaggio, G.; Sinatra, F.; Bongiorno, C.; Nicotra, G.; Libertino, S. Photo-physical characterization of fluorophore Ru(bpy)32+ for optical biosensing applications. Sensing and Bio-Sensing Research, 2015, 6, 67–71. doi: 10.1016/j.sbsr.2015.09.003
  70. Hickey, S. F.; Hammond, M.C. Structure-Guided Design of Fluorescent S-Adenosylmethionine Analogs for a High-Throughput Screen to Target SAM-I Riboswitch RNAs. Chemistry & Biology, 2014, 21(3), 345–356. doi: 10.1016/j.chembiol.2014.01.004
  71. Terekhov, S.S.; Smirnov, I.V.; Shamborant, O.G.; Zenkova, M.A.; Chernolovskaya, E.L.; Gladkikh, D.V.; Murashev, A.N.; Dyachenko, I.A.; Knorre, V.D.; Belogurov, A.A.; Ponomarenko, N.A.; Deyev, S.M.; Vlasov, V.V.; Gabibov, A.G. Excessive Labeling Technique Provides a Highly Sensitive Fluorescent Probe for Real-time Monitoring of Biodegradation of Biopolymer Pharmaceuticals in vivo. Acta Naturae, 2014, 6(4), 54–59
  72. Ayala-Orozco, C.; Liu, J.G.; Knight, M.W.; Wang, Y.; Day, J.K.; Nordlander, P.; Halas, N.J. Fluorescence Enhancement of Molecules Inside a Gold Nanomatryoshka. Nano Letters, 2014, 14(5), 2926-2933. doi: 10.1021/nl501027j
  73. Brand, C.; Abdel-Atti, D.; Zhang, Y.; Carlin, S.; Clardy, S.M.; Keliher, E.J.; Weber, W.A.; Lewis, J.S.; Reiner, T. In Vivo Imaging of GLP-1R with a Targeted Bimodal PET/Fluorescence Imaging Agent. Bioconjugate Chemistry, 2014, 25(7), 1323-1330. doi: 10.1021/bc500178d
  74. Graen, T.M.D.; Hoefling, M.; Grubmüller, H. AMBER-DYES: Characterization of Charge Fluctuations and Force Field Parameterization of Fluorescent Dyes for Molecular Dynamics Simulations. Journal of Chemical Theory and Computation, 2014, 10(12), 5505-5512. doi: 10.1021/ct500869p
  75. Li, L.-L.; Xu, J.-H.; Qi, G.-B.; Zhao, X.; Yu, F.; Wang, H. Core-Shell Supramolecular Gelatin Nanoparticles for Adaptive and "On-Demand" Antibiotic Delivery. ACS Nano, 2014, 8(5), 4975-4983. doi: 10.1021/nn501040h
  76. Viehweger, K.; Barbaro, L.; García, K.P.; Joshi, T.; Geipel, G.; Steinbach, J.; Stephan, H.; Spiccia, L.; Graham, B. EGF Receptor-Targeting Peptide Conjugate Incorporating a Near-IR Fluorescent Dye and a Novel 1,4,7-Triazacyclononane-Based 64Cu(II) Chelator Assembled via Click Chemistry. Bioconjugate Chemistry, 2014, 25(5), 1011-1022. doi: 10.1021/bc5001388
  77. Zhou, Z.; Wu, X.; Kresak, A.; Griswold, M.; Lu, Z.-R. Peptide targeted tripod macrocyclic Gd(III) chelates for cancer molecular MRI. Biomaterials, 2013, 34(31), 7683-7693. doi: 10.1016/j.biomaterials.2013.06.057
  78. Zou, C.; Loka, R.S.; Zhang, Y.; Cairo, C.W. Glycoform Remodeling Generates a Synthetic T Cell Phenotype. Bioconjugate Chemistry, 2013, 24(6), 907-914. doi: 10.1021/bc300599w

Sulfo-Cyanine5 алкин

  1. Rojas-Sánchez, L.; Sokolova, V.; Riebe, S.; Voskuhl, J.; Epple, M. Covalent Surface Functionalization of Calcium Phosphate Nanoparticles with Fluorescent Dyes by Copper-Catalysed and by Strain-Promoted Azide-Alkyne Click Chemistry. ChemNanoMat, 2019, 5(4), 436–446. doi: 10.1002/cnma.201800509
  2. Braselmann, E.; Wierzba, A.J.; Polaski, J.T.; Chromiński, M.; Holmes, Z.E.; Hung, S.-T.; Batan, D.; Wheeler, J.R.; Parker, R.; Jimenez, R.; Gryko, D.; Batey, R.T.; Palmer, A.E. A multicolor riboswitch-based platform for imaging of RNA in live mammalian cells. Nature Chemical Biology, 2018, 14(10), 964–971. doi: 10.1038/s41589-018-0103-7
  3. Qu, S.; Shi, Y.; Benavides, S.; Hunter, A.J.; Gao, H.; Phillip, W.A. Copolymer Nanofilters with Charge-Patterned Domains for Enhanced Electrolyte Transport. Chemistry of Materials, 2017, 29(2), 762–772. doi: 10.1021/acs.chemmater.6b04660
  4. Ngambenjawong, C.; Gustafson, H.H.; Pineda, J.M.; Kacherovsky, N.A.; Cieslewicz, M.; Pun, S.H. Serum Stability and Affinity Optimization of an M2 Macrophage-Targeting Peptide (M2pep). Theranostics, 2016, 6(9), 1403–1414. doi: 10.7150/thno.15394

Sulfo-Cyanine5 амин

  1. Guo, A.; Durymanov, M.; Permyakova, A.; Sene, S.; Serre, C.; Reineke, J. Metal Organic Framework (MOF) Particles as Potential Bacteria-Mimicking Delivery Systems for Infectious Diseases: Characterization and Cellular Internalization in Alveolar Macrophages , 2019, 36, 53. doi: 10.1007/s11095-019-2589-4
  2. Xie, J.; Yang, C.; Liu, Q.; Li, J.; Liang, R.; Shen, C.; Zhang, Y.; Wang, K.; Liu, L.; Shezad, K.; Sullivan, M.; Xu, Y.; Shen, G.; Tao, J.; Zhu, J.; Zhang, Z. Encapsulation of Hydrophilic and Hydrophobic Peptides into Hollow Mesoporous Silica Nanoparticles for Enhancement of Antitumor Immune Response. Small, 2017, 13(40), 1701741. doi: 10.1002/smll.201701741

Sulfo-Cyanine5 карбоновая кислота

  1. Ranjit, S.; Malacrida, L.; Gratton, E. Differences between FLIM phasor analyses for data collected with the Becker and Hickl SPC830 card and with the FLIMbox card. Microscopy Research and Technique, 2018, 81(9), 980–989. doi: 10.1002/jemt.23061
  2. Razgoniaeva, N.; Rogers, S.; Moroz, P.; Cassidy, J.; Zamkov, M. Improving the spectral resolution in fluorescence microscopy through shaped-excitation imaging. Methods and Applications in Fluorescence, 2018, 6(4), 045006. doi: 10.1088/2050-6120/aad81c
  3. Siltanen, C.A.; Cole, R.H.; Poust, S.; Chao, L.; Tyerman, J.; Kaufmann-Malaga, B.; Ubersax, J.; Gartner, Z.J.; Abate, A.R. An Oil-Free Picodrop Bioassay Platform for Synthetic Biology. Scientific Reports, 2018, 8, 7913. doi: 10.1038/s41598-018-25577-4
  4. Zhao, Y.; Zhang, W.; Li, C. Optimization of the conical mirror design based on Monte Carlo simulations for fluorescence molecular tomography. SPIE Proceedings: Multimodal Biomedical Imaging XIII, 2018, 10487, 104870M. doi: 10.1117/12.2290665
  5. Cho, U.; Riordan, D.P.; Ciepla, P.; Kocherlakota, K.S.; Chen, J.K.; Harbury, P.B. Ultrasensitive optical imaging with lanthanide lumiphores. Nature Chemical Biology, 2018, 14(1), 15–21. doi: 10.1038/nchembio.2513
  6. Than, A.; Liang, K.; Xu, S.; Sun, L.; Duan, H.; Xi, F.; Xu, C.; Chen, P. Transdermal Delivery of Anti-Obesity Compounds to Subcutaneous Adipose Tissue with Polymeric Microneedle Patches. Small Methods, 2017, 1(11), 1700269. doi: 10.1002/smtd.201700269
  7. Summer, D.; Grossrubatscher, L.; Petrik, M.; Michalcikova, T.; Novy, Z.; Rangger, C.; Klingler, M.; von Guggenberg, E.; Haubner, R.; Kaeopookum, P.; Haas, H.; Decristoforo, C. Developing targeted hybrid imaging probes by chelator scaffolding. Bioconjugate Chemistry, 2017, 28(6), 1722–1733. doi: 10.1021/acs.bioconjchem.7b00182
  8. Hatai, J.; Motiei, L.; Margulies, D. Analyzing Amyloid Beta Aggregates with a Combinatorial Fluorescent Molecular Sensor. Journal of the American Chemical Society, 2017, 139(6), 2136–2139. doi: 10.1021/jacs.6b10809
  9. Schlegel, I.; Muñoz-Espí, R.; Renz, P.; Lieberwirth, I.; Floudas, G.; Suzuki, Y.; Crespy, D.; Landfester, K. Crystallinity Tunes Permeability of Polymer Nanocapsules. Macromolecules, 2017, 50(12), 4725–4732. doi: 10.1021/acs.macromol.7b00667
  10. Liu, M.; Richardson, R.R.; Mountford, S.J.; Zhang, L.; Tempone, M.H.; Herzog, H.; Holliday, N.D.; Thompson, P.E. Identification of a Cyanine-Dye Labelled Peptidic Ligand for Y1R and Y4R, based upon the Neuropeptide Y C-terminal analogue, BVD-15. Bioconjugate Chemistry, 2016, 27(9), 2166–2175. doi: 10.1021/acs.bioconjchem.6b00376
  11. Gao, P.; Hunter, A.J.; Summe, M.J.; Phillip, W.A. A Method for the Efficient Fabrication of Multifunctional Mosaic Membranes by Inkjet Printing. ACS Applied Materials & Interfaces, 2016, 8(30), 19772–19779. doi: 10.1021/acsami.6b06048
  12. Calver, C.F.; Liu, H.-W.; Cosa, G. Exploiting Conjugated Polyelectrolyte Photophysics towards Monitoring Real-Time Lipid Membrane-Surface Interaction Dynamics at the Single Particle Level. Langmuir, 2015, 31(43), 11842–11850. doi: 10.1021/acs.langmuir.5b00979
  13. Lee, S.J.; Shim, Y.H.; Oh, J.-S.; Jeong, Y.-I. Park, I.-K.; Lee, H.C. Folic-acid-conjugated pullulan/poly(DL-lactide-co-glycolide) graft copolymer nanoparticles for folate-receptor-mediated drug delivery. Nanoscale Research Letters, 2015, 10, 43. doi: 10.1186/s11671-014-0706-1
  14. Tucker, K.R.; Block, E.R.; Levitan, E.S. Action potentials and amphetamine release antipsychotic drug from dopamine neuron synaptic VMAT vesicles. Proceedings of the National Academy of Sciences of the U.S.A., 2015, 112(32), E4485–E4494. doi: 10.1073/pnas.1503766112
  15. Lin, W.; Liu, J.; Jeffries, C.; Yang, L.; Lu, Y.; Lee, R.E.; Chen, T. Development of BODIPY FL Vindoline as a Novel and High-Affinity Pregnane X Receptor Fluorescent Probe. Bioconjugate Chemistry, 2014, 25(9), 1664-1677. doi: 10.1021/bc5002856

Sulfo-Cyanine5 малеимид

  1. Baranova, N.; Radler, P.; Hernandez-Rocamora, V.M.; Alfonso, C.; Lopez-Pelegrin, M.; Rivas, G.; Vollmer, W.; Loose, M. FtsZ assembles the bacterial cell division machinery by a diffusion-and-capture mechanism. bioRxiv, preprint. doi: 10.1101/485656
  2. Graham, T.G.W.; Carney, S.M.; Walter, J.C.; Loparo, J.J. A single XLF dimer bridges DNA ends during nonhomologous end joining. Nature Structural & Molecular Biology, 2018, 25(9), 877–884. doi: 10.1038/s41594-018-0120-y
  3. Torres, O.B.; Duval, A.J.; Sulima, A.; Antoline, J.F.G.; Jacobson, A.E.; Rice, K.C.; Alving, C.R.; Matyas, G.R. A rapid solution-based method for determining the affinity of heroin hapten-induced antibodies to heroin, its metabolites, and other opioids. Analytical and Bioanalytical Chemistry, 2018, 410(16), 3885–3903. doi: 10.1007/s00216-018-1060-4
  4. Liu, L.; Zhang, C.; Li, Z.; Wang, C.; Bi, J.; Yin, S.; Wang, Q.; Yu, R.; Liu, Y.D.; Su, Z. Albumin binding domain fusing R/K-X-X-R/K sequence for enhancing tumor delivery of doxorubicin. Molecular Pharmaceutics, 2017, 14(11), 3739–3749. doi: 10.1021/acs.molpharmaceut.7b00497
  5. Guo, L.Y.; Allu, P.K.; Zandarashvili, L.; McKinley, K.L.; Sekulic, N.; Dawicki-McKenna, J.M.; Fachinetti, D.; Logsdon, G.A.; Jamiolkowski, R.M.; Cleveland, D.W.; Cheeseman, I.M.; Black, B.E. Centromeres are maintained by fastening CENP-A to DNA and directing an arginine anchor-dependent nucleosome transition. Nature Communications, 2017, 8, 15775. doi: 10.1038/ncomms15775
  6. Nemudraya, A.; Kuligina, E.; Ilyichev, A.; Fomin, A.; Stepanov, G.; Savelyeva, A.; Koval, O.; Richter, V. Selection of antitumor displayed peptides for the specific delivery of the anticancer drug lactaptin. Oncology Letters, 2016, 12(6), 4547–4555. doi: 10.3892/ol.2016.5266
  7. Bruckman, M.A.; Czapar, A.E.; VanMeter, A.; Randolph, L.N.; Steinmetz, N.F. Tobacco mosaic virus-based protein nanoparticles and nanorods for chemotherapy delivery targeting breast cancer. Journal of Controlled Release, 2016, 231, 103–113. doi: 10.1016/j.jconrel.2016.02.045
  8. Shebl, B., Menke, D.E.; Pennella, M.; Poudyal, R.R.; Burke, D.H.; Cornish, P.V. Preparation of ribosomes for smFRET studies: A simplified approach. Archives of Biochemistry and Biophysics, 2016, 603, 118–130. doi: 10.1016/j.abb.2016.05.010

Sulfo-Cyanine5.5 azide

  1. Erel-Akbaba, G.; Carvalho, L.A.; Tian, T.; Zinter, M.; Akbaba, H.; Obeid, P.J.; Chiocca, E.A.; Weissleder, R.; Kantarci, A.G.; Tannous, B.A. Radiation-Induced Targeted Nanoparticle-Based Gene Delivery for Brain Tumor Therapy. ACS Nano, 2019, 13(4), 4028–4040. doi: 10.1021/acsnano.8b08177
  2. Gu, W.; Bobrin, V.A.; Chen, S.-P.R.; Wang, Z.; Schoning, J.P.; Gu, Y.; Chen, W.; Chen, M.; Jia, Z.; Monteiro, M.J. Biodistribution of PNIPAM-Coated Nanostructures Synthesized by the TDMT Method. Biomacromolecules, 2019, 20(2), 625–634. doi: 10.1021/acs.biomac.8b01196

Sulfo-Cyanine5.5 активированный эфир

  1. Guenter, R.E.; Aweda, T.; Carmona Matos, D.M.; Whitt, J.; Chang, A.W.; Cheng, E.Y.; Liu, X.M.; Chen, H.; Lapi, S.E.; Jaskula-Sztul, R. Pulmonary Carcinoid Surface Receptor Modulation Using Histone Deacetylase Inhibitors. Cancers, 2019, 11(6), 767. doi: 10.3390/cancers11060767
  2. Kwon, Y.-D.; Oh, J.-M.; La, M.T.; Chung, H.-J.; Lee, S.J.; Chun, S.; Lee, S.-H.; Jeong, B.-H.; Kim, H.-K. Synthesis and Evaluation of Multifunctional Fluorescent Inhibitors with Synergistic Interaction of PSMA and Hypoxia for Prostate Cancer. Bioconjugate Chemistry, 2019, 30(1), 90–100. doi: 10.1021/acs.bioconjchem.8b00767
  3. Liu, Y.; Wang, Z.; Li, X.; Ma, X.; Wang, S.; Kang, F.; Yang, W.; Ma, W.; Wang, J. Near-infrared Fluorescent Peptides with High Tumor Selectivity: Novel Probes for Image-Guided Surgical Resection of Orthotopic Glioma. Molecular Pharmaceutics, 2019, 16(1), 108–117. doi: 10.1021/acs.molpharmaceut.8b00888
  4. Jasinski, D.L.; Yin, H.; Li, Z.; Guo, P. The Hydrophobic Effect from Conjugated Chemicals or Drugs on in Vivo Biodistribution of RNA Nanoparticles. Human Gene Therapy, 2018, 29(1), 77–86. doi: 10.1089/hum.2017.054
  5. Park, S.; Shevlin, E.; Vedvyas, Y.; Zaman, M.; Park, S.; Hsu, Y.-M.S.; Min, I.M.; Jin, M.M. Micromolar affinity CAR T cells to ICAM-1 achieves rapid tumor elimination while avoiding systemic toxicity. Scientific Reports, 2017, 7, 14366. doi: 10.1038/s41598-017-14749-3
  6. Zhang, C.; Zhao, X.; Guo, S.; Lin, T.; Guo, H. Highly effective photothermal chemotherapy with pH-responsive polymer-coated drug-loaded melanin-like nanoparticles. International Journal of Nanomedicine, 2017, 12, 1827–1840. doi: 10.2147/ijn.s130539
  7. Duan, X.; Li, H.; Zhou, J.; Zhou, Q.; Oldham, K.R.; Wang, T.D. Visualizing epithelial expression of EGFR in vivo with distal scanning side-viewing confocal endomicroscope. Scientific Reports, 2016, 6, 37315. doi: 10.1038/srep37315
  8. Zhou, Q.; Li, Z.; Zhou, J.; Joshi, B.P.; Li, G.; Duan, X.; Kuick, R.; Owens, S.R.; Wang, T.D. In vivo photoacoustic tomography of EGFR overexpressed in hepatocellular carcinoma mouse xenograft. Photoacoustics, 2016, 4(2), 43–54. doi: 10.1016/j.pacs.2016.04.001
  9. Abolmaali, S.; Tamaddon, A.; Kamali-Sarvestani, E.; Ashraf, M.; Dinarvand, R. Stealth Nanogels of Histinylated Poly Ethyleneimine for Sustained Delivery of Methotrexate in Collagen-Induced Arthritis Model. Pharmaceutical Research, 2015, 32(10), 3309–3323. doi: 10.1007/s11095-015-1708-0

Sulfo-Cyanine5.5 амин

  1. Malinovskaya, Y.; Melnikov, P.; Baklaushev, V.; Gabashvili, A.; Osipova, N.; Mantrov, S.; Ermolenko, Y.; Maksimenko, O.; Gorshkova, M.; Balabanyan, V.; Kreuter, J.; Gelperina, S. Delivery of doxorubicin-loaded PLGA nanoparticles into U87 human glioblastoma cells. International Journal of Pharmaceutics, 2017, 524(1–2), 77–90. doi: 10.1016/j.ijpharm.2017.03.049

Sulfo-Cyanine5.5 карбоновая кислота

  1. Wild, A.R.; Sinnen, B.L.; Dittmer, P.J.; Kennedy, M.J.; Sather, W.A.; Dell'Acqua, M.L. Synapse-to-Nucleus Communication through NFAT Is Mediated by L-type Ca2+ Channel Ca2+ Spike Propagation to the Soma. Cell Reports, 2019, 26, 3537–3550.e4. doi: 10.1016/j.celrep.2019.03.005

Sulfo-Cyanine7 активированный эфир

  1. Bykov, Y.; Cohen, N.; Gabrielli, N.; Manenschijn, H.; Welsch, S.; Chlanda, P.; Kukulski, W.; Patil, K.R.R.; Schuldiner, M.; Briggs, J.A.G. Multiplexed electron microscopy by fluorescent barcoding allows screening for ultrastructural phenotype. bioRxiv, preprint. doi: 10.1101/515841
  2. Wang, H.-N.; Register, J.K.; Fales, A.M.; Gandra, N.; Strobbia, P.; Cho, E.H.; Boico, A.; Palmer, G.M.; Klitzman, B.; Vo-Dinh, T. Implantable "smart tattoo" SERS nanosensors for in vivo detection of nucleic acid biotargets in a large animal model. Plasmonics in Biology and Medicine XVI (Proceedings SPIE 10894), 2019, 108941J. doi: 10.1117/12.2514634
  3. Chan, P.S.; Xian, J.W.; Li, Q.; Chan, C.W.; Leung, S.S.Y.; To, K.K.W. Biodegradable Thermosensitive PLGA-PEG-PLGA Polymer for Non-irritating and Sustained Ophthalmic Drug Delivery. AAPS Journal, 2019, 21, 59. doi: 10.1208/s12248-019-0326-x
  4. Song, J.Y.; Larson, N.R.; Thati, S.; Torres-Vazquez, I.; Martinez-Rivera, N.; Subelzu-Aispuru, N.J.; Leon, M.A.; Rosa-Molinar, E.; Schöneich, C.; Middaugh, C.R.; Berkland, C.J. Glatiramer acetate persists at the injection site and draining lymph nodes via electrostatically-induced aggregation. Journal of Controlled Release, 2019, 293, 36–47. doi: 10.1016/j.jconrel.2018.11.007
  5. Ishihara, J.; Ishihara, A.; Potin, L.; Hosseinchi, P.; Fukunaga, K.; Damo, M.; Gajewski, T.F.; Swartz, M.A.; Hubbell, J.A. Improving Efficacy and Safety of Agonistic Anti-CD40 Antibody Through Extracellular Matrix Affinity. Molecular Cancer Therapeutics, 2018, 17(11), 2399–2411. doi: 10.1158/1535-7163.MCT-18-0091
  6. Henderson, L.; Neumann, O.; Kaffes, C.; Zhang, R.; Marangoni, V.; Ravoori, M.K.; Kundra, V.; Bankson, J.; Nordlander, P.; Halas, N.J. Routes to Potentially Safer T1 Magnetic Resonance Imaging Contrast in a Compact Plasmonic Nanoparticle with Enhanced Fluorescence. ACS Nano, 2018, 12(8), 8214–8223. doi: 10.1021/acsnano.8b03368
  7. Bhatnagar, S.; Verma, K.D.; Hu, Y.; Khera, E.; Priluck, A.; Smith, D.E.; Thurber, G.M. Oral Administration and Detection of a Near-Infrared Molecular Imaging Agent in an Orthotopic Mouse Model for Breast Cancer Screening. Molecular Pharmaceutics, 2018, 15(5), 1746–1754. doi: 10.1021/acs.molpharmaceut.7b00994
  8. Gaspar, I.; Hövelmann, F.; Chamiolo, J.; Ephrussi, A.; Seitz, O. Quantitative mRNA Imaging with Dual Channel qFIT Probes to Monitor Distribution and Degree of Hybridization. ACS Chemical Biology, 2018, 13(3), 742–749. doi: 10.1021/acschembio.7b01007
  9. Liu, Z.; Wang, S.; Li, W.; Tian, Y. Bioimaging and Biosensing of Ferrous Ion in Neurons and HepG2 Cells Upon Oxidative Stress. Analytical Chemistry, 2018, 90(4), 2816–2825. doi: 10.1021/acs.analchem.7b04934
  10. Das, S.; Haedicke, K.; Grimm, J. Cerenkov-activated sticky tag for in vivo fluorescence imaging. Journal of Nuclear Medicine, 2018, 59(1), 58–65. doi: 10.2967/jnumed.117.198549
  11. Timin, A.S.; Muslimov, A.R.; Lepik, K.V.; Epifanovskaya, O.S:; Shakirova, A.I.; Mock, U.; Riecken, K.; Okilova, M.V.; Sergeev, V.S.; Afanasyev, B.V.; Fehse, B.; Sukhorukov, G.B. Efficient gene editing via non-viral delivery of CRISPR-Cas9 system using polymeric and hybrid microcarriers. Nanomedicine: Nanotechnology, Biology, and Medicine, 2018, 14(1), 97–108. doi: 10.1016/j.nano.2017.09.001
  12. Huang, Y.; Zhou, J.; Hakamivala, A.; Wu, J.; Hong, Y.; Borrelli, J.; Tang, L. An optical probe for detecting chondrocyte apoptosis in response to mechanical injury. Scientific Reports, 2017, 7, 10906. doi: 10.1038/s41598-017-10653-y
  13. Nakhaei, E.; Kim, C.W.; Funamoto, D.; Sato, H.; Nakamura, Y.; Kishimura, A.; Mori, T.; Katayama, Y. Design of a ligand for cancer imaging with long blood circulation and an enhanced accumulation ability in tumors. MedChemComm, 2017, 8(6), 1190–1195. doi: 10.1039/c7md00102a
  14. Iyisan, B.; Kluge, J.; Formanek, P.; Voit, B.; Appelhans, D. Multifunctional and Dual-Responsive Polymersomes as Robust Nanocontainers: Design, Formation by Sequential Post-Conjugations, and pH-Controlled Drug Release. Chemistry of Materials, 2016, 28(5), 1513–1525. doi: 10.1021/acs.chemmater.5b05016
  15. Saita, M.; Kaneko, J.; Sato, T.; Takahashi, S.; Takahashi, S.W.; Kawamata, R.; Sakurai, T.; Lee, M.-C.; Hamada, N.; Kimoto, K.; Nagasaki, Y. Novel antioxidative nanotherapeutics in a rat periodontitis model: Reactive oxygen species scavenging by redox injectable gel suppresses alveolar bone resorption. Biomaterials, 2016, 76, 292–301. doi: 10.1016/j.biomaterials.2015.10.077
  16. Subedi, M.; Minn, I.; Chen, J.; Kim, Y.; Ok, K.; Jung, Y.W.; Pomper, M.G.; Byun, Y. Design, synthesis and biological evaluation of PSMA/hepsin-targeted heterobivalent ligands. European Journal of Medicinal Chemistry, 2016, 118, 208–218. doi: 10.1016/j.ejmech.2016.04.033
  17. Cilliers, C.; Liao, J.; Atangcho, L.; Thurber, G.M. Residualization Rates of Near-Infrared Dyes for the Rational Design of Molecular Imaging Agents. Molecular Imaging and Biology, 2015, 17(6), 757–762. doi: 10.1007/s11307-015-0851-7
  18. Terekhov, S., Smirnov, I.; Bobik, T.; Shamborant, O.; Zenkova, M.; Chernolovskaya, E.; Gladkikh, D.; Murashev, A.; Dyachenko, I.; Palikov, V.; Palikova, Y.; Knorre, V.; Belogurov Jr, A.; Ponomarenko, N.; Blackburn, G.M.; Masson, P.; Gabibov, A. A novel expression cassette delivers efficient production of exclusively tetrameric human butyrylcholinesterase with improved pharmacokinetics for protection against organophosphate poisoning. Biochimie, 2015, 118, 51–59. doi: 10.1016/j.biochi.2015.07.028
  19. Mahoney, D.; Owens, E.A.; Fan, C.; Hsiang, J.-C.; Henary, M.; Dickson, R.M. Tailoring Cyanine Dark States for Improved Optically Modulated Fluorescence Recovery. The Journal of Physical Chemistry B, 2015, 119(13), 4637–4643. doi: 10.1021/acs.jpcb.5b00777
  20. Zhang, X.-N.; Zhang, C.-G.; Zhu, Q.-L.; Zhou, Y.; Liu, Y.; Chen, W.-L.; Yang, S.-D. Zhou, X.-F. Zhu, A.-J.; Zhang, X.-N.; Jin, Y. N-Succinyl-chitosan nanoparticles coupled with low-density lipoprotein for targeted osthole-loaded delivery to low-density lipoprotein receptor-rich tumors. International Journal of Nanomedicine, 2014, 9, 2919–2932. doi: 10.2147/ijn.s59799
  21. Terekhov, S.S.; Smirnov, I.V.; Shamborant, O.G.; Zenkova, M.A.; Chernolovskaya, E.L.; Gladkikh, D.V.; Murashev, A.N.; Dyachenko, I.A.; Knorre, V.D.; Belogurov, A.A.; Ponomarenko, N.A.; Deyev, S.M.; Vlasov, V.V.; Gabibov, A.G. Excessive Labeling Technique Provides a Highly Sensitive Fluorescent Probe for Real-time Monitoring of Biodegradation of Biopolymer Pharmaceuticals in vivo. Acta Naturae, 2014, 6(4), 54–59
  22. Ayala-Orozco, C.; Liu, J.G.; Knight, M.W.; Wang, Y.; Day, J.K.; Nordlander, P.; Halas, N.J. Fluorescence Enhancement of Molecules Inside a Gold Nanomatryoshka. Nano Letters, 2014, 14(5), 2926-2933. doi: 10.1021/nl501027j

Sulfo-Cyanine7 амин

  1. Auzély, R.; Rippe, M.; Stefanello, T.; Kaplum, V.; Britta, E.; Garcia, F.; Poirot, R.; Companhoni, M.V.; Nakamura, C.V.; Szarpak, A. Heparosan as a potential alternative to hyaluronic acid for the design of biopolymer-based nanovectors for anticancer therapy. Biomaterials Science, in press. doi: 10.1039/c9bm00443b
  2. Guo, X.; Zou, C.-L.; Jung, H.; Gong, Z.; Bruch, A.; Jiang, L.; Tang, H.X. Efficient Generation of a Near-visible Frequency Comb via Cherenkov-like Radiation from a Kerr Microcomb. Physical Review Applied, 2018, 10(1), 014012. doi: 10.1103/PhysRevApplied.10.014012
  3. Tabe, H.; Sukenobe, K.; Kondo, T.; Sakurai, A.; Maruo, M.; Shimauchi, A.; Hirano, M.; Uno, S.-N.; Kamiya, M.; Urano, Y.; Matsushita, M.; Fujiyoshi, S. Cryogenic Fluorescence Localization Microscopy of Spectrally Selected Individual FRET Pairs in a Water Matrix. The Journal of Physical Chemistry B, 2018, 122(27), 6906–6911. doi: 10.1021/acs.jpcb.8b03977
  4. Miragoli, M.; Ceriotti, P.; Iafisco, M.; Vacchiano, M.; Salvarani, N.; Alogna, A.; Carullo, P.; Ramirez-Rodríguez, G.B.; Patrício, T.; Esposti, L.D.; Rossi, F.; Ravanetti, F.; Pinelli, S.; Alinovi, R.; Erreni, M.; Rossi, S.; Condorelli, G.; Post, H.; Tampieri, A.; Catalucci, D. Inhalation of peptide-loaded nanoparticles improves heart failure. Science Translational Medicine, 2018, 10(424), eaan6205. doi: 10.1126/scitranslmed.aan6205
  5. Park, H.-K.; Lee, S.J.; Oh, J.-S.; Lee, S.-G.; Jeong, Y.-I.; Lee, H.C. Smart Nanoparticles Based on Hyaluronic Acid for Redox-Responsive and CD44 Receptor-Mediated Targeting of Tumor. Nanoscale Research Letters, 2015, 10(1), 981. doi: 10.1186/s11671-015-0981-5

Sulfo-Cyanine7 карбоновая кислота

  1. Luthman, A.S. Wide-Field fHSI with a Linescan SRDA. In: Spectrally Resolved Detector Arrays for Multiplexed Biomedical Fluorescence Imaging (Springer Thesis), 2018, 51–85. doi: 10.1007/978-3-319-98255-7_3
  2. Luthman, A.S.; Dumitru, S.; Quiros-Gonzalez, I.; Joseph, J.; Bohndiek, S.E. Fluorescence hyperspectral imaging (fHSI) using a spectrally resolved detector array. Journal of Biophotonics, 2017, 10(6–7), 840–853. doi: 10.1002/jbio.201600304

Sulfo-Cyanine7.5 карбоновая кислота

  1. Shi, F.; Li, M.; Wu, S.; Yang, F.; Di, W.; Pan, M.; Zhao, F.; Luo, S.; Gu, N.; Dou, J. Enhancing the Anti-Multiple Myeloma Efficiency in a Cancer Stem Cell Xenograft Model by Conjugating the ABCG2 Antibody with Microbubbles for a Targeted Delivery of Ultrasound Mediated Epirubicin. Biochemical Pharmacology, 2017, 132, 18–28. doi: 10.1016/j.bcp.2017.02.014

TAMRA азид, 5-изомер

  1. Zhang, S.; Spiegelman, N.A.; Lin, H. Global Profiling of Sirtuin Deacylase Substrates Using a Chemical Proteomic Strategy and Validation by Fluorescent Labeling. Methods in Molecular Biology, 2019, 2009, 137–147. doi: 10.1007/978-1-4939-9532-5_11
  2. Tang, G.; Liu, L.; Wang, X.; Pan, Z. Discovery of 7H-pyrrolo[2,3-d]pyrimidine derivatives as selective covalent irreversible inhibitors of interleukin-2-inducible T-cell kinase (Itk). European Journal of Medicinal Chemistry, 2019, 173, 167–183. doi: 10.1016/j.ejmech.2019.03.055
  3. Eelen, G.; Dubois, C.; Cantelmo, A.R.; Goveia, J.; Brüning, U.; DeRan, M.; Jarugumilli, G.; van Rijssel, J.; Saladino, G.; Comitani, F.; Zecchin, A.; Rocha, S.; Chen, R.; Huang, H.; Vandekeere, S.; Kalucka, J.; Lange, C.; Morales-Rodriguez, F.; Cruys, B.; Treps, L.; Ramer, L.; Vinckier, S.; Brepoels, K.; Wyns, S.; Souffreau, J.; Schoonjans, L.; Lamers, W.H.; Wu, Y.; Haustraete, J.; Hofkens, J.; Liekens, S.; Cubbon, R.; Ghesquière, B.; Dewerchin, M.; Gervasio, F.L.; Li, X.; van Buul, J.D.; Wu, X.; Carmeliet, P. Role of glutamine synthetase in angiogenesis beyond glutamine synthesis. Nature, 2018, 561(7721), 63–69. doi: 10.1038/s41586-018-0466-7
  4. Spangler, B.; Dovala, D.; Sawyer, W.S.; Thompson, K.V.; Six, D.A.; Reck, F.; Feng, B.Y. Molecular probes for the determination of sub-cellular compound exposure profiles in Gram-negative bacteria. ACS Infectious Diseases, 2018, 4(9), 1355–1367. doi: 10.1021/acsinfecdis.8b00093
  5. Moynihan, K.D.; Holden, R.L.; Mehta, N.K.; Wang, C.; Karver, M.R.; Dinter, J.; Liang, S.; Abraham, W.; Melo, M.B.; Zhang, A.Q.; Li, N.; Le Gall, S.; Pentelute, B.; Irvine, D.J. Enhancement of peptide vaccine immunogenicity by increasing lymphatic drainage and boosting serum stability. Cancer Immunology Research, 2018, 6(9), 1025–1038. doi: 10.1158/2326-6066.CIR-17-0607
  6. Li, W.; Zhou, Y.; Tang, G.; Wong, N.-K.; Yang, M.; Tan, D.; Xiao, Y. Chemoproteomics Reveals the Anti-proliferative Potential of Parkinson's Disease Kinase Inhibitor LRRK2-IN-1 by Targeting PCNA Protein. Molecular Pharmaceutics, 2018, 15(8), 3252–3259. doi: 10.1021/acs.molpharmaceut.8b00325
  7. Nemmara, V.J.; Subramanian, V.; Muth, A.; Mondal, S.; Salinger, A.J.; Maurais, A.J.; Tilvawala, R.; Weerapana, E.; Thompson, P.R. The Development of Benzimidazole-Based Clickable Probes for the Efficient Labeling of Cellular Protein Arginine Deiminases (PADs). ACS Chemical Biology, 2018, 13(3), 712–722. doi: 10.1021/acschembio.7b00957
  8. Niessen, S.; Dix, M.M.; Barbas, S.; Potter, Z.E.; Lu, S.; Brodsky, O.; Planken, S.; Behenna, D.; Almaden, C.; Gajiwala, K.S.; Ryan, K.; Ferre, R.; Lazear, M.R.; Hayward, M.M.; Kath, J.C.; Cravatt, B.F. Proteome-wide Map of Targets of T790M-EGFR-Directed Covalent Inhibitors. Cell Chemical Biology, 2017, 24(11), 1388–1400.e7. doi: 10.1016/j.chembiol.2017.08.017
  9. Schonhoft, J.D.; Monteiro, C.; Plate, L.; Eisele, Y.S.; Kelly, J.M.; Boland, D.; Parker, C.G.; Cravatt, B.F.; Teruya, S.; Helmke, S.; Maurer, M.; Berk, J.; Sekijima, Y.; Novais, M.; Coelho, T.; Powers, E.T.; Kelly, J.W. Peptide probes detect misfolded transthyretin oligomers in plasma of hereditary amyloidosis patients. Science Translational Medicine, 2017, 9(407), eaam7621. doi: 10.1126/scitranslmed.aam7621
  10. Planken, S.; Behenna, D.C.; Nair, S.K.; Johnson, T.O.; Nagata, A.; Almaden, C.; Bailey, S.; Ballard, T.E.; Bernier, L.; Cheng, H. et al. Discovery of N-((3R, 4R)-4-fluoro-1-(6-((3-methoxy-1-methyl-1H-pyrazol-4-yl) amino)-9-methyl-9H-purin-2-yl) pyrrolidine-3-yl) acrylamide (PF-06747775) Through Structure-Based Drug Design; ... Journal of Medicinal Chemistry, 2017, 60(7), 3002–3019. doi: 10.1021/acs.jmedchem.6b01894
  11. Zhou, Y.; Li, W.; Wang, M.; Zhang, X.; Zhang, H.; Tong, X.; Xiao, Y. Competitive profiling of celastrol targets in human cervical cancer HeLa cells via quantitative chemical proteomics. Molecular BioSystems, 2017, 13(1), 83–91. doi: 10.1039/c6mb00691d
  12. Butler, C.R.; Beck, E.M.; Harris, A.R.; Huang, Z.; McAllister, L.A.; Am Ende, C.W.; Fennell, K.F.; Foley, T.L.; Fonseca, K.R.; Hawrylik, S.J.; Johnson, D.S.; Knafels, J.D.; Mente, S.; Noell, S.; Pandit, J.; Phillips, T.B.; Piro, J.R.; Rogers, B.N.; Samad, T.A.; Wang, J.; Wan, S.; Brodney, M.A. Azetidine and Piperidine Carbamates as Efficient, Covalent Inhibitors of Monoacylglycerol Lipase. Journal of Medicinal Chemistry, 2017, 60(23), 9860–9873. doi: 10.1021/acs.jmedchem.7b01531
  13. Zuhl, A.M.; Nolan, C.E.; Brodney, M.A.; Niessen, S.; Atchison, K.; Houle, C.; Karanian, D.A.; Ambroise, Cl.; Brulet, J.W.; Beck, E.M.; Doran, S.D.; O'Neill, B.T.; am Ende, C.W.; Chang, C.; Geoghegan, K.F.; West, G.M.; Judkins, J.C.; Hou, X.; Riddell, D.R.; Johnson, D.S. Chemoproteomic profiling reveals that cathepsin D off-target activity drives ocular toxicity of β-secretase inhibitors. Nature communications, 2016, 7, 13042. doi: 10.1038/ncomms13042
  14. Rana, S.; Blowers, E.C.; Tebbe, C.; Contreras, J.I.; Radhakrishnan, P.; Kizhake, S.; Zhou, T.; Rajule, R.N.; Arnst, J.L.; Munkarah, A.R.; Rattan, R.; Natarajan, A. Isatin Derived Spirocyclic Analogues with α-Methylene-γ-butyrolactone as Anticancer Agents: A Structure-Activity Relationship Study. Journal of Medicinal Chemistry, 2016, 59(10), 5121–5127. doi: 10.1021/acs.jmedchem.6b00400
  15. Zhou, Y.; Li, W.; Xiao, Y. Profiling of Multiple Targets of Artemisinin Activated by Hemin in Cancer Cell Proteome. ACS Chemical Biology, 2016, 11(4), 882–888. doi: 10.1021/acschembio.5b01043
  16. Nusshold, C.; Üllen, A.; Kogelnik, N.; Bernhart, E.; Reicher, H.; Plastira, I.; Glasnov, T.; Zangger, K.; Rechberger, G.; Kollroser, M.; Fauler, G.; Wolinski, H.; Weksler, B.B.; Romero, I.A.; Kohlwein, S.D.; Couraud, P.-O.; Malle, E.; Sattler, W. Assessment of electrophile damage in a human brain endothelial cell line utilizing a clickable alkyne analogue of 2-chlorohexadecanal. Free Radical Biology and Medicine, 2016, 90, 59–74. doi: 10.1016/j.freeradbiomed.2015.11.010
  17. Li, W.; Zhou, Y.; Tang, G.; Xiao, Y. Characterization of the Artemisinin Binding Site for Translationally Controlled Tumor Protein (TCTP) by Bioorthogonal Click Chemistry. Bioconjugate Chemistry, 2016, 27(12), 2828–2833. doi: 10.1021/acs.bioconjchem.6b00556
  18. Mahmoodi, M.M.; Rashidian, M.; Zhang, Y.; Distefano, M.D. Application of meta- and para- Phenylenediamine as Enhanced Oxime Ligation Catalysts for Protein Labeling, PEGylation, Immobilization, and Release. Current Protocols in Protein Science, 2015, 79, 15.4.1–15.4.28. doi: 10.1002/0471140864.ps1504s79
  19. Jia, L.; Chisari, M.; Maktabi, M.H.; Sobieski, C.; Zhou, H.; Konopko, A.M.; Martin, B.R.; Mennerick, S.J.; Blumer, K.J. A Mechanism Regulating G Protein-coupled Receptor Signaling That Requires Cycles of Protein Palmitoylation and Depalmitoylation. Journal of Biological Chemistry, 2014, 289(9), 6249–6257. doi: 10.1074/jbc.m113.531475
  20. Zhou, Y.; Guo, T.; Li, X.; Dong, Y.; Galatsis, P.; Johnson, D.S.; Pan, Z. Discovery of selective 2,4-diaminopyrimidine-based photoaffinity probes for glyoxalase I. Medicinal Chemistry Communications, 2014, 5(3), 352–357. doi: 10.1039/c3md00286a
  21. Zhou, Y.; Guo, T.; Tang, G.; Wu, H.; Wong, N.-K.; Pan, Z. Site-Selective Protein Immobilization by Covalent Modification of GST Fusion Proteins. Bioconjugate Chemistry, 2014, 25(11), 1911-1915. doi: 10.1021/bc500347b

TAMRA азид, 6-изомер

  1. Zhang, S.; Spiegelman, N.A.; Lin, H. Global Profiling of Sirtuin Deacylase Substrates Using a Chemical Proteomic Strategy and Validation by Fluorescent Labeling. Methods in Molecular Biology, 2019, 2009, 137–147. doi: 10.1007/978-1-4939-9532-5_11
  2. Tang, G.; Liu, L.; Wang, X.; Pan, Z. Discovery of 7H-pyrrolo[2,3-d]pyrimidine derivatives as selective covalent irreversible inhibitors of interleukin-2-inducible T-cell kinase (Itk). European Journal of Medicinal Chemistry, 2019, 173, 167–183. doi: 10.1016/j.ejmech.2019.03.055
  3. Eelen, G.; Dubois, C.; Cantelmo, A.R.; Goveia, J.; Brüning, U.; DeRan, M.; Jarugumilli, G.; van Rijssel, J.; Saladino, G.; Comitani, F.; Zecchin, A.; Rocha, S.; Chen, R.; Huang, H.; Vandekeere, S.; Kalucka, J.; Lange, C.; Morales-Rodriguez, F.; Cruys, B.; Treps, L.; Ramer, L.; Vinckier, S.; Brepoels, K.; Wyns, S.; Souffreau, J.; Schoonjans, L.; Lamers, W.H.; Wu, Y.; Haustraete, J.; Hofkens, J.; Liekens, S.; Cubbon, R.; Ghesquière, B.; Dewerchin, M.; Gervasio, F.L.; Li, X.; van Buul, J.D.; Wu, X.; Carmeliet, P. Role of glutamine synthetase in angiogenesis beyond glutamine synthesis. Nature, 2018, 561(7721), 63–69. doi: 10.1038/s41586-018-0466-7
  4. Li, W.; Zhou, Y.; Tang, G.; Wong, N.-K.; Yang, M.; Tan, D.; Xiao, Y. Chemoproteomics Reveals the Anti-proliferative Potential of Parkinson's Disease Kinase Inhibitor LRRK2-IN-1 by Targeting PCNA Protein. Molecular Pharmaceutics, 2018, 15(8), 3252–3259. doi: 10.1021/acs.molpharmaceut.8b00325
  5. Nemmara, V.J.; Subramanian, V.; Muth, A.; Mondal, S.; Salinger, A.J.; Maurais, A.J.; Tilvawala, R.; Weerapana, E.; Thompson, P.R. The Development of Benzimidazole-Based Clickable Probes for the Efficient Labeling of Cellular Protein Arginine Deiminases (PADs). ACS Chemical Biology, 2018, 13(3), 712–722. doi: 10.1021/acschembio.7b00957
  6. Zhou, Y.; Li, W.; Wang, M.; Zhang, X.; Zhang, H.; Tong, X.; Xiao, Y. Competitive profiling of celastrol targets in human cervical cancer HeLa cells via quantitative chemical proteomics. Molecular BioSystems, 2017, 13(1), 83–91. doi: 10.1039/c6mb00691d
  7. Butler, C.R.; Beck, E.M.; Harris, A.R.; Huang, Z.; McAllister, L.A.; Am Ende, C.W.; Fennell, K.F.; Foley, T.L.; Fonseca, K.R.; Hawrylik, S.J.; Johnson, D.S.; Knafels, J.D.; Mente, S.; Noell, S.; Pandit, J.; Phillips, T.B.; Piro, J.R.; Rogers, B.N.; Samad, T.A.; Wang, J.; Wan, S.; Brodney, M.A. Azetidine and Piperidine Carbamates as Efficient, Covalent Inhibitors of Monoacylglycerol Lipase. Journal of Medicinal Chemistry, 2017, 60(23), 9860–9873. doi: 10.1021/acs.jmedchem.7b01531
  8. Zuhl, A.M.; Nolan, C.E.; Brodney, M.A.; Niessen, S.; Atchison, K.; Houle, C.; Karanian, D.A.; Ambroise, Cl.; Brulet, J.W.; Beck, E.M.; Doran, S.D.; O'Neill, B.T.; am Ende, C.W.; Chang, C.; Geoghegan, K.F.; West, G.M.; Judkins, J.C.; Hou, X.; Riddell, D.R.; Johnson, D.S. Chemoproteomic profiling reveals that cathepsin D off-target activity drives ocular toxicity of β-secretase inhibitors. Nature communications, 2016, 7, 13042. doi: 10.1038/ncomms13042
  9. Zhou, Y.; Li, W.; Xiao, Y. Profiling of Multiple Targets of Artemisinin Activated by Hemin in Cancer Cell Proteome. ACS Chemical Biology, 2016, 11(4), 882–888. doi: 10.1021/acschembio.5b01043
  10. Li, W.; Zhou, Y.; Tang, G.; Xiao, Y. Characterization of the Artemisinin Binding Site for Translationally Controlled Tumor Protein (TCTP) by Bioorthogonal Click Chemistry. Bioconjugate Chemistry, 2016, 27(12), 2828–2833. doi: 10.1021/acs.bioconjchem.6b00556
  11. Mahmoodi, M.M.; Rashidian, M.; Zhang, Y.; Distefano, M.D. Application of meta- and para- Phenylenediamine as Enhanced Oxime Ligation Catalysts for Protein Labeling, PEGylation, Immobilization, and Release. Current Protocols in Protein Science, 2015, 79, 15.4.1–15.4.28. doi: 10.1002/0471140864.ps1504s79
  12. Jia, L.; Chisari, M.; Maktabi, M.H.; Sobieski, C.; Zhou, H.; Konopko, A.M.; Martin, B.R.; Mennerick, S.J.; Blumer, K.J. A Mechanism Regulating G Protein-coupled Receptor Signaling That Requires Cycles of Protein Palmitoylation and Depalmitoylation. Journal of Biological Chemistry, 2014, 289(9), 6249–6257. doi: 10.1074/jbc.m113.531475
  13. Zhou, Y.; Guo, T.; Li, X.; Dong, Y.; Galatsis, P.; Johnson, D.S.; Pan, Z. Discovery of selective 2,4-diaminopyrimidine-based photoaffinity probes for glyoxalase I. Medicinal Chemistry Communications, 2014, 5(3), 352–357. doi: 10.1039/c3md00286a

TAMRA алкин, 5-изомер

  1. Rojas-Sánchez, L.; Sokolova, V.; Riebe, S.; Voskuhl, J.; Epple, M. Covalent Surface Functionalization of Calcium Phosphate Nanoparticles with Fluorescent Dyes by Copper-Catalysed and by Strain-Promoted Azide-Alkyne Click Chemistry. ChemNanoMat, 2019, 5(4), 436–446. doi: 10.1002/cnma.201800509

TAMRA алкин, 6-изомер

  1. Rink, W.M.; Thomas, F. Decoration of Coiled-Coil Peptides with N-Cysteine Peptide Thioesters As Cyclic Peptide Precursors Using Copper-Catalyzed Azide-Alkyne Cycloaddition (CuAAC) Click Reaction. Organic Letters, 2018, 20(23), 7493–7497. doi: 10.1021/acs.orglett.8b03261

TAMRA малеимид, 6-изомер

  1. Ast, J.; Arvaniti, A.; Fine, N.H.F.; Nasteska, D.; Ashford, F.B.; Stamataki, Z.M Koszegi, Z.; Bacon, A.; Trapp, S.; Jones, B.J.; Hastoy, B.; Tomas, A.; Reissaus, C.; Linnemann, A.K.; D'Este, E.; Calebiro, D.; Johnsson, K.; Podewin, T.; Broichhagen, J.; Hodson, D.J. LUXendins reveal endogenous glucagon-like peptide-1 receptor distribution and dynamics. bioRxiv, preprint. doi: 10.1101/557132

TFA-амино CPG 500

  1. Taskova, M.; Uhd, J.; Miotke, L.; Kubit, M.; Bell, J.; Ji, H.P.; Astakhova, K. Tandem Oligonucleotide Probe Annealing and Elongation To Discriminate Viral Sequence. Analytical Chemistry, 2017, 89(8), 4363–4366. doi: 10.1021/acs.analchem.7b00646

THPTA лиганд

  1. Yang, H.; Sukamtoh, E.; Du, Z.; Wang, W.; Ando, M.; Kwakwa, Y.N.; Zhang, J.; Zhang, G. Click chemistry approach to characterize curcumin-protein interactions in vitro and in vivo}. The Journal of Nutritional Biochemistry, 2019, 68, 1–6. doi: 10.1016/j.jnutbio.2019.02.010
  2. Wilder, L.M.; Fies, W.A.; Rabin, C.; Webb, L.J.; Crooks, R.M. Conjugation of an α-Helical Peptide to the Surface of Gold Nanoparticles. Langmuir, 2019, 35(9), 3363–3371. doi: 10.1021/acs.langmuir.9b00075

sulfo-Cyanine5 бис- NHS-эфир

  1. Pettersson, J.R.; Lanni, F.; Rule, G.S. Dual lifetimes for complexes between Glutathione-S-transferase (hGSTA1-1) and product-like ligands detected by single-molecule fluorescence imaging. Biochemistry, 2017, 56(31), 4073–4083. doi: 10.1021/acs.biochem.7b00030

Азидомасляной кислоты активированный эфир

  1. Hou, W.; Li, Y.; Kang, W.; Wang, X.; Wu, X.; Wang, S.; Liu, F. Real-time analysis of quantum dot labeled single porcine epidemic diarrhea virus moving along the microtubules using single particle tracking. Scientific Reports, 2019, 9, 1307. doi: 10.1038/s41598-018-37789-9
  2. Kuznetsov, A.E.; Komarova, N.V.; Kuznetsov, E.V.; Andrianova, M.S.; Grudtsov, V.P.; Rybachek, E.N.; Puchnin, K.V.; Ryazantsev, D.V.; Saurov, A.N. Integration of a field effect transistor-based aptasensor under a hydrophobic membrane for bioelectronic nose applications. Biosensors and Bioelectronics, 2019, 129, 29–35. doi: 10.1016/j.bios.2019.01.013
  3. Kumar, P.; Kuhlmann, F.M.; Chakroborty, S.; Bourgeois, A.L.; Foulke-Abel, J.; Tumala, B.; Vickers, T.J.; Sack, D.A.; DeNearing, B.; Harro, C.D.; Wright, W.S.; Gildersleeve, J.C.; Ciorba, M.A.; Santhanam, S.; Porter, C.K.; Gutierrez, R.L.; Prouty, M.G.; Riddle, M.S.; Polino, A.; Sheikh, A.; Donowitz, M.; Fleckenstein, J.M. Enterotoxigenic Escherichia coli blood group A interactions intensify diarrheal severity. The Journal of Clinical Investigation, 2018, 128(8), 3298–3311. doi: 10.1172/JCI97659
  4. Andrianova, M.; Komarova, N.; Grudtsov, V.; Kuznetsov, E.; Kuznetsov, A. Amplified Detection of the Aptamer-Vanillin Complex with the Use of Bsm DNA Polymerase. Sensors, 2018, 18, 49. doi: 10.3390/s18010049
  5. Kuznetsov, A.; Komarova, N.; Andrianova, M.; Grudtsov, V.; Kuznetsov, E. Aptamer based vanillin sensor using an ion-sensitive field-effect transistor. Microchimica Acta, 2018, 185(1), 3. doi: 10.1007/s00604-017-2586-4
  6. Taskova, M.; Uhd, J.; Miotke, L.; Kubit, M.; Bell, J.; Ji, H.P.; Astakhova, K. Tandem Oligonucleotide Probe Annealing and Elongation To Discriminate Viral Sequence. Analytical Chemistry, 2017, 89(8), 4363–4366. doi: 10.1021/acs.analchem.7b00646
  7. Bu, J.; Pilo, A.L.; McLuckey, S.A. Gas Phase Click Chemistry via Ion/Ion Reactions. International Journal of Mass Spectrometry, 2015, 390, 118–123. doi: 10.1016/j.ijms.2015.05.010
  8. Potapova, I.; Eglin, D.; Laschke, M.W.; Bischoff, M.; Richards, R.G.; Moriarty, T.F. Two-step labeling of Staphylococcus aureus with Lysostaphin-Azide and DIBO-Alexa using click chemistry. Journal of Microbiological Methods, 2013, 92(1), 90-98. doi: 10.1016/j.mimet.2012.11.004

Алкиновый амидит (5'-концевой)

  1. Farzan, V.M.; Kvach, M.V.; Aparin, I.O.; Kireev, D.E.; Prikazchikova, T.A.; Ustinov, A.V.; Shmanai, V.V.; Shipulin, G.A.; Korshun, V.A.; Zatsepin, T.S. Novel homo Yin-Yang probes improve sensitivity in RT-qPCR detection of low copy HIV RNA. Talanta, 2019, 194, 226–232. doi: 10.1016/j.talanta.2018.10.043
  2. Taskova, M.; Uhd, J.; Miotke, L.; Kubit, M.; Bell, J.; Ji, H.P.; Astakhova, K. Tandem Oligonucleotide Probe Annealing and Elongation To Discriminate Viral Sequence. Analytical Chemistry, 2017, 89(8), 4363–4366. doi: 10.1021/acs.analchem.7b00646
  3. Aparin, I.O.; Farzan, V.M.; Veselova, O.A.; Chistov, A.A.; Podkolzin, A.T.; Ustinov, A.V.; Shipulin, G.A.; Formanovsky, A.A.; Korshun, V.A.; Zatsepin, T.S. 1-Phenylethynylpyrene (PEPy) as a novel blue-emitting dye for qPCR assay. Analyst, 2016, 141, 1331–1338. doi: 10.1039/c5an01767j
  4. Astakhova, I.K.; Santhosh Kumar, T.; Campbell, M.A.; Ustinov, A.V.; Korshun, V.A.; Wengel, J. Branched DNA nanostructures efficiently stabilised and monitored by novel pyrene-perylene 2'-alpha-L-amino-LNA FRET pairs. Chemical Communications, 2013, 49(5), 511-511. doi: 10.1039/c2cc37547h

Амино-11-ddUTP

  1. Gaspar, I.; Wippich, F.; Ephrussi, A. Enzymatic production of single molecule FISH and RNA capture probes. RNA, 2017, 23(10), 1582–1591. doi: 10.1261/rna.061184.117

Аскорбиновая кислота

  1. Taskova, M.; Uhd, J.; Miotke, L.; Kubit, M.; Bell, J.; Ji, H.P.; Astakhova, K. Tandem Oligonucleotide Probe Annealing and Elongation To Discriminate Viral Sequence. Analytical Chemistry, 2017, 89(8), 4363–4366. doi: 10.1021/acs.analchem.7b00646
  2. Samuelsen, S.V.; Maity, A.; Nybo, M.; Macaubas, C.; Lønstrup, L.; Balboni, I.M.; Mellins, E.D.; Astakhova, K. Novel Phospholipid-Protein Conjugates Allow Improved Detection of Antibodies in Patients with Autoimmune Diseases. PLoS One, 2016, 11(6), e0156125. doi: 10.1371/journal.pone.0156125
  3. Li, Z.; Liu, Z.; Chen, Z.; Ju, E.; Li, W.; Ren, J.; Qu, X. Bioorthogonal chemistry for selective recognition, separation and killing bacteria over mammalian cells. Chemical Communications, 2016, 52(17), 3482–3485. doi: 10.1039/c5cc10625g
  4. Maity, A.; Macaubas, C.; Mellins, E.; Astakhova, K. Synthesis of Phospholipid-Protein Conjugates as New Antigens for Autoimmune Antibodies. Molecules, 2015, 20(6), 10253–10263. doi: 10.3390/molecules200610253

Биотин PEG3 азид

  1. Shen, Y.; Yang, S.; Hu, X.; Zhang, M.; Ma, X.; Wang, Z.; Hou, Y.; Bai, G. Natural product puerarin activates Akt and ameliorates glucose and lipid metabolism dysfunction in hepatic cells. Journal of Functional Foods, 2019, 55, 296–304. doi: 10.1016/j.jff.2019.02.035
  2. Wang, E.; Hunter, C.P. SID-1 Functions in Multiple Roles To Support Parental RNAi in Caenorhabditis elegans. Genetics, 2017, 207(2), 547–557. doi: 10.1534/genetics.117.300067
  3. Bruckman, M.A.; Czapar, A.E.; VanMeter, A.; Randolph, L.N.; Steinmetz, N.F. Tobacco mosaic virus-based protein nanoparticles and nanorods for chemotherapy delivery targeting breast cancer. Journal of Controlled Release, 2016, 231, 103–113. doi: 10.1016/j.jconrel.2016.02.045

Биотин алкин

  1. Rink, W.M.; Thomas, F. Decoration of Coiled-Coil Peptides with N-Cysteine Peptide Thioesters As Cyclic Peptide Precursors Using Copper-Catalyzed Azide-Alkyne Cycloaddition (CuAAC) Click Reaction. Organic Letters, 2018, 20(23), 7493–7497. doi: 10.1021/acs.orglett.8b03261
  2. Cui, X.-Y.; Sun, N.-N.; Xie, X.-N.; Sun, W.-C.; Zhao, Q.; Liu, N. Detection of Newly Synthesized Proteins via Metabolic Incorporation of Non-natural Amino Acid. Chinese Journal of Analytical Chemistry, 2018, 46(11), 1808–1813. doi: 10.1016/s1872-2040(18)61125-9
  3. Ullrich, M.; Liang, V.; Chew, Y.L.; Banister, S.; Song, X.; Zaw, T.; Lam, H.; Berber, S.; Kassiou, M.; Nicholas, H.R. et al. Bio-orthogonal labeling as a tool to visualize and identify newly synthesized proteins in Caenorhabditis elegans. Nature Protocols, 2014, 9(9), 2237-2255. doi: 10.1038/nprot.2014.150

ДБЦО активированный эфир

  1. Alshanski, I.; Blaszkiewicz, J.; Mervinetsky, E.; Rademann, J.; Yitzchaik, S.; Hurevich, M. Sulfation Patterns of Saccharides and Heavy Metal Ions Binding. Chemistry, in press. doi: 10.1002/chem.201901538

Диметилформамид для мечения

  1. Gu, R.; Oweida, T.; Yingling, Y.G.; Chilkoti, A.; Zauscher, S. Enzymatic synthesis of nucleobase-modified single-stranded DNA offers tunable resistance to nuclease degradation. Biomacromolecules, 2018, 19(8), 3525–3535. doi: 10.1021/acs.biomac.8b00816

Краситель Pico488 для определения концентрации дцДНК, 200x раствор в ДМСО

  1. Norred, S.E.; Dabbs, R.M.; Chauhan, G.; Caveney, P.M.; Collier, C.P.; Abel, S.M.; Simpson, M.L. Synergistic interactions between confinement and macromolecular crowding spatially order transcription and translation in cell-free expression. bioRxiv, preprint. doi: 10.1101/445544

Кумарин 343 азид

  1. Musiol-Kroll, E.M.; Zubeil, F.; Schafhauser, T.; Härtner, T.; Kulik, A.; McArthur, J.B.; Koryakina, I.; Wohlleben, W.; Grond, S.; Williams, G.J.; Lee, S.Y.; Weber, T. Polyketide bio-derivatization using the promiscuous acyltransferase KirCII. ACS Synthetic Biology, 2017, 6(3), 421–427. doi: 10.1021/acssynbio.6b00341
  2. Teske, N.S.; Voigt, J.; Shastri, V.P. Clickable Degradable Aliphatic Polyesters via Copolymerization with Alkyne Epoxy Esters: Synthesis and Postfunctionalization with Organic Dyes. Journal of the American Chemical Society, 2014, 136(29), 10527-10533. doi: 10.1021/ja505629w

Пентиновой кислоты активированный эфир (STP)

  1. Samuelsen, S.V.; Maity, A.; Nybo, M.; Macaubas, C.; Lønstrup, L.; Balboni, I.M.; Mellins, E.D.; Astakhova, K. Novel Phospholipid-Protein Conjugates Allow Improved Detection of Antibodies in Patients with Autoimmune Diseases. PLoS One, 2016, 11(6), e0156125. doi: 10.1371/journal.pone.0156125
  2. Maity, A.; Macaubas, C.; Mellins, E.; Astakhova, K. Synthesis of Phospholipid-Protein Conjugates as New Antigens for Autoimmune Antibodies. Molecules, 2015, 20(6), 10253–10263. doi: 10.3390/molecules200610253

Перилен азид

  1. Westergaard Mulberg, M.; Taskova, M.; Thomsen, R.P.; Okholm, A.H.; Kjems, J.; Astakhova, K. New Fluorescent Nanoparticles for Ultrasensitive Detection of Nucleic Acids by Optical Methods. Chembiochem, 2017, 18(16), 1599–1603. doi: 10.1002/cbic.201700125
  2. Okholm, A.; Kjems, J.; Astakhova, K. Fluorescence detection of natural RNA using rationally designed "clickable" oligonucleotide probes. RSC Advances, 2014, 4(86), 45653–45656. doi: 10.1039/c4ra07165d

Пирен азид 2

  1. Wanat, P.; Walczak, S.; Wojtczak, B.A.; Nowakowska, M.; Jemielity, J.; Kowalska, J. Ethynyl, 2-Propynyl, and 3-Butynyl C-Phosphonate Analogues of Nucleoside Di- and Triphosphates: Synthesis and Reactivity in CuAAC. Organic Letters, 2015, 17(12), 3062–3065. doi: 10.1021/acs.orglett.5b01346
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