Lumiprobe citation list

Here is a list of research publications citing use of Lumiprobe products, sorted by product.

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1-Ethynyl pyrene

  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

3-Ethynyl perylene

  1. Beri, D.; Jakoby, M.; Howard, I.A.; Busko, D.; Richards, B.S.; Turshatov, A. Improved photon absorption in dye-functionalized silicon nanocrystals synthesized via microwave-assisted hydrosilylation. Dalton Transactions, 2020, 49(7), 2290–2299. doi: 10.1039/c9dt04497c

AF488 NHS ester

  1. Huang, D.; Yue, F.; Qiu, J.; Deng, M.; Kuang, S. Polymeric nanoparticles functionalized with muscle-homing peptides for targeted delivery of phosphatase and tensin homolog inhibitor to skeletal muscle. Acta Biomaterialia, 2020, 118, 196–206. doi: 10.1016/j.actbio.2020.10.009

Alkyne NHS ester (hexynoic acid NHS ester)

  1. Kleinpenning, F.; Steigenberger, B.; Wu, W.; Heck, A.J.R. Fishing for newly synthesized proteins with phosphonate-handles. Nature Communications, 2020, 11, 3244. doi: 10.1038/s41467-020-17010-0

Alkyne Phosphoramidite, 5'-terminal

  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

Alkyne-PEG3-COOH

  1. Petrov, R.A.; Mefedova, S.R.; Yamansarov, E.Y.; Maklakova, S.Y.; Grishin, D.A.; Lopatukhina, E.V.; Burenina, O.Y.; Lopukhov, A.V.; Kovalev, S.V.; Timchenko, Y.V.; Ondar, E.E.; Ivanenkov, Y.A.; Evteev, S.A.; Vaneev, A.N.; Timoshenko, R.V.; Klyachko, N.L.; Erofeev, A.S.; Gorelkin, P.V.; Beloglazkina, E.K.; Majouga, A.G. New Small-Molecule Glycoconjugates of Docetaxel and GalNAc for Targeted Delivery to Hepatocellular Carcinoma. Molecular Pharmaceutics, 2021, 18(1), 461–468. doi: 10.1021/acs.molpharmaceut.0c00980

Amino-11-ddUTP

  1. Bakker, R.; Mani, M.; Carthew, R.W. The Wg and Dpp morphogens regulate gene expression by modulating the frequency of transcriptional bursts. bioRxiv, preprint. doi: 10.1101/2020.01.24.918623
  2. Boersma, S.; Rabouw, H.H.; Bruurs, L.J.M.; Pavlovič, T.; van Vliet, A.L.W.; Beumer, J.; Clevers, H.; van Kuppeveld, F.J.M.; Tanenbaum, M.E. Translation and Replication Dynamics of Single RNA Viruses. Cell, 2020, 183(7), 1930–1945.e23. doi: 10.1016/j.cell.2020.10.019
  3. Yu, Y.; Guo, Y.; Tian, Q.; Lan, Y.; Yeh, H.; Zhang, M.; Tasan, I.; Jain, S.; Zhao, H. An efficient gene knock-in strategy using 5'-modified double-stranded DNA donors with short homology arms. Nature Chemical Biology, 2020, 16(4), 387–390. doi: 10.1038/s41589-019-0432-1
  4. Hampoelz, B.; Schwarz, A.; Ronchi, P.; Bragulat-Teixidor, H.; Tischer, C.; Gaspar, I.; Ephrussi, A.; Schwab, Y.; Beck, M. Nuclear Pores Assemble from Nucleoporin Condensates During Oogenesis. Cell, 2019, 179, 671–686.e17. doi: 10.1016/j.cell.2019.09.022
  5. Wang, S. Single Molecule RNA FISH smFISH in Whole-Mount Mouse Embryonic Organs. Current Protocols in Cell Biology, 2019, 83(1), e79. doi: 10.1002/cpcb.79
  6. 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

Ascorbic acid

  1. Novopashina, D.S.; Vorobyeva, M.A.; Lomzov, A.A.; Silnikov, V.N.; Venyaminova, A.G. Terminal Mono- and Bis-Conjugates of Oligonucleotides with Closo-Dodecaborate: Synthesis and Physico-Chemical Properties. International Journal of Molecular Sciences, 2021, 22(1), 182. doi: 10.3390/ijms22010182
  2. Jandl, B.; Sedghiniya, S.; Carstens, A.; Astakhova, K. Peptide–Fluorophore Hydrogel as a Signal Boosting Approach in Rapid Detection of Cancer DNA. ACS Omega, 2019, 4(9), 13889–13895. doi: 10.1021/acsomega.9b01586
  3. 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
  4. 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
  5. 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
  6. 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

Azide-PEG3-Azide

  1. Hull, S.M.; Lindsay, C.D.; Brunel, L.G.; Shiwarski, D.J.; Tashman, J.W.; Roth, J.G.; Myung, D.; Feinberg, A.W.; Heilshorn, S.C. 3D Bioprinting using UNIversal Orthogonal Network (UNION) Bioinks. Advanced Functional Materials, 2021, 31(7), 2007983. doi: 10.1002/adfm.202007983
  2. Tolentino, M.Q.; Hartmann, A.K.; Loe, D.T.; Rouge, J.L. Controlled release of small molecules and proteins from DNA-surfactant stabilized metal organic frameworks. Journal of Materials Chemistry B, 2020, 8(26), 5627–5635. doi: 10.1039/d0tb00767f

Azidobutyric acid NHS ester

  1. Wang, Y.; Yao, J.; Cai, L.; Liu, T.; Wang, X.; Zhang, Y.; Zhou, Z.; Li, T.; Liu, M.; Lai, R.; Liu, X. Bone-targeted extracellular vesicles from mesenchymal stem cells for osteoporosis therapy. Research Square, preprint. doi: 10.21203/rs.3.rs-18279/v1
  2. Kleinpenning, F.; Steigenberger, B.; Wu, W.; Heck, A.J.R. Fishing for newly synthesized proteins with phosphonate-handles. Nature Communications, 2020, 11, 3244. doi: 10.1038/s41467-020-17010-0
  3. Blanchard, A.T.; Bazrafshan, A.S.; Yi, J.; Eisman, J.T.; Yehl, K.M.; Bian, T.; Mugler, A.; Salaita, K. Highly Polyvalent DNA Motors Generate 100+ pN of Force via Autochemophoresis. Nano Letters, 2019, 19(10), 6977–6986. doi: 10.1021/acs.nanolett.9b02311
  4. 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
  5. 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
  6. 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
  7. 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
  8. 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
  9. 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
  10. 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
  11. 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

BDP 558/568 NHS ester

  1. Best, Q.A.; Haack, R.A.; Swift, K.M.; Bax, B.M.; Tetin, S.Y.; Hershberger, S.J. A Rainbow of Acridinium Chemiluminescence. Luminescence, in press. doi: 10.1002/bio.4038
  2. Nechaeva, N.L.; Sorokina, O.N.; Konstantinova, T.S.; Vasilyeva, A.D.; Yurina, L.V.; Byzova, N.A.; Bugrova, A.E.; Yanovich, S.V.; Eremenko, A.V.; Kurochkin, I.N. Simultaneous express immunoassay of multiple cardiac biomarkers with an automatic platform in human plasma. Talanta, 2021, 224, 121860. doi: 10.1016/j.talanta.2020.121860
  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

BDP 558/568 carboxylic acid

  1. Kochappan, R.; Cao, E.; Han, S.; Hu, L.; Quach, T.; Senyschyn, D.; Ferreira, V.I.; Lee, G.; Leong, N.; Sharma, G.; Lim, S.F.; Nowell, C.J.; Chen, Z.; von Andrian, U.H.; Bonner, D.; Mintern, J.D.; Simpson, J.S.; Trevaskis, N.L.; Porter, C.J.H. Targeted delivery of mycophenolic acid to the mesenteric lymph node using a triglyceride mimetic prodrug approach enhances gut-specific immunomodulation in mice. Journal of Controlled Release, in press. doi: 10.1016/j.jconrel.2021.02.008

BDP 581/591 NHS ester

  1. Brachi, G.; Ruiz-Ramírez, J.; Dogra, P.; Wang, Z.; Cristini, V.; Ciardelli, G.; Rostomily, R.C.; Ferrari, M.; Mikheev, A.M.; Blanco, E.; Mattu, C. Intratumoral injection of hydrogel-embedded nanoparticles enhances retention in glioblastoma. Nanoscale, 2020, 12(46), 23838–23850. doi: 10.1039/d0nr05053a
  2. 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 X NHS ester

  1. Grätz, L.; Tropmann, K.; Bresinsky, M.; Müller, C.; Bernhardt, G.; Pockes, S. NanoBRET binding assay for histamine H2 receptor ligands using live recombinant HEK293T cells. Scientific Reports, 2020, 10, 13288. doi: 10.1038/s41598-020-70332-3
  2. Gruber, C.G.; Pegoli, A.; Müller, C.; Grätz, L.; She, X.; Keller, M. Differently fluorescence-labelled dibenzodiazepinone-type muscarinic acetylcholine receptor ligands with high M2R affinity. RSC Medicinal Chemistry, 2020, 11(7), 823–832. doi: 10.1039/D0MD00137F
  3. Zhong, X.; Shtukenberg, A.G.; Liu, M.; Olson, I.A.; Weck, M.; Ward, M.D.; Kahr, B. Dislocation Generation by Microparticle Inclusions. Crystal Growth & Design, 2019, 19(11), 6649–6655. doi: 10.1021/acs.cgd.9b01041

BDP 630/650 amine

  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 carboxylic acid

  1. Pfister, J.; Lichius, A.; Summer, D.; Haas, H.; Kanagasundaram, T.; Kopka, K.; Decristoforo, C. Live-cell imaging with Aspergillus fumigatus-specific fluorescent siderophore conjugates. Scientific Reports, 2020, 10, 15519. doi: 10.1038/s41598-020-72452-2
  2. 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 DBCO

  1. Merlo, R.; Caprioglio, D.; Cillo, M.; Valenti, A.; Mattossovich, R.; Morrone, C.; Massarotti, A.; Rossi, F.; Miggiano, R.; Leonardi, A.; Minassi, A.; Perugino, G. The SNAP-tag technology revised: an effective chemo-enzymatic approach by using a universal azide-based substrate. Journal of Enzyme Inhibition and Medicinal Chemistry, 2021, 36(1), 85–97. doi: 10.1080/14756366.2020.1841182
  2. Islam, M.R.; Nguy, C.; Pandit, S.; Lyon, L.A. Design and Synthesis of Core–Shell Microgels with One‐Step Clickable Crosslinked Cores and Ultralow Crosslinked Shells. Macromolecular Chemistry and Physics, 2020, 221(19), 2000156. doi: 10.1002/macp.202000156

BDP FL NHS ester

  1. Best, Q.A.; Haack, R.A.; Swift, K.M.; Bax, B.M.; Tetin, S.Y.; Hershberger, S.J. A Rainbow of Acridinium Chemiluminescence. Luminescence, in press. doi: 10.1002/bio.4038
  2. González, M.I.; González-Arjona, M.; Santos-Coquillat, A.; Vaquero, J.; Vázquez-Ogando, E.; de Molina, A.; Peinado, H.; Desco, M.; Salinas, B. Covalently Labeled Fluorescent Exosomes for In Vitro and In Vivo Applications. Biomedicines, 2021, 9, 81. doi: 10.3390/biomedicines9010081
  3. Volz, J.; Kusch, C.; Beck, S.; Popp, M.; Vögtle, T.; Meub, M.; Scheller, I.; Heil, H.S.; Preu, J.; Schuhmann, M.K.; Hemmen, K.; Premsler, T.; Sickmann, A.; Heinze, K.G.; Stegner, D.; Stoll, G.; Braun, A.; Sauer, M.; Nieswandt, B. BIN2 orchestrates platelet calcium signaling in thrombosis and thrombo-inflammation. Journal of Clinical Investigation, 2020, 130(11), 6064–6079. doi: 10.1172/JCI136457
  4. Susnik, E.; Taladriz-Blanco, P.; Drasler, B.; Balog, S.; Petri-Fink, A.; Rothen-Rutishauser, B. Increased Uptake of Silica Nanoparticles in Inflamed Macrophages but Not upon Co-Exposure to Micron-Sized Particles. Cells, 2020, 9(9), 2099. doi: 10.3390/cells9092099
  5. FitzGerald, L.I.; Aurelio, L.; Chen, M.; Yuen, D.; Rennick, J.J.; Graham, B.; Johnston, A.P.R. A molecular sensor to quantify the localization of proteins, DNA and nanoparticles in cells. Nature Communications, 2020, 11(1), 4482. doi: 10.1038/s41467-020-18082-8
  6. Pereira de Sousa, I.; Gourmel, C.; Berkovska, O.; Burger, M.; Leroux, J.-C. A microparticulate based formulation to protect therapeutic enzymes from proteolytic digestion: phenylalanine ammonia lyase as case study. Scientific Reports, 2020, 10, 3651. doi: 10.1038/s41598-020-60463-y
  7. Viegas, A.; Dollinger, P.; Verma, N.; Kubiak, J.; Viennet, T.; Seidel, C.A.M.; Gohlke, H.; Etzkorn, M.; Kovacic, F.; Jaeger, K.-E. Structural and dynamic insights revealing how lipase binding domain MD1 of Pseudomonas aeruginosa foldase affects lipase activation. Scientific Reports, 2020, 10, 3578. doi: 10.1038/s41598-020-60093-4
  8. Korevaar, P.A.; Kaplan, C.N.; Grinthal, A.; Rust, R.M.; Aizenberg, J. Non-equilibrium signal integration in hydrogels. Nature Communications, 2020, 11, 386. doi: 10.1038/s41467-019-14114-0
  9. Martin, C.; Brachet, G.; Colas, C.; Allard-Vannier, E.; Kizlik-Masson, C.; Esnault, C.; Respaud, R.; Denevault-Sabourin, C.; Chourpa, I.; Gouilleux-Gruart, V.; Viaud-Massuard, M.-C.; Joubert, N. In Vitro Characterization and Stability Profiles of Antibody-Fluorophore Conjugates Derived from Interchain Cysteine Cross-Linking or Lysine Bioconjugation. Pharmaceuticals, 2019, 12(4), 176. doi: 10.3390/ph12040176
  10. Simpson, J.D.; Ediriweera, G.R.; Howard, C.B.; Fletcher, N.L.; Bell, C.A.; Thurecht, K.J. Polymer design and component selection contribute to uptake, distribution & trafficking behaviours of polyethylene glycol hyperbranched polymers in live MDA-MB-468 breast cancer cells. Biomaterials Science, 2019, 7(11), 4661–4674. doi: 10.1039/c9bm00957d
  11. Lee, S.A.; Biteen, J.S. Spectral Reshaping of Single Dye Molecules Coupled to Single Plasmonic Nanoparticles. Journal of Physical Chemistry Letters, 2019, 10, 5764–5769. doi: 10.1021/acs.jpclett.9b02480
  12. 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, 2019, 14(8), 1800640. doi: 10.1002/biot.201800640
  13. 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
  14. 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
  15. 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
  16. 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
  17. Bond, M.J.; Bleiler, M.; Harrison, L.E.; Scocchera, E.W.; Nakanishi, M.; G-Dayanandan, N.; Keshipeddy, S.; Rosenberg, D.W.; Wright, D.L.; Giardina, C. Spindle assembly disruption and cancer cell apoptosis with a CLTC-binding compound. Molecular Cancer Research, 2018, 16(9), 1361–1372. doi: 10.1158/1541-7786.MCR-18-0178
  18. 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
  19. 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
  20. 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
  21. 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
  22. 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
  23. 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
  24. 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
  25. 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 alkyne

  1. Abukar, T.; Rahmani, S.; Thompson, N.K.; Antonescu, C.N.; Wakarchuk, W.W. Development of BODIPY labelled sialic acids as sialyltransferase substrates for direct detection of terminal galactose on N- and O-linked glycans. Carbohydrate Research, 2021, 500, 108249. doi: 10.1016/j.carres.2021.108249
  2. Merlo, R.; Caprioglio, D.; Cillo, M.; Valenti, A.; Mattossovich, R.; Morrone, C.; Massarotti, A.; Rossi, F.; Miggiano, R.; Leonardi, A.; Minassi, A.; Perugino, G. The SNAP-tag technology revised: an effective chemo-enzymatic approach by using a universal azide-based substrate. Journal of Enzyme Inhibition and Medicinal Chemistry, 2021, 36(1), 85–97. doi: 10.1080/14756366.2020.1841182
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BDP FL amine

  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, 2019, 11(24), 11484–11495. doi: 10.1039/c9nr00989b

BDP FL azide

  1. Rodríguez-Hakim, M.; Anand, S.; Tajuelo, J.; Yao, Z.; Kannan, A.; Fuller, G.G. Asphaltene-induced spontaneous emulsification: Effects of interfacial co-adsorption and viscoelasticity. Journal of Rheology, 2020, 64(4), 799–816. doi: 10.1122/1.5145307
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BDP FL carboxylic acid

  1. Ridolfo, R.; Tavakoli, S.; Junnuthula, V.; Williams, D.S.; Urtti, A.; van Hest, J.C.M. Exploring the impact of morphology on the properties of biodegradable nanoparticles and their diffusion in complex biological medium. Biomacromolecules, 2021, 22(1), 126–133. doi: 10.1021/acs.biomac.0c00726
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BDP FL hydrazide

  1. Roloff, A.; Nirmalananthan-Budau, N.; Rühle, B.; Borcherding, H.; Thiele, T.; Schedler, U.; Resch-Genger, U. Quantification of Aldehydes on Polymeric Microbead Surfaces via Catch and Release of Reporter Chromophores. Analytical Chemistry, 2019, 91(14), 8827–8834. doi: 10.1021/acs.analchem.8b05515
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BDP FL maleimide

  1. Koch, S.; Seinen, A.-B.; Kamel, M.; Kuckla, D.; Monzel, C.; Kedrov, A.; Driessen, A.J.M. Single-molecule analysis of dynamics and interactions: of the SecYEG translocon. FEBS Journal, in press. doi: 10.1111/febs.15596
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  4. 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
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BDP R6G NHS ester

  1. Lee, S.A.; Biteen, J.S. Spectral Reshaping of Single Dye Molecules Coupled to Single Plasmonic Nanoparticles. Journal of Physical Chemistry Letters, 2019, 10, 5764–5769. doi: 10.1021/acs.jpclett.9b02480

BDP R6G alkyne

  1. Zhang, C.T.; Liu, Y.; Wang, X.; Wang, X.; Kolle, S.; Balazs, A.C.; Aizenberg, J. Patterning non-equilibrium morphologies in stimuli-responsive gels through topographical confinement. Soft Matter, 2020, 16(6), 1463–1472. doi: 10.1039/c9sm02221j

BDP TMR maleimide

  1. Gusev, I.D.; Firsov, A.M.; Chertkova, R.V.; Kotova, E.A.; Dolgikh, D.A.; Kirpichnikov, M.P.; Antonenko, Y.N. Study of Interaction of Fluorescent Cytochrome C with Liposomes, Mitochondria, and Mitoplasts by Fluorescence Correlation Spectroscopy. Russian Journal of Bioorganic Chemistry, 2020, 46(6), 1162–1171. doi: 10.1134/S1068162020060084

BDP TR NHS ester

  1. Best, Q.A.; Haack, R.A.; Swift, K.M.; Bax, B.M.; Tetin, S.Y.; Hershberger, S.J. A Rainbow of Acridinium Chemiluminescence. Luminescence, in press. doi: 10.1002/bio.4038

Biotin PEG3 azide

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Biotin alkyne

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Copper(II)-TBTA complex, 10 mM in 55% aq. DMSO

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Coumarin 343 X NHS ester

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Coumarin 343 azide

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Cyanine2 NHS ester minimal dye

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Cyanine3 tetrazine

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Cyanine3.5 NHS ester

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Cyanine3.5 azide

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Cyanine3.5 carboxylic acid

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Cyanine5 DBCO

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Cyanine5 NHS ester

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Cyanine5.5 azide

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Cyanine5.5 carboxylic acid

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Cyanine5.5 hydrazide

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Cyanine5.5 maleimide

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Cyanine7 DBCO

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Cyanine7 NHS ester

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Cyanine7 amine

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Cyanine7 azide

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Cyanine7 carboxylic acid

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Cyanine7 hydrazide

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Cyanine7 maleimide

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Cyanine7.5 NHS ester

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Cyanine7.5 alkyne

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Cyanine7.5 amine

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Cyanine7.5 azide

  1. Hellyer, S.D.; Aggarwal, S.; Chen, A.N.; Leach, K.; Lapinsky, D.J.; Gregory, K.J. Development of Clickable Photoaffinity Ligands for Metabotropic Glutamate Receptor 2 Based on Two Positive Allosteric Modulator Chemotypes. ACS Chemical Neuroscience, 2020, 11(11), 1597–1609. doi: 10.1021/acschemneuro.0c00009
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  6. 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 carboxylic acid

  1. Nie, T.; He, Z.; Zhu, J.; Chen, K.; Howard, G.P.; Pacheco-Torres, J.; Minn, I.; Zhao, P.; Bhujwalla, Z.M.; Mao, H.-Q.; Liu, L.; Chen, Y. Non-invasive delivery of levodopa-loaded nanoparticles to the brain via lymphatic vasculature to enhance treatment of Parkinson's disease. Nano Research, in press. doi: 10.1007/s12274-020-3280-0
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  14. 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
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Cyanine7.5 hydrazide

  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 maleimide

  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

DBCO NHS ester

  1. Adams, M.R.; Moody, C.T.; Sollinger, J.L.; Brudno, Y. Extracellular Matrix-Anchored Click Motifs for Specific Tissue Targeting. Molecular Pharmaceutics, 2020, 17(2), 392–403. doi: 10.1021/acs.molpharmaceut.9b00589
  2. Alshanski, I.; Blaszkiewicz, J.; Mervinetsky, E.; Rademann, J.; Yitzchaik, S.; Hurevich, M. Sulfation Patterns of Saccharides and Heavy Metal Ions Binding. Chemistry, 2019, 25(52), 12083–12090. doi: 10.1002/chem.201901538
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DMF (dimethylformamide), labeling grade

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DMS(O)MT aminolink C6

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EdU (5-ethynyl-2'-deoxyuridine)

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FAM NHS ester, 6-isomer

  1. Sasaki, K.; Harada, M.; Yoshikawa, T.; Tagawa, H.; Harada, Y.; Yonemitsu, Y.; Ryujin, T.; Kishimura, A.; Mori, T.; Katayama, Y. Fc-Binding Antibody-Recruiting Molecules Targeting Prostate-Specific Membrane Antigen: Defucosylation of Antibody for Efficacy Improvement. ChemRxiv, preprint. doi: 10.26434/chemrxiv.12654602.v1
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  4. Pinals, R.L.; Yang, D.; Lui, A.; Cao, W.; Landry, M.P. Corona exchange dynamics on carbon nanotubes by multiplexed fluorescence monitoring. Journal of the American Chemical Society, 2020, 142(3), 1254–1264. doi: 10.1021/jacs.9b09617
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  7. 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 Phosphoramidite, 6-Isomer

  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

FAM alkyne, 5-isomer

  1. Guarin, M.; Faelens, R.; Giusti, A.; De Croze, N.; Léonard, M.; Cabooter, D.; Annaert, P.; de Witte, P.; Ny, A. Spatiotemporal Imaging and Pharmacokinetic of Fluorescent Compounds in Zebrafish Eleuthero-Embryos After Different Routes of Administration. Research Square, preprint. doi: 10.21203/rs.3.rs-237483/v1
  2. Sokolova, V.; Mekky, G.; van der Meer, S.B.; Seeds, M.C.; Atala, A.J.; Epple, M. Transport of ultrasmall gold nanoparticles (2 nm) across the blood-brain barrier in a six-cell brain spheroid model. Scientific Reports, 2020, 10, 18033. doi: 10.1038/s41598-020-75125-2
  3. Warminski, M.; Kowalska, J.; Jemielity, J. Solid-Phase Synthesis of RNA 5'-Azides and Their Application for Labeling, Ligation, and Cyclization Via Click Chemistry. Current Protocols in Nucleic Acid Chemistry, 2020, 82(1), e112. doi: 10.1002/cpnc.112
  4. Sokolova, V.; Nzou, G.; van der Meer, S.B.; Ruks, T.; Heggen, M.; Loza, K.; Hagemann, N.; Murke, F.; Giebel, B.; Hermann, D.M.; Atala, A.J.; Epple, M. Ultrasmall gold nanoparticles (2 nm) can penetrate and enter cell nuclei in an in vitro 3D brain spheroid model. Acta Biomaterialia, 2020, 111, 349–362. doi: 10.1016/j.actbio.2020.04.023
  5. Rojas-Sánchez, L.; Loza, K.; Epple, M. Synthesis and intracellular tracing surface-functionalized calcium phosphate nanoparticles by super-resolution microscopy (STORM). Materialia, 2020, 12, 100773. doi: 10.1016/j.mtla.2020.100773
  6. Synakewicz, M.; Bauer, D.; Rief, M.; Itzhaki, L.S. Bioorthogonal protein-DNA conjugation methods for force spectroscopy. Scientific Reports, 2019, 9, 13820. doi: 10.1038/s41598-019-49843-1
  7. van der Meer, S.B.; Loza, K.; Wey, K.; Heggen, M.; Beuck, C.; Bayer, P.; Epple, M. Click Chemistry on the Surface of Ultrasmall Gold Nanoparticles (2 nm) for Covalent Ligand Attachment Followed by NMR Spectroscopy , 2019, 35(22), 7191–7204. doi: 10.1021/acs.langmuir.9b00295
  8. 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
  9. 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
  10. 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
  11. 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
  12. 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
  13. 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
  14. 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 alkyne, 6-isomer

  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 azide, 5-isomer

  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. Gueiderikh, A.; Maczkowiak-Chartois, F.; Rouvet, G.; Souquère-Besse, S.; Apcher, S.; Diaz, J.-J.; Rosselli, F. Fanconi anemia A protein participates in nucleolar homeostasis maintenance and ribosome biogenesis. Science Advances, 2021, 7(1), eabb5414. doi: 10.1126/sciadv.abb5414
  3. Ramey-Ward, A.N.; Su, H.; Salaita, K. Mechanical stimulation of adhesion receptors using light-responsive nanoparticle actuators enhances myogenesis. ACS Applied Materials & Interfaces, 2020, 12(32), 35903–35917. doi: 10.1021/acsami.0c08871
  4. Kim, D.; Singh, N.; Waldemer-Streyer, R.J.; Yoon, M.-S.; Chen, J. Muscle-derived TRAIL negatively regulates myogenic differentiation. Experimental Cell Research, 2020, 394(1), 112165. doi: 10.1016/j.yexcr.2020.112165
  5. Pink, M.; Verma, N.; Schmitz-Spanke, S. Benchmark dose analyses of toxic endpoints in lung cells provide sensitivity and toxicity ranking across metal oxide nanoparticles and give insights into the mode of action. Toxicology Letters, 2020, 331, 218–226. doi: 10.1016/j.toxlet.2020.06.012
  6. Nozeret, K.; Boucharlat, A.; Agou, F.; Buddelmeijer, N. A sensitive fluorescence-based assay to monitor enzymatic activity of the essential integral membrane protein Apolipoprotein N-acyltransferase (Lnt). Scientific Reports, 2019, 9, 15978. doi: 10.1038/s41598-019-52106-8
  7. Synakewicz, M.; Bauer, D.; Rief, M.; Itzhaki, L.S. Bioorthogonal protein-DNA conjugation methods for force spectroscopy. Scientific Reports, 2019, 9, 13820. doi: 10.1038/s41598-019-49843-1
  8. Son, K.; You, J.-S.; Yoon, M.-S.; Dai, C.; Kim, J.H.; Khanna, N.; Banerjee, A.; Martinis, S.A.; Han, G.; Han, J.M.; Kim, S.; Chen, J. Nontranslational function of leucyl-tRNA synthetase regulates myogenic differentiation and skeletal muscle regeneration. Journal of Clinical Investigation, 2019, 130, 2088–2093. doi: 10.1172/JCI122560
  9. 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
  10. 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
  11. 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
  12. 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
  13. 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
  14. 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
  15. 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
  16. 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
  17. 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
  18. 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
  19. 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
  20. 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
  21. 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
  22. 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
  23. 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 azide, 6-isomer

  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. Ramey-Ward, A.N.; Su, H.; Salaita, K. Mechanical stimulation of adhesion receptors using light-responsive nanoparticle actuators enhances myogenesis. ACS Applied Materials & Interfaces, 2020, 12(32), 35903–35917. doi: 10.1021/acsami.0c08871
  3. Reed, S.A.; Brzovic, D.A.; Takasaki, S.S.; Boyko, K.V.; Antos, J.M. Efficient Sortase-Mediated Ligation Using a Common C-Terminal Fusion Tag. Bioconjugate Chemistry, 2020, 31(5), 1463–1473. doi: 10.1021/acs.bioconjchem.0c00156
  4. Morais, C.M.; Cunha, P.P.; Melo, T.; Cardoso, A.M.; Domingues, P.; Domingues, M.R.; Pedroso de Lima, M.C.; Jurado, A.S. Glucosylceramide synthase silencing combined with the receptor tyrosine kinase inhibitor axitinib as a new multimodal strategy for glioblastoma. Human Molecular Genetics, 2019, 28(21), 3664–3679. doi: 10.1093/hmg/ddz152
  5. 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
  6. 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
  7. 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
  8. 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
  9. 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 maleimide, 6-isomer

  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. Sauer, F.; Klemm, T.; Kollampally, R.B.; Tessmer, I.; Nair, R.K.; Popov, N.; Kisker, C. Differential Oligomerization of the Deubiquitinases USP25 and USP28 Regulates Their Activities. Molecular Cell, 2019, 74(3), 421–435.e10. doi: 10.1016/j.molcel.2019.02.029
  3. 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

JOE azide, 5- isomer

  1. Taskova, M.; Astakhova, K. Fluorescent Oligonucleotides with Bis(prop-2-yn-1-yloxy)butane-1,3-diol Scaffold Rapidly Detect Disease-Associated Nucleic Acids. Bioconjugate Chemistry, 2019, 30(12), 3007–3012. doi: 10.1021/acs.bioconjchem.9b00746
  2. 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

PEP azide

  1. Taskova, M.; Astakhova, K. Fluorescent Oligonucleotides with Bis(prop-2-yn-1-yloxy)butane-1,3-diol Scaffold Rapidly Detect Disease-Associated Nucleic Acids. Bioconjugate Chemistry, 2019, 30(12), 3007–3012. doi: 10.1021/acs.bioconjchem.9b00746

Pentynoic acid STP ester

  1. Antonov, S.A.; Novosadova, E.V.; Kobylansky, A.G.; Tarantul, V.Z.; Grivennikov, I.A. A Hybrid Detection Method Based on Peroxidase-mediated Signal Amplification and Click Chemistry for Highly Sensitive Background-free Immunofluorescent Staining. Journal of Histochemistry & Cytochemistry, 2019, 67(10), 771–782. doi: 10.1369/0022155419864113
  2. Jandl, B.; Sedghiniya, S.; Carstens, A.; Astakhova, K. Peptide–Fluorophore Hydrogel as a Signal Boosting Approach in Rapid Detection of Cancer DNA. ACS Omega, 2019, 4(9), 13889–13895. doi: 10.1021/acsomega.9b01586
  3. 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
  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

Perylene azide

  1. Taskova, M.; Astakhova, K. Fluorescent Oligonucleotides with Bis(prop-2-yn-1-yloxy)butane-1,3-diol Scaffold Rapidly Detect Disease-Associated Nucleic Acids. Bioconjugate Chemistry, 2019, 30(12), 3007–3012. doi: 10.1021/acs.bioconjchem.9b00746
  2. 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
  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

Pico488 dsDNA quantification reagent, 200x solution in DMSO

  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
  2. Morozov, V.N.; Kolyvanova, M.A.; Dement'eva, O.V.; Rudoy, V.M.; Kuzmin, V.A. Comparison of quenching efficacy of SYBR green I and picoGreen fluorescence by ultrasmall gold nanoparticles in isotropic and liquid-crystalline DNA systems. Journal of Molecular Liquids, 2021, 321, 114751. doi: 10.1016/j.molliq.2020.114751
  3. Cuccaro, A.; De Marchi, L.; Oliva, M.; Sanches, M.V.; Freitas, R.; Casu, V.; Monni, G.; Miragliotta, V.; Pretti, C. Sperm quality assessment in Ficopomatus enigmaticus (Fauvel, 1923): Effects of selected organic and inorganic chemicals across salinity levels. Ecotoxicology and Environmental Safety, 2021, 207, 111219. doi: 10.1016/j.ecoenv.2020.111219
  4. Covarrubias-Zambrano, O.; Shrestha, T.B.; Pyle, M.; Montes-Gonzalez, M.L.; Troyer, D.L.; Bossmann, S.H. Development of a gene delivery system composed of a cell penetrating peptide and a nontoxic polymer. ACS Applied Bio Materials, 2020, 3(11), 7418–7427. doi: 10.1021/acsabm.0c00561
  5. Kosmider, B.; Lin, C.-R.; Karim, L.; Tomar, D.; Vlasenko, L.; Marchetti, N.; Bolla, S.; Madesh, M.; Criner, G.J.; Bahmed, K. Mitochondrial dysfunction in human primary alveolar type II cells in emphysema. EBioMedicine, 2019, 46, 305–316. doi: 10.1016/j.ebiom.2019.07.063
  6. Pantelidou, C.; Sonzogni, O.; De Oliveria Taveira, M.; Mehta, A.K.; Kothari, A.; Wang, D.; Visal, T.; Li, M.K.; Pinto, J.; Castrillon, J.A.; Cheney, E.M.; Bouwman, P.; Jonkers, J.; Rottenberg, S.; Guerriero, J.L.; Wulf, G.M.; Shapiro, G.I. PARP Inhibitor Efficacy Depends on CD8+ T-cell Recruitment via Intratumoral STING Pathway Activation in BRCA-Deficient Models of Triple-Negative Breast Cancer. Cancer Discovery, 2019, 9(6), 722–737. doi: 10.1158/2159-8290.CD-18-1218

ProteOrange protein quantification reagent, 500x

  1. Berditchevskii, G.M.; Vasina, L.V.; Ageev, S.V.; Meshcheriakov, A.A.; Galkin, M.A.; Ishmukhametov, R.R.; Nashchekin, A.V.; Kirilenko, D.A.; Petrov, A.V.; Martynova, S.D.; Semenov, K.N.; Sharoyko, V.V. A comprehensive study of biocompatibility of detonation nanodiamonds. Journal of Molecular Liquids. doi: 10.1016/j.molliq.2021.115763

Pyrene azide 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

R110 azide, 5- isomer

  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 azide, 6- isomer

  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

R6G alkyne, 6-isomer

  1. Guarin, M.; Faelens, R.; Giusti, A.; De Croze, N.; Léonard, M.; Cabooter, D.; Annaert, P.; de Witte, P.; Ny, A. Spatiotemporal Imaging and Pharmacokinetic of Fluorescent Compounds in Zebrafish Eleuthero-Embryos After Different Routes of Administration. Research Square, preprint. doi: 10.21203/rs.3.rs-237483/v1
  2. Gao, F.; Hunter, A.; Qu, S.; Hoffman, J.R.; Gao, P.; Phillip, W.A. Interfacial Junctions Control Electrolyte Transport Through Charge-Patterned Membranes. ACS Nano, 2019, 13(7), 7655–7664. doi: 10.1021/acsnano.9b00780

ROX NHS ester, 5-isomer

  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 NHS ester, 6- isomer

  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 azide, 5- isomer

  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
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ROX reference dye for qPCR

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Sulfo-Cyanine3 NHS ester

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Sulfo-Cyanine3 alkyne

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Sulfo-Cyanine3 amine

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Sulfo-Cyanine3 azide

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Sulfo-Cyanine5 bis-NHS ester

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Sulfo-Cyanine5 carboxylic acid

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Sulfo-Cyanine5 maleimide

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Sulfo-Cyanine5.5 NHS ester

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Sulfo-Cyanine5.5 alkyne

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Sulfo-Cyanine5.5 amine

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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
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Sulfo-Cyanine5.5 carboxylic acid

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Sulfo-Cyanine5.5 maleimide

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Sulfo-Cyanine7 NHS ester

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Sulfo-Cyanine7 amine

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Sulfo-Cyanine7 carboxylic acid

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Sulfo-Cyanine7.5 NHS ester

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Sulfo-Cyanine7.5 carboxylic acid

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TAMRA alkyne, 5-isomer

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TAMRA alkyne, 6-isomer

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TAMRA azide, 5-isomer

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  10. 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
  11. 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
  12. 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
  13. 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
  14. 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
  15. 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
  16. 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
  17. 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
  18. 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
  19. 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
  20. 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
  21. 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
  22. 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
  23. 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
  24. 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
  25. 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
  26. 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
  27. 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
  28. 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 azide, 6-isomer

  1. Chen, X.; Xu, J.; Wong, N.-K.; Zhong, S.; Yang, M.; Liu, Z.; Lu, Y.; Li, W.; Zhou, Y. Chemoproteomic profiling of cobalamin-independent methionine synthases in plant with a covalent probe. Journal of Agricultural and Food Chemistry, 2020, 68(30), 8050–8056. doi: 10.1021/acs.jafc.0c03301
  2. Xu, Y.; Deng, Z.; Shi, Y.; Chen, X.; Xu, J.; Zhong, S.; Xiao, Y.; Wong, N.-K.; Zhou, Y. Molecular Imaging and In Situ Quantitative Profiling of Fatty Acid Synthase with a Chemical Probe. Analytical Chemistry, 2020, 92(6), 4419–4426. doi: 10.1021/acs.analchem.9b05327
  3. 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
  4. 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
  5. 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
  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. 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
  9. 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
  10. 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
  11. 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
  12. 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
  13. 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
  14. 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
  15. 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 maleimide, 6-isomer

  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. Sagert, L.; Hennig, F.; Thomas, C.; Tampé, R. A loop structure allows TAPBPR to exert its dual function as MHC I chaperone and peptide editor. eLife, 2020, 9, e55326. doi: 10.7554/eLife.55326
  3. Ast, J.; Arvaniti, A.; Fine, N.H.F.; Nasteska, D.; Ashford, F.B.; Stamataki, Z.; Koszegi, Z.; Bacon, A.; Jones, B.J.; Lucey, M.A.; Sasaki, S.; Brierley, D.I.; Hastoy, B.; Tomas, A.; D'Agostino, G.; Reimann, F.; Lynn, F.C.; Reissaus, C.A.; Linnemann, A.K.; D'Este, E.; Calebiro, D.; Trapp, S.; Johnsson, K.; Podewin, T.; Broichhagen, J.; Hodson, D.J. Super-resolution microscopy compatible fluorescent probes reveal endogenous glucagon-like peptide-1 receptor distribution and dynamics. Nature Communications, 2020, 11, 467. doi: 10.1038/s41467-020-14309-w

TFA-Amino modifier 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 ligand

  1. Rudack, T.; Teuber, C.; Scherlo, M.; Güldenhaupt, J.; Schartner, J.; Lübben, M.; Klare, J.P.; Gerwert, K.; Kötting, C. The Ras Dimer Structure. ChemRxiv, preprint. doi: 10.26434/chemrxiv.14039810.v1
  2. Wilder, L.M. Handali, P.R.; Webb, L.J.; Crooks, R.M. Interactions between Oligoethylene Glycol-Capped AuNPs and Attached Peptides Control Peptide Structure. Bioconjugate Chemistry, 2020, 31(10), 2383–2391. doi: 10.1021/acs.bioconjchem.0c00447
  3. Ramey-Ward, A.N.; Su, H.; Salaita, K. Mechanical stimulation of adhesion receptors using light-responsive nanoparticle actuators enhances myogenesis. ACS Applied Materials & Interfaces, 2020, 12(32), 35903–35917. doi: 10.1021/acsami.0c08871
  4. Hahn, F.; Niesar, A.; Wangen, C.; Wild, M.; Grau, B.; Herrmann, L.; Capci, A.; Adrait, A.; Couté, Y.; Tsogoeva, S.B.; Marschall, M. Target verification of artesunate-related antiviral drugs: assessing the role of mitochondrial and regulatory proteins by click chemistry and fluorescence labeling. Antiviral Research, 2020, 180, 104861. doi: 10.1016/j.antiviral.2020.104861
  5. Kleinpenning, F.; Steigenberger, B.; Wu, W.; Heck, A.J.R. Fishing for newly synthesized proteins with phosphonate-handles. Nature Communications, 2020, 11, 3244. doi: 10.1038/s41467-020-17010-0
  6. Zhou, J.; Wang, W.; Zhang, J.; Du, Z.; Yang, H.; Zhang, G. Click chemistry-based imaging to study tissue distribution of curcumin-protein complex in mice. Food & Function, 2020, 11(2), 1684–1691. doi: 10.1039/c9fo02012h
  7. Wang, Y.; Dattmore, D.A.; Wang, W:; Pohnert, G.; Wolfram, S.; Zhang, J.; Yang, R.; Decker, E.A.; Lee, K.S.S.; Zhang, G. trans, trans-2,4-decadienal, a lipid peroxidation product, induces inflammatory responses via Hsp90- or 14–3-3ζ-dependent mechanisms. Journal of Nutritional Biochemistry, 2020, 76, 108286. doi: 10.1016/j.jnutbio.2019.108286
  8. Sundah, N.R.; Ho, N.R.Y.; Lim, G.S.; Natalia, A.; Ding, X.; Liu, Y.; Seet, J.E.; Chan, C.W.; Loh, T.P.; Shao, H. Barcoded DNA nanostructures for the multiplexed profiling of subcellular protein distribution. Nature Biomedical Engineering, 2019, 3(9), 684–694. doi: 10.1038/s41551-019-0417-0
  9. 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
  10. 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

dsGreen Gel Staining Solution, 10000×

  1. Chetverikov, P.E.; Craemer, C.; Cvrković, T.; Klimov, P.B.; Petanović, R.U.; Romanovich, A.E.; Sukhareva, S.I.; Zukoff, S.N.; Bolton, S.; Amrine, J. Molecular phylogeny of the phytoparasitic mite family Phytoptidae (Acariformes: Eriophyoidea) identified the female genitalic anatomy as a major macroevolutionary factor and revealed multiple origins of gall induction. Experimental & Applied Acarology, 2021, 83(1), 31–68. doi: 10.1007/s10493-020-00571-6
  2. Chetverikov, P.E.; Cvrković, T.; Efimov, P.G.; Klimov, P.B.; Petanović, R.U.; Romanovich, A.E.; Schubert, M.A.; Sukhareva, S.I.; Zukoff, S.N.; Amrine, J. Molecular phylogenetic analyses reveal a deep dichotomy in the conifer-inhabiting genus Trisetacus (Eriophyoidea: Nalepellidae), with the two lineages differing in their female genital morphology and host associations. Experimental and Applied Acarology, 2020, 81(3), 287–316. doi: 10.1007/s10493-020-00503-4
  3. Kirkham, C.M.; Scott, J.N.F.; Wang, X.; Smith, A.L.; Kupinski, A.P.; Ford, A.M.; Westhead, D.R.; Stockley, P.G.; Tuma, R.; Boyes, J. Cut-and-Run: A Distinct Mechanism by which V(D)J Recombination Causes Genome Instability. Molecular Cell, 2019, 74(3), 584–597.e9. doi: 10.1016/j.molcel.2019.02.025
  4. 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
  5. 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
  6. 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
  7. 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
  8. 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
  9. 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
  10. 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

dsGreen for Real-Time PCR, 100×

  1. Carter, J.G.; Iturbe, L.O.; Duprey, J.-L.H.A.; Carter, I.R.; Southern, C.D.; Rana, M.; Bosworth, A. Sub-5-minute Detection of SARS-CoV-2 RNA using a Reverse Transcriptase-Free Exponential Amplification Reaction, RTF-EXPAR. medRxiv, preprint. doi: 10.1101/2020.12.31.20248236
  2. Fang, Y.; Coulter, J.A.; Wu, J.; Liu, L.; Li, X.; Dong, Y.; Ma, L.; Pu, Y.; Sun, B.; Niu, Z.; Jin, J.; Zhao, Y.; Mi, W.; Xu, Y.; Sun, W. Identification of differentially expressed genes involved in amino acid and lipid accumulation of winter turnip rape (Brassica rapa L.) in response to cold stress. PloS ONE, 2021, 16(2), e0245494. doi: 10.1371/journal.pone.0245494
  3. Morozov, V.N.; Kolyvanova, M.A.; Dement'eva, O.V.; Rudoy, V.M.; Kuzmin, V.A. Comparison of quenching efficacy of SYBR green I and picoGreen fluorescence by ultrasmall gold nanoparticles in isotropic and liquid-crystalline DNA systems. Journal of Molecular Liquids, 2021, 321, 114751. doi: 10.1016/j.molliq.2020.114751
  4. Bitarishvili, S. V. and Bondarenko, V. S. and Geras'kin, S. A. Expression of Gibberelline Biosynthesis and Catabolism Genes in the Embryos of γ-Irradiated Barley Seeds. Biology Bulletin, 2020, 47(11), 1558–1563. doi: 10.1134/S1062359020110059
  5. Sapozhnikova, Y.P.; Koroleva, A.G.; Yakhnenko, V.M.; Tyagun, M.L.; Glyzina, O.Y.; Coffin, A.B.; Makarov, M.M.; Shagun, A.N.; Kulikov, V.A.; Gasarov, P.V.; Kirilchik, S.V.; Klimenkov, I.V.; Sudakov, N.P.; Anoshko, P.N.; Kurashova, N.A.; Sukhanova, L.V. Molecular and cellular responses to long-term sound exposure in peled (Coregonus peled). Journal of the Acoustical Society of America, 2020, 148(2), 895–907. doi: 10.1121/10.0001674
  6. Thompson, T.A.; Touré, M.B.; Sanogo, D.; Shaffer, J.G.; Doumbia, S.O.; Krogstad, D.J. Template copy number and the sensitivity of quantitative PCR for Plasmodium falciparum in asymptomatic individuals. Malaria Journal, 2020, 19, 295. doi: 10.1186/s12936-020-03365-8
  7. Garafutdinov, R.R.; Gilvanov, A.R.; Kupova, O.Y.; Sakhabutdinova, A.R. Effect of metal ions on isothermal amplification with Bst exo- DNA polymerase. International Journal of Biological Macromolecules, 2020, 161, 1447–1455. doi: 10.1016/j.ijbiomac.2020.08.028
  8. Sakhabutdinova, A.R.; Chemeris, A.V.; Garafutdinov, R.R. Enhancement of PCR efficiency using mono- and disaccharides. Analytical Biochemistry, 2020, 606, 113858. doi: 10.1016/j.ab.2020.113858
  9. Garafutdinov, R.R.; Sakhabutdinova, A.R.; Kupryushkin, M.S.; Pyshnyi, D.V. Data on multimerization efficiency for short linear DNA templates and phosphoryl guanidine primers during isothermal amplification with Bst exo- DNA polymerase. Data in Brief, 2020, 29, 105188. doi: 10.1016/j.dib.2020.105188
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sulfo-Cyanine3 DBCO

  1. Tugel, U.; Casas, M.G.; Wiltschi, B. Site-Specific Incorporation of Non-canonical Amino Acids by Amber Stop Codon Suppression in Escherichia coli. Peptide and Protein Engineering (Springer Protocols Handbooks), 2020, 267–281. doi: 10.1007/978-1-0716-0720-6_14
  2. Desai, B.J.; Gonzalez, R.L. Multiplexed genomic encoding of non-canonical amino acids for labeling large complexes. Nature Chemical Biology, 2020, 16, 1129–1135. doi: 10.1038/s41589-020-0599-5

sulfo-Cyanine5 DBCO

  1. Lim, S.; Kim, W.; Song, S.; Shim, M.K.; Yoon, H.Y.; Kim, B.-S.; Kwon, I.C.; Kim, K. Intracellular Uptake Mechanism of Bioorthogonally Conjugated Nanoparticles on Metabolically Engineered Mesenchymal Stem Cells. Bioconjugate Chemistry, 2021, 32(1), 199–214. doi: 10.1021/acs.bioconjchem.0c00640
  2. Desai, B.J.; Gonzalez, R.L. Multiplexed genomic encoding of non-canonical amino acids for labeling large complexes. Nature Chemical Biology, 2020, 16, 1129–1135. doi: 10.1038/s41589-020-0599-5
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