Tailored Bioorthogonal and Bioconjugate Chemistry: A Source of Inspiration for Developing Kinetic Target-Guided Synthesis Strategies
Open accessAbstract
Kinetic target-guided synthesis (KTGS) is a promising tool for the discovery of biologically active compounds. It relies on the identification of potent ligands that are covalently assembled by the biological targets themselves from a pool of reagents. Significant effort is devoted to developing new KTGS strategies; however, only a handful of biocompatible reactions are available, which may be insufficient to meet the specificities (stability, dynamics, active site topology, etc.) of a wide range of biological targets with therapeutic potential. This Topical Review proposes a retrospective analysis of existing KTGS ligation tools, in terms of their kinetics and analogy with other biocompatible reactions, and provides new clues to expand the KTGS toolkit. By way of examples, a nonexhaustive selection of such chemical ligation tools belonging to different classes of reactions as promising candidate reactions for KTGS are suggested.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Currently there are limited methods to selectively covalently bind to a protein.
“Currently there are limited methods to selectively covalently bind to a protein56–58”
From PROTAC targeted protein degraders: the past is prologue (2022) · cites this paper as [58]
Cites
Tornøe, C. W., Christensen, C., & Meldal, M. (2002) · The Journal of Organic Chemistry · doi:10.1021/jo011148j · Cited by 8,696 · see citing works
Agard, N. J., Prescher, J. A., & Bertozzi, C. R. (2004) · Journal of the American Chemical Society · doi:10.1021/ja044996f · Cited by 3,026 · see citing works
Rowan, S. J., Cantrill, S., Cousins, G. R. L., Sanders, J. K. M., & Stoddart, J. F. (2002) · Angewandte Chemie International Edition · doi:10.1002/1521-3773(20020315)41:6 · Cited by 2,599 · see citing works
Tetrazine Ligation: Fast Bioconjugation Based on Inverse-Electron-Demand Diels−Alder Reactivity
Blackman, M. L., Royzen, M., & Fox, J. M. (2008) · Journal of the American Chemical Society · doi:10.1021/ja8053805 · Cited by 1,691 · see citing works
A ‘Rule of Three’ for fragment-based lead discovery?
Congreve, M., Carr, R. A. E., Murray, C. W., & Jhoti, H. (2003) · Drug Discovery Today · doi:10.1016/s1359-6446(03)02831-9 · Cited by 1,365 · see citing works
The Use of Esters of N-Hydroxysuccinimide in Peptide Synthesis
Anderson, G. W., Zimmerman, J. E., & Callahan, F. M. (1964) · Journal of the American Chemical Society · doi:10.1021/ja01063a037 · Cited by 1,241 · see citing works
Inverse electron demand Diels–Alder reactions in chemical biology
Oliveira, B. L., Guo, Z., & Bernardes, G. J. L. (2017) · Chemical Society Reviews · doi:10.1039/c7cs00184c · Cited by 1,149 · see citing works
Advances in Chemical Protein Modification
Boutureira, O., & Bernardes, G. J. L. (2015) · Chemical Reviews · doi:10.1021/cr500399p · Cited by 1,137 · see citing works
Ruthenium-Catalyzed Cycloaddition of Alkynes and Organic Azides
Zhang, L., Chen, X., Xue, P., Sun, H. H. Y., Williams, I. D., Sharpless, K. B., Fokin, V. V., & Jia, G. (2005) · Journal of the American Chemical Society · doi:10.1021/ja054114s · Cited by 1,124 · see citing works
Twenty years on: the impact of fragments on drug discovery
Erlanson, D. A., Fesik, S. W., Hubbard, R. E., Jahnke, W., & Jhoti, H. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.109 · Cited by 1,000 · see citing works
The 1,2,3-triazole ring as a bioisostere in medicinal chemistry
Bonandi, E., Christodoulou, M. S., Fumagalli, G., Perdicchia, D., Rastelli, G., & Passarella, D. (2017) · Drug Discovery Today · doi:10.1016/j.drudis.2017.05.014 · Cited by 753 · see citing works
[12] Dansyl chloride procedure
Gray, W. R. (1967) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(67)11014-8 · Cited by 652 · see citing works
Weber, G. (1952) · Biochemical Journal · doi:10.1042/bj0510155 · Cited by 616 · see citing works
Koniev, O., & Wagner, A. (2015) · Chemical Society Reviews · doi:10.1039/c5cs00048c · Cited by 600 · see citing works
Bioconjugation with Strained Alkenes and Alkynes
Debets, M. F., van Berkel, S. S., Dommerholt, J., Dirks, A. J., Rutjes, F. P. J. T., & van Delft, F. L. (2011) · Accounts of Chemical Research · doi:10.1021/ar200059z · Cited by 565 · see citing works
Bioconjugation with Maleimides: A Useful Tool for Chemical Biology
Ravasco, J. M. J. M., Faustino, H., Trindade, A. F., & Góis, P. M. P. (2018) · Chemistry - A European Journal · doi:10.1002/chem.201803174 · Cited by 525 · see citing works
In Situ Click Chemistry: Enzyme Inhibitors Made to Their Own Specifications
Manetsch, R., Krasiński, A., Radić, Z., Raushel, J., Taylor, P., Sharpless, K. B., & Kolb, H. C. (2004) · Journal of the American Chemical Society · doi:10.1021/ja046382g · Cited by 424 · see citing works
Functionalized Cyclopropenes As Bioorthogonal Chemical Reporters
Patterson, D. M., Nazarova, L. A., Xie, B. J., Kamber, D. N., & Prescher, J. A. (2012) · Journal of the American Chemical Society · doi:10.1021/ja3060436 · Cited by 371 · see citing works
Sun, X., Stabler, C. L., Cazalis, C. S., & Chaikof, E. L. (2005) · Bioconjugate Chemistry · doi:10.1021/bc0502311 · Cited by 353 · see citing works
Presolski, S. I., Hong, V., Cho, S., & Finn, M. G. (2010) · Journal of the American Chemical Society · doi:10.1021/ja105743g · Cited by 348 · see citing works
Freeze-frame inhibitor captures acetylcholinesterase in a unique conformation.
Bourne, Y., Kolb, H., Radić, Z., Sharpless, K., Taylor, P., & Marchot, P. (2004) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0308206100 · Cited by 296 · see citing works
Darko, A. K., Wallace, S., Dmitrenko, O., Machovina, M. M., Mehl, R. A., Chin, J. W., & Fox, J. M. (2014) · Chemical Science · doi:10.1039/c4sc01348d · Cited by 284 · see citing works
Mock, W. L., Irra, T. A., Wepsiec, J. P., & Adhya, M. (1989) · The Journal of Organic Chemistry · doi:10.1021/jo00283a024 · Cited by 265 · see citing works
Covalent Modification of Biomolecules through Maleimide-Based Labeling Strategies
Renault, K., Fredy, J. W., Renard, P., & Sabot, C. (2018) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.8b00252 · Cited by 264 · see citing works
Self-citationCycloaddition induced by cucurbituril. A case of Pauling principle catalysis
Mock, W. L., Irra, T. A., Wepsiec, J. P., & Manimaran, T. (1983) · The Journal of Organic Chemistry · doi:10.1021/jo00168a070 · Cited by 254 · see citing works
Design and Development of Molecular Imaging Probes
Chen, K., & Chen, X. (2010) · Current Topics in Medicinal Chemistry · doi:10.2174/156802610791384225 · Cited by 231 · see citing works
Precise small-molecule recognition of a toxic CUG RNA repeat expansion
Rzuczek, S. G., Colgan, L. A., Nakai, Y., Cameron, M. D., Furling, D., Yasuda, R., & Disney, M. D. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2251 · Cited by 205 · see citing works
Liu, F., Liang, Y. F., & Houk, K. N. (2017) · Accounts of Chemical Research · doi:10.1021/acs.accounts.7b00265 · Cited by 202 · see citing works
Murray, C. W., & Verdonk, M. L. (2002) · Journal of Computer-Aided Molecular Design · doi:10.1023/a:1022446720849 · Cited by 201 · see citing works
Simple Methods and Rational Design for Enhancing Aptamer Sensitivity and Specificity
Kalra, P., Dhiman, A., Cho, W. C. S., Bruno, J. G., & Sharma, T. K. (2018) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2018.00041 · Cited by 184 · see citing works
Kim, W. G., Kang, M. E., Lee, J. B., Jeon, M. H., Lee, S., Lee, J., Choi, B., Cal, P. M. S. D., Kang, S., Kee, J., et al. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b06338 · Cited by 176 · see citing works
Visualizing biologically active small molecules in cells using click chemistry
Cañeque, T., Müller, S., & Rodriguez, R. (2018) · Nature Reviews Chemistry · doi:10.1038/s41570-018-0030-x · Cited by 176 · see citing works
1,2,4-Triazines Are Versatile Bioorthogonal Reagents
Kamber, D. N., Liang, Y. F., Blizzard, R. J., Liu, F., Mehl, R. A., Houk, K. N., & Prescher, J. A. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b05100 · Cited by 163 · see citing works
Jeon, B., Wang, S., Ruszczycky, M. W., & Liu, H. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00578 · Cited by 156 · see citing works
Structure-based design and analysis of SuFEx chemical probes
Jones, L. H., & Kelly, J. W. (2020) · RSC Medicinal Chemistry · doi:10.1039/c9md00542k · Cited by 136 · see citing works
Li, Q., Dong, T., Liu, X., & Lei, X. (2013) · Journal of the American Chemical Society · doi:10.1021/ja401989p · Cited by 133 · see citing works
Stabilization of cysteine-linked antibody drug conjugates with N-aryl maleimides
Christie, R. J., Fleming, R. L., Bezabeh, B. Z., Woods, R., Mao, S., Harper, J. W., Joseph, A., Wang, Q., Xu, Z., Wu, H., et al. (2015) · Journal of Controlled Release · doi:10.1016/j.jconrel.2015.09.032 · Cited by 132 · see citing works
Yang, J., Liang, Y. F., Šečkutė, J., Houk, K. N., & Devaraj, N. K. (2014) · Chemistry - A European Journal · doi:10.1002/chem.201304225 · Cited by 128 · see citing works
Goddard, D. R., & Michaelis, L. (1935) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)74993-4 · Cited by 127 · see citing works
Cysteine‐Selective Phosphonamidate Electrophiles for Modular Protein Bioconjugations
Kasper, M., Glanz, M., Stengl, A., Penkert, M., Klenk, S., Sauer, T., Schumacher, D., Helma, J., Krause, E., Cardoso, M. C., et al. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201814715 · Cited by 111 · see citing works
A Genetically Encoded Acrylamide Functionality
Lee, Y., Wu, B., Raymond, J. E., Zeng, Y., Fang, X., Wooley, K. L., & Liu, W. R. (2013) · ACS Chemical Biology · doi:10.1021/cb400267m · Cited by 107 · see citing works
Heteroatom‐embedded Medium‐Sized Cycloalkynes: Concise Synthesis, Structural Analysis, and Reactions
Ni, R., Mitsuda, N., Kashiwagi, T., Igawa, K., & Tomooka, K. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201409910 · Cited by 107 · see citing works
Sydnone–alkyne cycloaddition: applications in synthesis and bioconjugation
Decuypère, E., Plougastel, L., Audisio, D., & Taran, F. (2017) · Chemical Communications · doi:10.1039/c7cc06405e · Cited by 103 · see citing works
Merkx, R., Brouwer, A. J., Rijkers, D. T. S., & Liskamp, R. M. J. (2005) · Organic Letters · doi:10.1021/ol0501119 · Cited by 92 · see citing works
Kinetics and mechanisms of the aminolysis of N-hydroxysuccinimide esters in aqueous buffers
Cline, G. W., & Hanna, S. B. (1988) · The Journal of Organic Chemistry · doi:10.1021/jo00250a031 · Cited by 91 · see citing works
Panda, D., Saha, P., Das, T., & Dash, J. (2017) · Nature Communications · doi:10.1038/ncomms16103 · Cited by 77 · see citing works
Hu, X., Sun, J., Wang, H., & Manetsch, R. (2008) · Journal of the American Chemical Society · doi:10.1021/ja802683u · Cited by 76 · see citing works
Entropic Contribution to the Linking Coefficient in Fragment Based Drug Design: A Case Study
Borsi, V., Calderone, V., Fragai, M., Luchinat, C., & Sarti, N. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm901723z · Cited by 74 · see citing works
Matos, M. J., Navo, C. D., Hakala, T. A., Ferhati, X., Guerreiro, A., Hartmann, D., Bernardim, B., Saar, K. L., Compañón, I., Corzana, F., et al. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201901405 · Cited by 72 · see citing works
Tuning the Diels–Alder Reaction for Bioconjugation to Maleimide Drug-Linkers
Amant, A. H. S., Lemen, D., Florinas, S., Mao, S., Fazenbaker, C. A., Zhong, H., Wu, H., Gao, C., Christie, R. J., & de Alaniz, J. R. (2018) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.8b00320 · Cited by 71 · see citing works
Protein‐Templated Fragment Ligations—From Molecular Recognition to Drug Discovery
Jaegle, M., Wong, E. L., Tauber, C., Nawrotzky, E., Arkona, C., & Rademann, J. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201610372 · Cited by 70 · see citing works
Willand, N., Desroses, M., Toto, P., Dirié, B., Lens, Z., Villeret, V., Rucktooa, P., Locht, C., Baulard, A. R., & Deprez, B. P. (2010) · ACS Chemical Biology · doi:10.1021/cb100177g · Cited by 67 · see citing works
Radkiewicz, J. L., McAllister, M. A., Goldstein, E., & Houk, K. N. (1998) · The Journal of Organic Chemistry · doi:10.1021/jo971425f · Cited by 62 · see citing works
Genetically encoded unstrained olefins for live cell labeling with tetrazine dyes
Lee, Y., Kurra, Y., Yang, Y., Torres‐Kolbus, J., Deiters, A., & Liu, W. R. (2014) · Chemical Communications · doi:10.1039/c4cc06435f · Cited by 59 · see citing works
Nazaré, M., Matter, H., Will, D. W., Wagner, M., Urmann, M., Czech, J., Schreuder, H., Bauer, A., Ritter, K., & Wehner, V. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201107091 · Cited by 59 · see citing works
ANTIMITOTIC ACTION OF MALEIMIDE AND RELATED SUBSTANCES
Friedmann, E., Marrian, D. H., & Simon-Reuss, I. (1949) · British Journal of Pharmacology and Chemotherapy · doi:10.1111/j.1476-5381.1949.tb00521.x · Cited by 56 · see citing works
Predictive Multivariate Models for Bioorthogonal Inverse-Electron Demand Diels–Alder Reactions
Ravasco, J. M. J. M., & Coelho, J. A. S. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.9b11948 · Cited by 54 · see citing works
Tang, S., Shi, J. M., & Guo, Q. (2012) · Organic & Biomolecular Chemistry · doi:10.1039/c2ob07079k · Cited by 53 · see citing works
Quantitative and Orthogonal Formation and Reactivity of SuFEx Platforms
Gahtory, D., Sen, R., Pujari, S. P., Li, S., Zheng, Q., Moses, J. E., Sharpless, K. B., & Zuilhof, H. T. (2018) · Chemistry - A European Journal · doi:10.1002/chem.201802356 · Cited by 53 · see citing works
Rijkers, D. T. S., Merkx, R., Yim, C., Brouwer, A. J., & Liskamp, R. M. J. (2009) · Journal of Peptide Science · doi:10.1002/psc.1197 · Cited by 52 · see citing works
Versatile Peptide Macrocyclization with Diels–Alder Cycloadditions
Montgomery, J. E., Donnelly, J. A., Fanning, S. W., Speltz, T. E., Shangguan, X., Coukos, J. S., Greene, G. L., & Moellering, R. E. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b07578 · Cited by 50 · see citing works
Tetrakis(trimethylsilyl)cyclobutadiene and Tetrakis(trimethylsilyl)tetrahedrane
Maier, G., Neudert, J., & Wolf, O. (2001) · Angewandte Chemie International Edition · doi:10.1002/1521-3773(20010504)40:9 · Cited by 46 · see citing works
New insights into the kinetic target-guided synthesis of protein ligands
Oueis, E., Sabot, C., & Renard, P. (2015) · Chemical Communications · doi:10.1039/c5cc04183j · Cited by 44 · see citing works
Self-citationBosc, D., Jakhlal, J., Deprez, B. P., & Deprez-Poulain, R. F. (2016) · Future Medicinal Chemistry · doi:10.4155/fmc-2015-0007 · Cited by 44 · see citing works
Merkx, R., van Haren, M. J., Rijkers, D. T. S., & Liskamp, R. M. J. (2007) · The Journal of Organic Chemistry · doi:10.1021/jo0704513 · Cited by 40 · see citing works
Phospha‐Michael Addition as a New Click Reaction for Protein Functionalization
Lee, Y., Kurra, Y., & Liu, W. R. (2016) · ChemBioChem · doi:10.1002/cbic.201500697 · Cited by 39 · see citing works
Kinetic Target-Guided Synthesis: Reaching the Age of Maturity
Bosc, D., Camberlein, V., Gealageas, R., Castillo‐Aguilera, O., Deprez, B. P., & Deprez-Poulain, R. F. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01183 · Cited by 39 · see citing works
Emerging affinity-based techniques in proteomics
Xie, S., Moya, C., Bilgin, B., Jayaraman, A., & Walton, S. P. (2009) · Expert Review of Proteomics · doi:10.1586/epr.09.74 · Cited by 38 · see citing works
Comparative reactivity analysis of small-molecule thiol surrogates
Petri, L., Ábrányi‐Balogh, P., Varga, P. R., Imre, T., & Keserű, G. M. (2020) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2020.115357 · Cited by 38 · see citing works
Wall, A., Wills, A. G., Forte, N., Bahou, C., Bonin, L., Nicholls, K., Ma, M., Chudasama, V., & Baker, J. R. (2020) · Chemical Science · doi:10.1039/d0sc05128d · Cited by 36 · see citing works
Amant, A. H. S., Huang, F., Lin, J., Rickert, K. W., Oganesyan, V., Lemen, D., Mao, S., Harper, J. W., Marelli, M., Wu, H., et al. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201903494 · Cited by 35 · see citing works
Moree, W. J., Schouten, A., Kroon, J., & Liskamp, R. M. J. (1995) · International journal of peptide & protein research · doi:10.1111/j.1399-3011.1995.tb01312.x · Cited by 33 · see citing works
Jaegle, M., Steinmetzer, T., & Rademann, J. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201611547 · Cited by 33 · see citing works
Gao, F., Yan, X., & Auclair, K. (2009) · Chemistry - A European Journal · doi:10.1002/chem.200802172 · Cited by 32 · see citing works
Kondrat’eva Ligation: Diels–Alder-Based Irreversible Reaction for Bioconjugation
Jouanno, L., Chevalier, A., Sekkat, N., Perzo, N., Castel, H., Romieu, A., Lange, N., Sabot, C., & Renard, P. (2014) · The Journal of Organic Chemistry · doi:10.1021/jo501972m · Cited by 32 · see citing works
Self-citationWong, E. L., Nawrotzky, E., Arkona, C., Kim, B. G., Beligny, S., Wang, X., Wagner, S., Lisurek, M., Carstanjen, D., & Rademann, J. (2019) · Nature Communications · doi:10.1038/s41467-018-07923-2 · Cited by 32 · see citing works
Hu, M.-H., Chen, X. D., Chen, S.-B., Ou, T., Yao, M., Gu, L., Huang, Z., & Tan, J. (2015) · Scientific Reports · doi:10.1038/srep17202 · Cited by 30 · see citing works
On the Reactivity of the Thiol Group of Thiolsubtilisin
Polgár, L., Halász, P., & Moravcsik, E. (1973) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1973.tb03140.x · Cited by 29 · see citing works
Reaction site-driven regioselective synthesis of AChE inhibitors
Oueis, E., Santoni, G., Ronco, C., Syzgantseva, O. A., Tognetti, V., Joubert, L., Romieu, A., Weik, M., Jean, L., Sabot, C., et al. (2013) · Organic & Biomolecular Chemistry · doi:10.1039/c3ob42109k · Cited by 29 · see citing works
Self-citationFirst enzymatic hydrolysis/thio-Michael addition cascade route to synthesis of AChE inhibitors
Oueis, E., Nachon, F., Sabot, C., & Renard, P. (2013) · Chemical Communications · doi:10.1039/c3cc48871c · Cited by 28 · see citing works
Self-citationMetalloprotein-Catalyzed Click Reaction for In Situ Generation of a Potent Inhibitor
Miyake, Y., Itoh, Y., Suzuma, Y., Kodama, H., Kurohara, T., Yamashita, Y., Narozny, R., Hanatani, Y., Uchida, S., & Suzuki, T. (2020) · ACS Catalysis · doi:10.1021/acscatal.0c00369 · Cited by 23 · see citing works
Druggability Assessment of Targets Used in Kinetic Target-Guided Synthesis
Ünver, M. Y., Gierse, R. M., Ritchie, H., & Hirsch, A. K. H. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00266 · Cited by 22 · see citing works
Discovery of Bivalent Kinase Inhibitors via Enzyme-Templated Fragment Elaboration
Kwarcinski, F. E., Steffey, M. E., Fox, C. C., & Soellner, M. B. (2015) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.5b00167 · Cited by 20 · see citing works
Mocharla, V. P., Walsh, J. C., Padgett, H. C., Su, H. C., Fueger, B. J., Weber, W., Czernin, J. G., & Kolb, H. C. (2012) · ChemMedChem · doi:10.1002/cmdc.201200466 · Cited by 17 · see citing works
An Entry of the Chemoselective Sulfo-Click Reaction into the Sphere of Nucleic Acids
Clavé, G., Dursun, E., Vasseur, J., & Smietana, M. (2020) · Organic Letters · doi:10.1021/acs.orglett.0c00265 · Cited by 17 · see citing works
Fredy, J. W., Cutolo, G., Poret, B., Nehmé, R., Hubert‐Roux, M., Gandolfo, P., Castel, H., Schuler, M., Tatibouët, A., Sabot, C., et al. (2019) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.9b00153 · Cited by 15 · see citing works
Self-citationAngelbello, A. J., & Disney, M. D. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00417 · Cited by 12 · see citing works
Masuda, R., Kawasaki, Y., Igawa, K., Manabe, Y., Fujii, H., Kato, N., Tomooka, K., & Ohkanda, J. (2020) · Chemistry - An Asian Journal · doi:10.1002/asia.202000042 · Cited by 11 · see citing works
Maleimide-based metal-free ligation with dienes: a comparative study
Lossouarn, A., Renault, K., Bailly, L., Frisby, A., Nahenec‐Martel, P. L., Renard, P., & Sabot, C. (2020) · Organic & Biomolecular Chemistry · doi:10.1039/d0ob00403k · Cited by 8 · see citing works
Self-citationFu, S., Nie, Q., Ma, Y., Song, P., Ren, X., Luo, C. Y., Shang, L., & Zheng, Y. (2018) · Chemical Communications · doi:10.1039/c8cc00469b · Cited by 3 · see citing works
Frontispiece: Protein‐Templated Hit Identification through an Ugi Four‐Component Reaction
Mancini, F., Ünver, M. Y., Elgaher, W. A. M., Jumde, V. R., Alhayek, A., Lukat, P., Herrmann, J. E., Witte, M. D., Köck, M., Blankenfeldt, W., et al. (2020) · Chemistry - A European Journal · doi:10.1002/chem.202086462 · Cited by 1 · see citing works
Rostovtsev, V. V., Green, L. G., Fokin, V. V., & Sharpless, K. B. (2002) · Angewandte Chemie International Edition · doi:10.1002/1521-3773(20020715)41:14
Kolb (2001) · doi:10.1002/1521-3773(20010601)40:11
Flagged first, then by citations
1 of the 94 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
PROTAC targeted protein degraders: the past is prologue
Békés, M., Langley, D. R., & Crews, C. M. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00371-6 · Cited by 3,395 · see citing works
Engineered Polymer-Supported Biorthogonal Nanocatalysts Using Flash Nanoprecipitation
Huang, R., Hirschbiegel, C., Zhang, X., Gupta, A., Fedeli, S., Xu, Y., & Rotello, V. M. (2022) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.2c04496 · Cited by 28 · see citing works
Protein-templated ligand discovery via the selection of DNA-encoded dynamic libraries
Zhou, Y., Shen, W., Gao, Y., Peng, J., Li, Q., Wei, X., Liu, S., Lam, F. S., Mayol-Llinàs, J., Zhao, G., et al. (2024) · Nature Chemistry · doi:10.1038/s41557-024-01442-y · Cited by 25 · see citing works
Heptamethine cyanines in bioorthogonal chemistry
Liao, Y., Liang, Y., Huang, Y., Zeng, X., Tian, H., & Yin, J. (2023) · Chinese Chemical Letters · doi:10.1016/j.cclet.2023.109092 · Cited by 24 · see citing works
Wang, F., Bao, C., Cui, S., Fan, J., Zhang, Z., Yang, W., Yu, Y., & Li, Y. (2024) · Analytical Chemistry · doi:10.1021/acs.analchem.4c01663 · Cited by 18 · see citing works
Luminescent lanthanide metallopeptides for biomolecule sensing and cellular imaging
Sánchez‐Fernández, R., Obregon-Gomez, I., Sarmiento, A., Vázquez, M. E., & Pazos, E. (2024) · Chemical Communications · doi:10.1039/d4cc03205e · Cited by 17 · see citing works
Maegawa, K., Tanimoto, H., Onishi, S., Tomohiro, T., Morimoto, T., & Kakiuchi, K. (2021) · Organic Chemistry Frontiers · doi:10.1039/d1qo01088c · Cited by 17 · see citing works
Tanimoto, H., & Tomohiro, T. (2024) · Chemical Communications · doi:10.1039/d4cc03359k · Cited by 16 · see citing works
Bhattacharyya, T., Panda, D., & Dash, J. (2021) · Organic Letters · doi:10.1021/acs.orglett.1c00685 · Cited by 10 · see citing works
Growing Impact of Bioorthogonal Click Chemistry in Cell Surface Glycan Labeling
Agrahari, A. K., Rajkhowa, S., Singh, S. K., Jaiswal, M. K., & Tiwari, V. K. (2024) · Current Organic Chemistry · doi:10.2174/0113852728326779240911055902 · Cited by 9 · see citing works
Metalloenzyme‐Mediated Thiol‐Yne Addition Towards Photoisomerizable Fluorescent Dyes
Lossouarn, A., Puteaux, C., Bailly, L., Tognetti, V., Joubert, L., Renard, P., & Sabot, C. (2022) · Chemistry - A European Journal · doi:10.1002/chem.202202180 · Cited by 8 · see citing works
Self-citationDiscovery of Boronic Acids-Based β-Lactamase Inhibitors Through In Situ Click Chemistry
Santi, N., Piccirilli, A., Corsini, F., Taracila, M. A., Perilli, M., Bonomo, R. A., Fini, F., Prati, F., & Caselli, E. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26094182 · Cited by 7 · see citing works
Coumarin-Conjugated Macromolecular Probe for Sequential Stimuli-Mediated Activation
Jiang, Y., Li, R., Ren, F., Yang, S., & Shao, A. (2023) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.3c00418 · Cited by 7 · see citing works
Kugler, M., Hadzima, M., Dzijak, R., Rampmaier, R., Srb, P., Vrzal, L., Vobůrka, Z., Majer, P., Řezáčová, P., & Vrábel, M. (2022) · RSC Medicinal Chemistry · doi:10.1039/d2md00330a · Cited by 7 · see citing works
Bao, J., Tong, C., He, M., & Zhang, H. (2023) · Luminescence · doi:10.1002/bio.4594 · Cited by 7 · see citing works
Studies of the amidation of porphyrin-NHS esters in dilute aqueous solution
Siwawannapong, K., Wu, Z., Ngo, Q.-T., & Lindsey, J. S. (2025) · New Journal of Chemistry · doi:10.1039/d5nj02078f · Cited by 6 · see citing works
Zientek, S. H., Thompson, S., Sephton, S. M., & Aigbirhio, F. I. (2023) · Journal of Labelled Compounds and Radiopharmaceuticals · doi:10.1002/jlcr.4029 · Cited by 6 · see citing works
Biocompatible reactions: advances in kinetic target-guided synthesis
Parvatkar, P. T., Wagner, A. J., & Manetsch, R. (2023) · Trends in Chemistry · doi:10.1016/j.trechm.2023.06.002 · Cited by 6 · see citing works
Fluorescent Reporters for Antimicrobial Peptides
Hong, Y., & Li, W. (2021) · Australian Journal of Chemistry · doi:10.1071/ch21070 · Cited by 4 · see citing works
Cutting-edge bioorthogonal chemistry: Innovations, practical applications, and emerging trends
Chetry, A. B. (2024) · European Journal of Chemistry · doi:10.5155/eurjchem.15.4.355-365.2579 · Cited by 3 · see citing works
Puteaux, C., Toubia, I., Truong, L., Hubert‐Roux, M., Bailly, L., Oulyadi, H., Renard, P., & Sabot, C. (2024) · Angewandte Chemie International Edition · doi:10.1002/anie.202407888 · Cited by 2 · see citing works
Self-citationThe emergence of sulfo-click amidation in kinetic target-guided synthesis
Parvatkar, P. T., & Manetsch, R. (2024) · Medicinal Chemistry Research · doi:10.1007/s00044-024-03236-w · Cited by 2 · see citing works
Chemoselective seleno-click amidation in kinetic target-guided synthesis
Huang, L., Parvatkar, P. T., Wagner, A. J., Kulkarni, S. S., & Manetsch, R. (2024) · Chemical Communications · doi:10.1039/d4cc04491f · Cited by 1 · see citing works
Puteaux, C., Toubia, I., Truong, L., Hubert‐Roux, M., Bailly, L., Oulyadi, H., Renard, P., & Sabot, C. (2024) · Angewandte Chemie · doi:10.1002/ange.202407888
Self-citationRoadmap for click and combinatorial approaches to quadruplex ligand discovery: 2024
Dash, J., Saha, U., & Basu, S. (2024) · Annual reports in medicinal chemistry · doi:10.1016/bs.armc.2024.09.004
Clicked H-Shaped Arylopeptoids
Chamas, Z., Akhdar, A., Charnay‐Pouget, F., Faure, S., & Gautier, A. (2025) · Molecules · doi:10.3390/molecules30030724
BindingDB Entry 50019156: Identification of specific carbonic anhydrase inhibitors
BindingDB (2024) · UC San Diego · doi:10.7270/q2x06cb9
- Authors
- Lossouarn, A., Renard, P.-Y., & Sabot, C.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Sabot, Cyrille
- Venue
- Bioconjugate Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2020-11-24
- Volume
- 32
- Issue
- 1
- Pages
- 63-72
- ISSN
- 1043-1802 (ISSN-L)
- 1520-4812
- OpenAlex
- W3109296721
- Cited by
- 26
- References
- 94
- Citations by year
- 2025: 3 · 2024: 11 · 2023: 5 · 2022: 4 · 2021: 3
- FWCI
- 0.23
- Type
- journal article
- Language
- en
- Open access
- Licence
- Locations
- Bioconjugate Chemistry (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- Funders
- Agence Nationale de la Recherche (ANR-11-LABX-0029, ANR-16-CE07-0004)
- Universit? de Rouen
- Centre National de la Recherche Scientifique
- INSA Rouen Normandie
- Topics
- Physical Sciences › Chemistry › Organic Chemistry › Click Chemistry and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Keywords
- bioorthogonal chemistry, bioconjugation, chemical ligation, covalent drug discovery, ligand discovery, reaction kinetics, active site topology
- MeSH terms
- Kinetics, Ligands, Retrospective Studies, Thermodynamics, Drug Discovery
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review