Strategies for Discovering and Derisking Covalent, Irreversible Enzyme Inhibitors

The growing impact of click chemistry on drug discovery

Kolb, H. C., & Sharpless, K. B. (2003) · Drug Discovery Today · doi:10.1016/s1359-6446(03)02933-7 · Cited by 3,155 · see citing works

The T790M mutation in EGFR kinase causes drug resistance by increasing the affinity for ATP

Yun, C.-H., Mengwasser, K. E., Toms, A. V., Woo, M. S., Greulich, H., Wong, K.-K., Meyerson, M., & Eck, M. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0709662105 · Cited by 2,118 · cited 2× · see citing works

The molecular logic of endocannabinoid signalling

Piomelli, D. (2003) · Nature Reviews Neuroscience · doi:10.1038/nrn1247 · Cited by 1,957 · see citing works

Drug-target residence time and its implications for lead optimization

Copeland, R. A., Pompliano, D. L., & Meek, T. D. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2082 · Cited by 1,464 · see citing works

Activity-Based Protein Profiling: From Enzyme Chemistry to Proteomic Chemistry

Cravatt, B. F., Wright, A. T., & Kozarich, J. W. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.124125 · Cited by 1,270 · see citing works

Activity-based protein profiling: The serine hydrolases

Liu, Y., Patricelli, M. P., & Cravatt, B. F. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.26.14694 · Cited by 1,133 · see citing works

Irreversible Inhibitors of Serine, Cysteine, and Threonine Proteases

Powers, J. C., Asgian, J. L., Ekici, Ö. D., & James, K. E. (2002) · Chemical Reviews · doi:10.1021/cr010182v · Cited by 1,090 · see citing works

Evaluation of enzyme inhibitors in drug discovery. A guide for medicinal chemists and pharmacologists.

Copeland, R. A. (2005) · PubMed · Cited by 1,045 · see citing works

Acetylation of prostaglandin synthase by aspirin.

Roth, G. J., Stanford, N., & Majerus, P. W. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.8.3073 · Cited by 1,012 · see citing works

Mechanism of action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine.

Tipper, D. J., & Strominger, J. L. (1965) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.54.4.1133 · Cited by 1,008 · see citing works

Activity-Based Protein Profiling in Vivo Using a Copper(I)-Catalyzed Azide-Alkyne [3 + 2] Cycloaddition

Speers, A. E., Adam, G. C., & Cravatt, B. F. (2003) · Journal of the American Chemical Society · doi:10.1021/ja034490h · Cited by 955 · see citing works

Irreversible inhibitors of the EGF receptor may circumvent acquired resistance to gefitinib

Kwak, E. L., Sordella, R., Bell, D. W., Godin-Heymann, N., Okimoto, R. A., Brannigan, B. W., Harris, P. L., Driscoll, D. R., Fidias, P. M., Lynch, T. J., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502860102 · Cited by 950 · see citing works

Selective blockade of 2-arachidonoylglycerol hydrolysis produces cannabinoid behavioral effects

Long, J. Z., Li, W., Booker, L., Burston, J. J., Kinsey, S. G., Schlosburg, J. E., Pavón, F. J., Serrano, A., Selley, D. E., Parsons, L. H., et al. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.129 · Cited by 938 · see citing works

Paradigm shift in neuroprotection by NMDA receptor blockade: memantine and beyond

Lipton, S. A. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd1958 · Cited by 909 · see citing works

Photoactivated γ-secretase inhibitors directed to the active site covalently label presenilin 1

Li, Y.-M., Xu, M., Lai, M.-T., Huang, Q., Castro, J. L., DiMuzio-Mower, J., Harrison, T., Lellis, C., Nadin, A., Neduvelil, J. G., et al. (2000) · Nature · doi:10.1038/35015085 · Cited by 866 · see citing works

Targeting the endocannabinoid system: to enhance or reduce?

Marzo, V. D. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2553 · Cited by 798 · see citing works

Profiling Enzyme Activities In Vivo Using Click Chemistry Methods

Speers, A. E., & Cravatt, B. F. (2004) · Chemistry & Biology · doi:10.1016/j.chembiol.2004.03.012 · Cited by 774 · see citing works

Identification and Biological Activity of the Active Metabolite of Clopidogrel

Savi, P., Pereillo, J., Uzabiaga, M.-F., Combalbert, J., Picard, C., Maffrand, J., Pascal, M., & Herbert, J. (2000) · Thrombosis and Haemostasis · doi:10.1055/s-0037-1614133 · Cited by 752 · see citing works

Drug−Protein Adducts: An Industry Perspective on Minimizing the Potential for Drug Bioactivation in Drug Discovery and Development

Evans, D. C., Watt, A. P., Nicoll‐Griffith, D. A., & Baillie, T. A. (2003) · Chemical Research in Toxicology · doi:10.1021/tx034170b · Cited by 707 · see citing works

Structure and function of fatty acid amide hydrolase

McKinney, M. K., & Cravatt, B. F. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133450 · Cited by 680 · see citing works

Click Chemistry and Bioorthogonal Reactions: Unprecedented Selectivity in the Labeling of Biological Molecules

Best, M. D. (2009) · Biochemistry · doi:10.1021/bi9007726 · Cited by 643 · see citing works

A Comprehensive Listing of Bioactivation Pathways of Organic Functional Groups

Kalgutkar, A. S. S., Gardner, I. B., Obach, R. S., Shaffer, C. L., Callegari, E., Henne, K. R., Mutlib, A. E., Dalvie, D., Lee, J. S., Nakai, Y., et al. (2005) · Current Drug Metabolism · doi:10.2174/1389200054021799 · Cited by 623 · see citing works

Chemistry-Based Functional Proteomics Reveals Novel Members of the Deubiquitinating Enzyme Family

Borodovsky, A., Ovaa, H., Kolli, N., Gan-Erdene, T., Wilkinson, K. D., Ploegh, H. L., & Kessler, B. M. (2002) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00248-x · Cited by 588 · see citing works

Epoxide electrophiles as activity-dependent cysteine protease profiling and discovery tools

Greenbaum, D. C., Medzihradszky, K. F., Burlingame, A. L., & Bogyo, M. S. (2000) · Chemistry & Biology · doi:10.1016/s1074-5521(00)00014-4 · Cited by 581 · see citing works

Mechanism-Based Profiling of Enzyme Families

Evans, M. J., & Cravatt, B. F. (2006) · Chemical Reviews · doi:10.1021/cr050288g · Cited by 568 · see citing works

Residence Time of Receptor−Ligand Complexes and Its Effect on Biological Function

Tummino, P. J., & Copeland, R. A. (2008) · Biochemistry · doi:10.1021/bi8002023 · Cited by 547 · see citing works

Enzymatic pathways that regulate endocannabinoid signaling in the nervous system

Ahn, K., McKinney, M. K., & Cravatt, B. F. (2008) · Chemical Reviews · doi:10.1021/cr0782067 · Cited by 529 · see citing works

Molecular structure of the acyl-enzyme intermediate in β-lactam hydrolysis at 1.7 Å resolution

Strynadka, N. C. J., Adachi, H., Jensen, S. E., Johns, K. L., Sielecki, A. R., Betzel, C., Sutoh, K., & James, M. N. G. (1992) · Nature · doi:10.1038/359700a0 · Cited by 525 · see citing works

Structural Bioinformatics-Based Design of Selective, Irreversible Kinase Inhibitors

Cohen, M. S., Zhang, C., Shokat, K. M., & Taunton, J. (2005) · Science · doi:10.1126/science1108367 · Cited by 509 · see citing works

Structure and Stereochemistry of the Active Metabolite of Clopidogrel

Pereillo, J., Maftouh, M., Andrieu, A., Uzabiaga, M.-F., Fedeli, O., Savi, P., Pascal, M., Herbert, J., Maffrand, J., & Picard, C. (2002) · Drug Metabolism and Disposition · doi:10.1124/dmd.30.11.1288 · Cited by 459 · see citing works

Activity-based probes for the proteomic profiling of metalloproteases

Saghatelian, A., Jessani, N., Joseph, A., Humphrey, M., & Cravatt, B. F. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402784101 · Cited by 456 · see citing works

Suicide substrates: mechanism-based enzyme inactivators

Walsh, C. T. (1982) · Tetrahedron · doi:10.1016/0040-4020(82)85068-0 · Cited by 447 · see citing works

Structural basis for the β lactam resistance of PBP2a from methicillin-resistant Staphylococcus aureus

Lim, D., & Strynadka, N. C. J. (2002) · Nature Structural Biology · doi:10.1038/nsb858 · Cited by 442 · see citing works

Discovery and Characterization of a Highly Selective FAAH Inhibitor that Reduces Inflammatory Pain

Ahn, K., Johnson, D. S., Mileni, M., Beidler, D., Long, J. Z., McKinney, M. K., Weerapana, E., Sadagopan, N., Liimatta, M., Smith, S. E., et al. (2009) · Chemistry & Biology · doi:10.1016/j.chembiol.2009.02.013 · Cited by 439 · see citing works

The aspirin and heme-binding sites of ovine and murine prostaglandin endoperoxide synthases.

DeWitt, D. L., El-Harith, E. A., Kraemer, S. A., Andrews, M. J., Yao, E. F., Armstrong, R. L., & Smith, W. L. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)34105-5 · Cited by 429 · see citing works

Characterization of the Fatty Acid Amide Hydrolase Inhibitor Cyclohexyl Carbamic Acid 3′-Carbamoyl-biphenyl-3-yl Ester (URB597): Effects on Anandamide and Oleoylethanolamide Deactivation

Fegley, D., Gaetani, S., Duranti, A., Tontini, A., Mor, M., Tarzia, G., & Piomelli, D. (2005) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.104.078980 · Cited by 427 · see citing works

Functional Interrogation of the Kinome Using Nucleotide Acyl Phosphates

Patricelli, M. P., Szardenings, A. K., Liyanage, M., Nomanbhoy, T. K., Wu, M., Weissig, H., Aban, A., Chun, D., Tanner, S. W., & Kozarich, J. W. (2006) · Biochemistry · doi:10.1021/bi062142x · Cited by 426 · see citing works

A proton-pump inhibitor expedition: the case histories of omeprazole and esomeprazole

Olbe, L. C., Carlsson, E. I., & Lindberg, P. (2003) · Nature Reviews Drug Discovery · doi:10.1038/nrd1010 · Cited by 419 · see citing works

Scientific and therapeutic advances in antiplatelet therapy

Bhatt, D. L., & Topol, E. J. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd985 · Cited by 409 · see citing works

Biochemical mechanisms of drug action: what does it take for success?

Swinney, D. C. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1500 · Cited by 396 · see citing works

Dual blockade of FAAH and MAGL identifies behavioral processes regulated by endocannabinoid crosstalk in vivo

Long, J. Z., Nomura, D. K., Vann, R. E., Walentiny, D. M., Booker, L., Jin, X., Burston, J. J., Sim‐Selley, L. J., Lichtman, A. H., Wiley, J. L., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0909411106 · Cited by 393 · see citing works

Discovering potent and selective reversible inhibitors of enzymes in complex proteomes

Leung, D., Hardouin, C., Boger, D. L., & Cravatt, B. F. (2003) · Nature Biotechnology · doi:10.1038/nbt826 · Cited by 387 · see citing works

β-Lactam antibiotic resistance: a current structural perspective

Wilke, M. S., Lovering, A. L., & Strynadka, N. C. (2005) · Current Opinion in Microbiology · doi:10.1016/j.mib.2005.08.016 · Cited by 383 · see citing works

Profiling Serine Hydrolase Activities in Complex Proteomes

Kidd, D., Liu, Y., & Cravatt, B. F. (2001) · Biochemistry · doi:10.1021/bi002579j · Cited by 369 · see citing works

Activity-based probes that target diverse cysteine protease families

Kato, D., Boatright, K. M., Berger, A. B., Nazif, T. M., Blum, G., Ryan, C., Chehade, K. A. H., Salvesen, G. S., & Bogyo, M. S. (2005) · Nature Chemical Biology · doi:10.1038/nchembio707 · Cited by 356 · see citing works

Covalent Modifiers: An Orthogonal Approach to Drug Design

Potashman, M. H., & Duggan, M. E. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm8008597 · Cited by 348 · see citing works

Kinetic and Structural Studies on the Interaction of Cholinesterases with the Anti-Alzheimer Drug Rivastigmine ,

Bar-On, P., Millard, C. B., Harel, M., Dvir, H., Enz, A., Sussman, J. L., & Silman, I. (2002) · Biochemistry · doi:10.1021/bi020016x · Cited by 332 · see citing works

Reversible Inhibitors of Fatty Acid Amide Hydrolase That Promote Analgesia: Evidence for an Unprecedented Combination of Potency and Selectivity

Lichtman, A. H., Leung, D., Shelton, C. C., Saghatelian, A., Hardouin, C., Boger, D. L., & Cravatt, B. F. (2004) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.104.069401 · Cited by 329 · see citing works

Mode of action of orlistat.

Guerciolini, R. (1997) · PubMed · Cited by 326 · see citing works

The active metabolite of Clopidogrel disrupts P2Y12 receptor oligomers and partitions them out of lipid rafts

Savi, P., Zachayus, J., Delesque-Touchard, N., Labouret, C., Hervé, C., Uzabiaga, M.-F., Pereillo, J., Culouscou, J., Bono, F., Ferrara, P., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510446103 · Cited by 316 · see citing works

The mechanism of action of the antisecretory agent omeprazole

Lindberg, P., Nordberg, P., Alminger, T., BRAENDSTROEM, A., & Wallmark, B. (1986) · Journal of Medicinal Chemistry · doi:10.1021/jm00158a001 · Cited by 306 · see citing works

Characterization of Monoacylglycerol Lipase Inhibition Reveals Differences in Central and Peripheral Endocannabinoid Metabolism

Long, J. Z., Nomura, D. K., & Cravatt, B. F. (2009) · Chemistry & Biology · doi:10.1016/j.chembiol.2009.05.009 · Cited by 305 · see citing works

Optimization of 6,7-Disubstituted-4-(arylamino)quinoline-3-carbonitriles as Orally Active, Irreversible Inhibitors of Human Epidermal Growth Factor Receptor-2 Kinase Activity

Tsou, H., Overbeek, E., Hallett, W. A., Reich, M. F., Floyd, M. B., Johnson, B. D., Michalak, R. S., Nilakantan, R., Discafani, C. M., Golas, J., et al. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm040159c · Cited by 302 · see citing works

Chemical Approaches for Functionally Probing the Proteome

Greenbaum, D. C., Baruch, A., Hayrapetian, L., Darula, Z., Burlingame, A. L., Medzihradszky, K. F., & Bogyo, M. S. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.t100003-mcp200 · Cited by 291 · see citing works

Chemistry of Covalent Inhibition of the Gastric (H+, K+)-ATPase by Proton Pump Inhibitors

Shin, J. M., Cho, Y. M., & Sachs, G. M. (2004) · Journal of the American Chemical Society · doi:10.1021/ja049607w · Cited by 285 · see citing works

Activity-based protein profiling for the functional annotation of enzymes

Barglow, K. T., & Cravatt, B. F. (2007) · Nature Methods · doi:10.1038/nmeth1092 · Cited by 281 · see citing works

The lipase inhibitor tetrahydrolipstatin binds covalently to the putative active site serine of pancreatic lipase

Hadváry, P., Sidler, W., Meister, W., Vetter, W., & Wolfer, H. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)52203-1 · Cited by 281 · see citing works

Tandem orthogonal proteolysis-activity-based protein profiling (TOP-ABPP)—a general method for mapping sites of probe modification in proteomes

Weerapana, E., Speers, A. E., & Cravatt, B. F. (2007) · Nature Protocols · doi:10.1038/nprot.2007.194 · Cited by 276 · see citing works

Drug Bioactivation Covalent Binding to Target Proteins and Toxicity Relevance

Zhou, S., Chan, E., Duan, W., Huang, M., & Chen, Y. (2005) · Drug Metabolism Reviews · doi:10.1081/dmr-200028812 · Cited by 273 · see citing works

Activity probe for in vivo profiling of the specificity of proteasome inhibitor bortezomib

Berkers, C. R., Verdoes, M., Lichtman, E. I., Fiebiger, E., Kessler, B. M., Anderson, K. C., Ploegh, H. L., Ovaa, H., & Galardy, P. J. (2005) · Nature Methods · doi:10.1038/nmeth759 · Cited by 262 · see citing works

Identification of proteases that regulate erythrocyte rupture by the malaria parasite Plasmodium falciparum

Arastu‐Kapur, S., Ponder, E. L., Fonović, U. P., Yeoh, S., Yuan, F., Fonovič, M., Grainger, M., Phillips, C. I., Powers, J. C., & Bogyo, M. S. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.70 · Cited by 260 · see citing works

Idiosyncratic Drug Reactions: Past, Present, and Future

Uetrecht, J. (2007) · Chemical Research in Toxicology · doi:10.1021/tx700186p · Cited by 258 · see citing works

A Zone Classification System for Risk Assessment of Idiosyncratic Drug Toxicity Using Daily Dose and Covalent Binding

Nakayama, S., Atsumi, R., Takakusa, H., Kobayashi, Y., Kurihara, A., Nagai, Y., Nakai, D., & Okazaki, O. (2009) · Drug Metabolism and Disposition · doi:10.1124/dmd.109.027797 · Cited by 252 · see citing works

Mechanistic Basis of Enzyme-Targeted Drugs

Robertson, J. G. (2005) · Biochemistry · doi:10.1021/bi050247e · Cited by 247 · see citing works

Proteomic profiling of metalloprotease activities with cocktails of active-site probes

Sieber, S. A., Niessen, S., Hoover, H. S., & Cravatt, B. F. (2006) · Nature Chemical Biology · doi:10.1038/nchembio781 · Cited by 247 · see citing works

Tagging and detection strategies for activity-based proteomics

Sadaghiani, A. M., Verhelst, S. H. L., & Bogyo, M. S. (2006) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2006.11.030 · Cited by 246 · see citing works

Activity-based probes for proteomic profiling of histone deacetylase complexes

Salisbury, C. M., & Cravatt, B. F. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608659104 · Cited by 243 · see citing works

G Protein-Coupled Receptor Trafficking in Health and Disease: Lessons Learned to Prepare for Therapeutic Mutant Rescue in Vivo

Conn, P. M., Ulloa‐Aguirre, A., Ito, J., & Janovick, J. A. (2007) · Pharmacological Reviews · doi:10.1124/pr.59.3.2 · Cited by 242 · see citing works

A streamlined platform for high-content functional proteomics of primary human specimens

Jessani, N., Niessen, S., Wei, B. Q., Nicolau, M. M., Humphrey, M., Ji, Y., Han, W., Noh, D., Yates, J. R., Jeffrey, S. S., et al. (2005) · Nature Methods · doi:10.1038/nmeth778 · Cited by 240 · see citing works

Protein Damage by Reactive Electrophiles: Targets and Consequences

Liebler, D. C. (2007) · Chemical Research in Toxicology · doi:10.1021/tx700235t · Cited by 235 · see citing works

Mechanism of Carbamate Inactivation of FAAH: Implications for the Design of Covalent Inhibitors and In Vivo Functional Probes for Enzymes

Alexander, J. P., & Cravatt, B. F. (2005) · Chemistry & Biology · doi:10.1016/j.chembiol.2005.08.011 · Cited by 226 · see citing works

Developing Photoactive Affinity Probes for Proteomic Profiling: Hydroxamate-based Probes for Metalloproteases

Chan, E. W. S., Chattopadhaya, S., Panicker, R. C., Huang, X., & Yao, S. Q. (2004) · Journal of the American Chemical Society · doi:10.1021/ja047044i · Cited by 224 · see citing works

Proteomic profiling of mechanistically distinct enzyme classes using a common chemotype

Adam, G. C., Sorensen, E. J., & Cravatt, B. F. (2002) · Nature Biotechnology · doi:10.1038/nbt714 · Cited by 224 · see citing works

Irreversible Inhibition of the Mycobacterium tuberculosis β-Lactamase by Clavulanate

Hugonnet, J., & Blanchard, J. S. (2007) · Biochemistry · doi:10.1021/bi701506h · Cited by 221 · see citing works

Novel Mechanistic Class of Fatty Acid Amide Hydrolase Inhibitors with Remarkable Selectivity

Ahn, K., Johnson, D. S., Fitzgerald, L. R., Liimatta, M. B., Arendse, A., Stevenson, T. I., Lund, E. T., Nugent, R. A., Nomanbhoy, T. K., Alexander, J. P., et al. (2007) · Biochemistry · doi:10.1021/bi701378g · Cited by 217 · see citing works

Mechanisms, biology and inhibitors of deubiquitinating enzymes

Love, K. R., Catic, A., Schlieker, C. D., & Ploegh, H. L. (2007) · Nature Chemical Biology · doi:10.1038/nchembio.2007.43 · Cited by 211 · see citing works

β-Lactones as Specific Inhibitors of ClpP Attenuate the Production of Extracellular Virulence Factors of <i>Staphylococcus aureus</i>

Böttcher, T., & Sieber, S. A. (2008) · Journal of the American Chemical Society · doi:10.1021/ja8051365 · Cited by 207 · see citing works

Structure-guided development of affinity probes for tyrosine kinases using chemical genetics

Blair, J. A., Rauh, D., Kung, C. K.-H., Yun, C., Fan, Q.-W., Rode, H. B., Zhang, C., Eck, M. J., Weiss, W. A., & Shokat, K. M. (2007) · Nature Chemical Biology · doi:10.1038/nchembio866 · Cited by 204 · see citing works

Fatty acid amide hydrolase as a potential therapeutic target for the treatment of pain and CNS disorders

Ahn, K., Johnson, D. S., & Cravatt, B. F. (2009) · Expert Opinion on Drug Discovery · doi:10.1517/17460440903018857 · Cited by 198 · see citing works

Beyond Picomolar Affinities: Quantitative Aspects of Noncovalent and Covalent Binding of Drugs to Proteins

Smith, A. J. T., Zhang, X., Leach, A. G., & Houk, K. N. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm800498e · Cited by 193 · see citing works

The role of binding kinetics in therapeutically useful drug action.

Swinney, D. C. (2009) · PubMed · Cited by 184 · see citing works

β‐Lactones as Privileged Structures for the Active‐Site Labeling of Versatile Bacterial Enzyme Classes

Böttcher, T., & Sieber, S. A. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200705768 · Cited by 181 · see citing works

A Functional Proteomic Strategy to Discover Inhibitors for Uncharacterized Hydrolases

Li, W., Blankman, J. L., & Cravatt, B. F. (2007) · Journal of the American Chemical Society · doi:10.1021/ja073650c · Cited by 180 · see citing works

The Development of HKI‐272 and Related Compounds for the Treatment of Cancer

Wissner, A., & Mansour, T. S. (2008) · Archiv der Pharmazie · doi:10.1002/ardp.200800009 · Cited by 179 · see citing works

Discovery and Development of Fatty Acid Amide Hydrolase (FAAH) Inhibitors

Seierstad, M. J., & Breitenbucher, J. G. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm800311k · Cited by 179 · see citing works

Proteomic analysis of Fasciola hepatica excretory-secretory products

Jefferies, J. R., Campbell, A. M., van Rossum, A. J., Barrett, J., & Brophy, P. M. (2001) · PROTEOMICS · doi:10.1002/1615-9861(200109)1:9 · Cited by 171 · see citing works

Small Molecule Affinity Fingerprinting

Greenbaum, D. C., Arnold, W. D., Lu, F., Hayrapetian, L., Baruch, A., Krumrine, J. R., Toba, S., Chehade, K. A. H., Brömme, D., Kuntz, I. D., et al. (2002) · Chemistry & Biology · doi:10.1016/s1074-5521(02)00238-7 · Cited by 168 · see citing works

Clavulanic acid, a novel β-lactam isolated from Streptomyces clavuligerus; X-ray crystal structure analysis

Howarth, T. T., BROWN, A. G., & King, T. J. (1976) · Journal of the Chemical Society Chemical Communications · doi:10.1039/c3976000266b · Cited by 162 · see citing works

Acetylation of Prostaglandin Endoperoxide Synthetase with Acetylsalicylic Acid

van der Ouderaa, F. J. G., Buytenhek, M., Nugteren, D. H., & van Dorp, D. A. (1980) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1980.tb04760.x · Cited by 160 · see citing works

A clickable inhibitor reveals context-dependent autoactivation of p90 RSK

Cohen, M. S., Hadjivassiliou, H., & Taunton, J. (2007) · Nature Chemical Biology · doi:10.1038/nchembio859 · Cited by 157 · see citing works

Structure-guided inhibitor design for human FAAH by interspecies active site conversion

Mileni, M., Johnson, D. S., Wang, Z., Everdeen, D. S., Liimatta, M. B., Pabst, B. A., Bhattacharya, K., Nugent, R. A., Kamtekar, S., Cravatt, B. F., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806121105 · Cited by 154 · see citing works

Profiling the specific reactivity of the proteome with non-directed activity-based probes

Adam, G. C., Cravatt, B. F., & Sorensen, E. J. (2001) · Chemistry & Biology · doi:10.1016/s1074-5521(00)90060-7 · Cited by 150 · see citing works

A Strategy for Functional Proteomic Analysis of Glycosidase Activity from Cell Lysates

Vocadlo, D. J., & Bertozzi, C. R. (2004) · Angewandte Chemie International Edition · doi:10.1002/anie.200454235 · Cited by 143 · see citing works

Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases.

Yocum, R. R., Waxman, D. J., Rasmussen, J. R., & Strominger, J. L. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.6.2730 · Cited by 139 · see citing works

Optimization of Activity-Based Probes for Proteomic Profiling of Histone Deacetylase Complexes

Salisbury, C. M., & Cravatt, B. F. (2008) · Journal of the American Chemical Society · doi:10.1021/ja074138u · Cited by 127 · see citing works

β-Lactams as Selective Chemical Probes for the in Vivo Labeling of Bacterial Enzymes Involved in Cell Wall Biosynthesis, Antibiotic Resistance, and Virulence

Staub, I., & Sieber, S. A. (2008) · Journal of the American Chemical Society · doi:10.1021/ja803349j · Cited by 117 · see citing works

A Suite of Activity-Based Probes for Human Cytochrome P450 Enzymes

Wright, A., Song, J. D., & Cravatt, B. F. (2009) · Journal of the American Chemical Society · doi:10.1021/ja9037609 · Cited by 111 · see citing works

Immune-Mediated Adverse Drug Reactions

Uetrecht, J. (2008) · Chemical Research in Toxicology · doi:10.1021/tx800389u · Cited by 109 · see citing works

Discovery of an exceptionally potent and selective class of fatty acid amide hydrolase inhibitors enlisting proteome-wide selectivity screening: concurrent optimization of enzyme inhibitor potency and selectivity

Leung, D., Du, W., Hardouin, C., Cheng, H. W., Hwang, I., Cravatt, B. F., & Boger, D. L. (2005) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2004.12.085 · Cited by 106 · see citing works

Omeprazole, a specific inhibitor of gastric (H+-K+)-ATPase, is a H+-activated oxidizing agent of sulfhydryl groups.

Im, W. B., Sih, J. C., Blakeman, D. P., & McGrath, J. P. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)89112-8 · Cited by 105 · see citing works

The importance of drug-target residence time.

Zhang, R., & Monsma, F. J. (2009) · PubMed · Cited by 103 · see citing works

Chemical Proteomic Probes for Profiling Cytochrome P450 Activities and Drug Interactions In Vivo

Wright, A., & Cravatt, B. F. (2007) · Chemistry & Biology · doi:10.1016/j.chembiol.2007.08.008 · Cited by 102 · see citing works

Fatty acid amide hydrolase inhibitors display broad selectivity and inhibit multiple carboxylesterases as off-targets

Zhang, D., Saraf, A., Kolasa, T., Bhatia, P., Zheng, G. Z., Patel, M., Lannoye, G. S., Richardson, P., Stewart, A., Rogers, J. C., et al. (2007) · Neuropharmacology · doi:10.1016/j.neuropharm.2006.11.009 · Cited by 99 · see citing works

Designing transient binding drugs: A new concept for drug discovery

Ohlson, S. (2008) · Drug Discovery Today · doi:10.1016/j.drudis.2008.02.001 · Cited by 95 · see citing works

Biochemical Mechanisms of New Molecular Entities (NMEs) Approved by United States FDA During 2001-2004: Mechanisms Leading to Optimal Efficacy and Safety

Swinney, D. C. (2006) · Current Topics in Medicinal Chemistry · doi:10.2174/156802606776743093 · Cited by 92 · see citing works

Ubiquitin C-Terminal Electrophiles Are Activity-Based Probes for Identification and Mechanistic Study of Ubiquitin Conjugating Machinery

Love, K. R., Pandya, R. K., Spooner, E., & Ploegh, H. L. (2009) · ACS Chemical Biology · doi:10.1021/cb9000348 · Cited by 90 · see citing works

Divergent Synthesis of Multifunctional Molecular Probes To Elucidate the Enzyme Specificity of Dipeptidic γ-Secretase Inhibitors

Fuwa, H., Takahashi, Y., Konno, Y., Watanabe, N., Miyashita, H., Sasaki, M., Natsugari, H., Kan, T., Fukuyama, T., Tomita, T., et al. (2007) · ACS Chemical Biology · doi:10.1021/cb700073y · Cited by 90 · see citing works

Thiadiazolopiperazinyl ureas as inhibitors of fatty acid amide hydrolase

Keith, J. M., Apodaca, R. L., Xiao, W., Seierstad, M. J., Pattabiraman, K., Wu, J., Webb, M., Karbarz, M. J., Brown, S. M., Wilson, S. M. B., et al. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.07.081 · Cited by 90 · see citing works

Binding and Inactivation Mechanism of a Humanized Fatty Acid Amide Hydrolase by α-Ketoheterocycle Inhibitors Revealed from Cocrystal Structures

Mileni, M., Garfunkle, J., DeMartino, J. K., Cravatt, B. F., Boger, D. L., & Stevens, R. C. (2009) · Journal of the American Chemical Society · doi:10.1021/ja902694n · Cited by 89 · see citing works

Active-site Peptide “Fingerprinting” of Glycosidases in Complex Mixtures by Mass Spectrometry

Hekmat, O., Kim, Y., Williams, S. J., He, S., & Withers, S. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508434200 · Cited by 82 · see citing works

Selective Haptenation of Cellular or Extracellular Protein by Chemical Allergens: Association with Cytokine Polarization

Hopkins, J. E., Naisbitt, D. J., Kitteringham, N. R., Dearman, R. J., Kimber, I., & Park, B. K. (2005) · Chemical Research in Toxicology · doi:10.1021/tx049688+ · Cited by 78 · see citing works

β-Lactam Probes As Selective Chemical-Proteomic Tools for the Identification and Functional Characterization of Resistance Associated Enzymes in MRSA

Staub, I., & Sieber, S. A. (2009) · Journal of the American Chemical Society · doi:10.1021/ja901304n · Cited by 76 · see citing works

Design, Synthesis, and Evaluation of In Vivo Potency and Selectivity of Epoxysuccinyl-Based Inhibitors of Papain-Family Cysteine Proteases

Sadaghiani, A. M., Verhelst, S. H. L., Gocheva, V., Hill, K. D., Majerová, E., Stinson, S. F., Joyce, J. A., & Bogyo, M. S. (2007) · Chemistry & Biology · doi:10.1016/j.chembiol.2007.03.010 · Cited by 76 · see citing works

Biochemical and Biological Properties of 4-(3-phenyl-[1,2,4] thiadiazol-5-yl)-piperazine-1-carboxylic acid phenylamide, a Mechanism-Based Inhibitor of Fatty Acid Amide Hydrolase

Karbarz, M. J., Luo, L., Chang, L., Tham, C.-S., Palmer, J. A., Wilson, S. J., Wennerholm, M. L., Brown, S. M., Scott, B. P., Apodaca, R. L., et al. (2009) · Anesthesia &amp; Analgesia · doi:10.1213/ane.0b013e31818c7cbd · Cited by 74 · see citing works

Enzymes as a special class of therapeutic target: clinical drugs and modes of action

Robertson, J. G. (2007) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2007.08.008 · Cited by 72 · see citing works

Analytical platforms for activity-based protein profiling ? exploiting the versatility of chemistry for functional proteomics

Sieber, S. A., & Cravatt, B. F. (2006) · Chemical Communications · doi:10.1039/b600653c · Cited by 71 · see citing works

A Selective Activity-Based Probe for the Papain Family Cysteine Protease Dipeptidyl Peptidase I/Cathepsin C

Yuan, F., Verhelst, S. H. L., Blum, G., Coussens, L. M., & Bogyo, M. S. (2006) · Journal of the American Chemical Society · doi:10.1021/ja060835v · Cited by 68 · see citing works

Benzothiophene piperazine and piperidine urea inhibitors of fatty acid amide hydrolase (FAAH)

Johnson, D. S., Ahn, K., Kesten, S. R., Lazerwith, S. E., Song, Y., Morris, M. J., Fay, L. K., Gregory, T. F., Stiff, C. M., Dunbar, J. B., et al. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.03.080 · Cited by 65 · see citing works

Structure of the Covalent Adduct Formed between Mycobacterium tuberculosis β-Lactamase and Clavulanate

Tremblay, L. W., Hugonnet, J., & Blanchard, J. S. (2008) · Biochemistry · doi:10.1021/bi8001055 · Cited by 64 · see citing works

Click Chemistry‐Led Advances in High Content Functional Proteomics

Salisbury, C. M., & Cravatt, B. F. (2007) · QSAR & Combinatorial Science · doi:10.1002/qsar.200740090 · Cited by 55 · see citing works

Evaluation of Which Reactive Metabolite, If Any, Is Responsible for a Specific Idiosyncratic Reaction

Uetrecht, J. (2006) · Drug Metabolism Reviews · doi:10.1080/03602530600959615 · Cited by 52 · see citing works

Minimizing metabolic activation during pharmaceutical lead optimization: progress, knowledge gaps and future directions.

Kumar, S., Kassahun, K., Tschirret-Guth, R. A., Mitra, K., & Baillie, T. A. (2008) · PubMed · Cited by 48 · see citing works

The roles of drug metabolism in the pathogenesis of T-cell-mediated drug hypersensitivity

Lavergne, S. N., Park, B. K., & Naisbitt, D. J. (2008) · Current Opinion in Allergy and Clinical Immunology · doi:10.1097/aci.0b013e3283079c64 · Cited by 48 · see citing works

Cross‐Linking Yield Variation of a Potent Matrix Metalloproteinase Photoaffinity Probe and Consequences for Functional Proteomics

David, A., Steer, D. L., Bregant, S., Devel, L., Makaritis, A., Beau, F., Yiotakis, A., & Dive, V. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200604408 · Cited by 48 · see citing works

Small molecule microarray-facilitated screening of affinity-based probes (AfBPs) for γ-secretase

Shi, H., Liu, K., Xu, A., & Yao, S. Q. (2009) · Chemical Communications · doi:10.1039/b910611a · Cited by 47 · see citing works

Design and Synthesis of AX7574: A Microcystin-Derived, Fluorescent Probe for Serine/Threonine Phosphatases

Shreder, K. R., Liu, Y., Nomanhboy, T., Fuller, S. R., Wong, M. S., Gai, W. Z., Wu, J., Leventhal, P. S., Lill, J. R., & Corral, S. (2004) · Bioconjugate Chemistry · doi:10.1021/bc0499580 · Cited by 46 · see citing works

On the mechanism of action of antibiotics which act as irreversible enzyme inhibitors

Rando, R. R. (1975) · Biochemical Pharmacology · doi:10.1016/0006-2952(75)90055-6 · Cited by 42 · see citing works

An Activity-Based Protein Profiling Probe for the Nicotinic Acetylcholine Receptor

Tantama, M., Lin, W.-C., & Licht, S. (2008) · Journal of the American Chemical Society · doi:10.1021/ja805868x · Cited by 41 · see citing works

Acetaminophen protein adducts: A review

Bond, G. R. (2009) · Clinical Toxicology · doi:10.1080/15563650801941831 · Cited by 39 · see citing works

Small molecule probes that target Ablkinase

Kalesh, K., Sim, D. S. B., Wang, J., Liu, K., Lin, Q., & Yao, S. Q. (2009) · Chemical Communications · doi:10.1039/b919888a · Cited by 36 · see citing works

Profiling protein tyrosine phosphatase activity with mechanistic probes

Krishnamurthy, D., & Barrios, A. M. (2009) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2009.07.017 · Cited by 23 · see citing works

Challenges for the 'chemical-systems' biologist

Simon, G. M., & Cravatt, B. F. (2008) · Nature Chemical Biology · doi:10.1038/nchembio1108-639 · Cited by 20 · see citing works

Second-generation epidermal growth factor tyrosine kinase inhibitors in non-small cell lung cancer

Mukherji, D., & Spicer, J. F. (2009) · Expert Opinion on Investigational Drugs · doi:10.1517/13543780902762843 · Cited by 17 · see citing works

Design of suicide substrates: an approach to the development of highly selective enzyme inhibitors as drugs

Penning, T. M. (1983) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(83)90369-3 · Cited by 13 · see citing works

Drugs as Haptens, Antigens, and Immunogens

Park, B. K., Sanderson, J. P., & Naisbitt, D. J. (2007) · KARGER eBooks · doi:10.1159/000104189 · Cited by 13 · see citing works

New modes of enzyme inactivator design

Rando, R. R. (1979) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(79)90060-9 · Cited by 3 · see citing works

Untitled work

Kolb (2001) · doi:10.1002/1521-3773(20010601)40:11

Click Chemistry for Drug Development and Diverse Chemical–Biology Applications

Prakasam, T., Matosiuk, D., & Jóźwiak, K. (2013) · Chemical Reviews · doi:10.1021/cr200409f · Cited by 1,907 · see citing works

The resurgence of covalent drugs

Singh, J., Petter, R. C., Baillie, T. A., & Whitty, A. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3410 · Cited by 1,873 · see citing works

How were new medicines discovered?

Swinney, D. C., & Anthony, J. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3480 · Cited by 1,812 · see citing works

Hijacking the E3 Ubiquitin Ligase Cereblon to Efficiently Target BRD4

Lu, J., Qian, Y., Altieri, M., Dong, H., Wang, J., Raina, K., Hines, J., Winkler, J. D., Crew, A. P., Coleman, K., et al. (2015) · Chemistry &amp; Biology · doi:10.1016/j.chembiol.2015.05.009 · Cited by 1,140 · see citing works

Recent progresses in small-molecule enzymatic fluorescent probes for cancer imaging

Liu, H.-W., Chen, L., Xu, C., Li, Z., Zhang, H., Zhang, X.-B., & Tan, W. (2018) · Chemical Society Reviews · doi:10.1039/c7cs00862g · Cited by 948 · see citing works

Developing Irreversible Inhibitors of the Protein Kinase Cysteinome

Liu, Q., Sabnis, Y. A., Zhao, Z., Zhang, T., Buhrlage, S. J., Jones, L. H., & Gray, N. S. (2013) · Chemistry & Biology · doi:10.1016/j.chembiol.2012.12.006 · Cited by 662 · see citing works

Covalent Modifiers: A Chemical Perspective on the Reactivity of α,β-Unsaturated Carbonyls with Thiols via Hetero-Michael Addition Reactions

Jackson, P. A., Widen, J. C., Harki, D. A., & Brummond, K. M. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00788 · Cited by 588 · see citing works

Targeted Covalent Inhibitors for Drug Design

Baillie, T. A. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201601091 · Cited by 578 · see citing works

Covalent inhibitors in drug discovery: from accidental discoveries to avoided liabilities and designed therapies

Bauer, R. A. (2015) · Drug Discovery Today · doi:10.1016/j.drudis.2015.05.005 · Cited by 534 · see citing works

A Perspective on the Kinetics of Covalent and Irreversible Inhibition

Strelow, J. M. (2017) · SLAS Discovery · doi:10.1177/1087057116671509 · Cited by 392 · see citing works

A road map to evaluate the proteome-wide selectivity of covalent kinase inhibitors

Lanning, B. R., Whitby, L. R., Dix, M. M., Douhan, J., Gilbert, A. M., Hett, E. C., Johnson, T., Joslyn, C. M., Kath, J. C., Niessen, S., et al. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1582 · Cited by 356 · see citing works

Redox Signaling by Reactive Electrophiles and Oxidants

Parvez, S., Long, M. J. C., Poganik, J. R., & Aye, Y. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00698 · Cited by 357 · see citing works

The emerging role of mass spectrometry-based proteomics in drug discovery

Meissner, F., Geddes‐McAlister, J., Mann, M., & Bantscheff, M. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00409-3 · Cited by 355 · see citing works

Chemical and Computational Methods for the Characterization of Covalent Reactive Groups for the Prospective Design of Irreversible Inhibitors

Flanagan, M. E., Abramite, J. A., Anderson, D. P., AULABAUGH, A. E., Dahal, U. P., Gilbert, A. M., Li, C., Montgomery, J. I., Oppenheimer, S. R., Ryder, T. F., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm501412a · Cited by 337 · see citing works

Advances in covalent kinase inhibitors

Abdeldayem, A., Raouf, Y. S., Constantinescu, S. N., Moriggl, R., & Gunning, P. T. (2020) · Chemical Society Reviews · doi:10.1039/c9cs00720b · Cited by 332 · see citing works

Rapid Covalent-Probe Discovery by Electrophile-Fragment Screening

Resnick, E., Bradley, A., Gan, J., Douangamath, A., Krojer, T., Sethi, R., Geurink, P. P., Aimon, A., Amitai, G., Bellini, D., et al. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b02822 · Cited by 335 · see citing works

Covalent inhibitors design and discovery.

De Cesco, S., Kurian, J., Dufresne, C., Mittermaier, A. K., & Moitessier, N. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.06.019 · Cited by 315 · see citing works

The pharmacological landscape and therapeutic potential of serine hydrolases

Bachovchin, D. A., & Cravatt, B. F. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3620 · Cited by 307 · see citing works

Electrophilic natural products and their biological targets

Gersch, M., Kreuzer, J., & Sieber, S. A. (2012) · Natural Product Reports · doi:10.1039/c2np20012k · Cited by 282 · see citing works

Structure- and Reactivity-Based Development of Covalent Inhibitors of the Activating and Gatekeeper Mutant Forms of the Epidermal Growth Factor Receptor (EGFR)

Ward, R. A., Anderton, M. J., Ashton, S., Bethel, P. A., Box, M., Butterworth, S., Colclough, N., Chorley, C. G., Chuaqui, C., Cross, D. A. E., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400822z · Cited by 279 · see citing works

Waste disposal—An attractive strategy for cancer therapy

Salami, J., & Crews, C. M. (2017) · Science · doi:10.1126/science.aam7340 · Cited by 279 · see citing works

Next generation 3D pharmacophore modeling

Schaller, D., Šribar, D., Noonan, T., Deng, L., Nguyen, T. N., Pach, S., Machalz, D., Bermúdez, M., & Wolber, G. (2020) · Wiley Interdisciplinary Reviews Computational Molecular Science · doi:10.1002/wcms.1468 · Cited by 276 · see citing works

Chemical Proteomics Identifies Druggable Vulnerabilities in a Genetically Defined Cancer

Bar-Peled, L., Kemper, E. K., Suciu, R. M., Vinogradova, E. V., Backus, K. M., Horning, B. D., Paul, T. A., Ichu, T.-A., Svensson, R. U., Olucha, J., et al. (2017) · Cell · doi:10.1016/j.cell.2017.08.051 · Cited by 262 · see citing works

Covalent docking using autodock: two-point attractor and flexible side chain methods.

Bianco, G., Forli, S., Goodsell, D. S., & Olson, A. J. (2016) · Protein Science · doi:10.1002/pro.2733 · Cited by 246 · see citing works

Click-generated triazole ureas as ultrapotent in vivo–active serine hydrolase inhibitors

Adibekian, A., Martin, B. R., Wang, C., Hsu, K., Bachovchin, D. A., Niessen, S., Hoover, H. S., & Cravatt, B. F. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.579 · Cited by 244 · see citing works

Lysine‐Targeting Covalent Inhibitors

Pettinger, J., Jones, K., & Cheeseman, M. D. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201707630 · Cited by 244 · see citing works

A proteome-wide atlas of lysine-reactive chemistry

Abbasov, M. E., Kavanagh, M. E., Ichu, T.-A., Lazear, M. R., Tao, Y., Crowley, V. M., Ende, C. W. A., Hacker, S. M., Ho, J. S., Dix, M. M., et al. (2021) · Nature Chemistry · doi:10.1038/s41557-021-00765-4 · Cited by 242 · see citing works

Mechanistic enzymology in drug discovery: a fresh perspective

Holdgate, G. A., Meek, T. D., & Grimley, R. L. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.219 · Cited by 224 · see citing works

Developing Covalent Protein Drugs via Proximity-Enabled Reactive Therapeutics

Li, Q., Qu, C., Klauser, P. C., Li, M., Zheng, F. J., Wang, N., Li, X., Zhang, Q., Fu, X., Wang, Q., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.028 · Cited by 214 · see citing works

Diverse Functional Roles of Reactive Cysteines

Pace, N. J., & Weerapana, E. (2012) · ACS Chemical Biology · doi:10.1021/cb3005269 · Cited by 205 · see citing works

Discovery of PF-04457845: A Highly Potent, Orally Bioavailable, and Selective Urea FAAH Inhibitor

Johnson, D. S., Stiff, C. M., Lazerwith, S. E., Kesten, S. R., Fay, L. K., Morris, M. J., Beidler, D. R., Liimatta, M. B., Smith, S. E., Dudley, D. T., et al. (2010) · ACS Medicinal Chemistry Letters · doi:10.1021/ml100190t · Cited by 200 · see citing works

Drug discovery considerations in the development of covalent inhibitors

Mah, R., Thomas, J. R., & Shafer, C. M. (2013) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.10.003 · Cited by 197 · see citing works

Systematic Evaluation of Bioorthogonal Reactions in Live Cells with Clickable HaloTag Ligands: Implications for Intracellular Imaging

Murrey, H. E., Judkins, J. C., Ende, C. W. A., Ballard, T. E., Fang, Y., Riccardi, K. A., Di, L., Guilmette, E. R., Schwartz, J. W., Fox, J. M., et al. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b06847 · Cited by 191 · see citing works

Observations on Screening-Based Research and Some Concerning Trends in the Literature

Baell, J. B. (2010) · Future Medicinal Chemistry · doi:10.4155/fmc.10.237 · Cited by 184 · see citing works

Expanding the Armory: Predicting and Tuning Covalent Warhead Reactivity

Lonsdale, R., Burgess, J., Colclough, N., Davies, N. L., Lenz, E. M., Orton, A. L., & Ward, R. A. (2017) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.7b00553 · Cited by 190 · see citing works

Erratum: Mechanistic enzymology in drug discovery: a fresh perspective

Holdgate, G. A., Meek, T. D., & Grimley, R. L. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.257 · Cited by 182 · see citing works

Drug discovery for a new generation of covalent drugs

Kalgutkar, A. S. S., & Dalvie, D. (2012) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2012.688744 · Cited by 169 · see citing works

Arylfluorosulfate‐Based Electrophiles for Covalent Protein Labeling: A New Addition to the Arsenal

Martín‐Gago, P., & Olsen, C. A. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201806037 · Cited by 167 · see citing works

Reactive-cysteine profiling for drug discovery

Maurais, A. J., & Weerapana, E. (2019) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2019.02.010 · Cited by 167 · see citing works

Promiscuity and Selectivity in Covalent Enzyme Inhibition: A Systematic Study of Electrophilic Fragments

Jöst, C., Nitsche, C., Scholz, T., Roux, L., & Klein, C. D. P. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm5006918 · Cited by 167 · see citing works

The Taxonomy of Covalent Inhibitors

Tuley, A., & Fast, W. L. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00315 · Cited by 163 · see citing works

Comparative Evaluation of Covalent Docking Tools

Scarpino, A., Ferenczy, G. G., & Keserű, G. M. (2018) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.8b00228 · Cited by 152 · see citing works

Investigating the Proteome Reactivity and Selectivity of Aryl Halides

Shannon, D. A., Banerjee, R., Webster, E. R., Bak, D. W., Wang, C., & Weerapana, E. (2014) · Journal of the American Chemical Society · doi:10.1021/ja4116204 · Cited by 143 · see citing works

Selective and reversible modification of kinase cysteines with chlorofluoroacetamides

Shindo, N., Fuchida, H., Sato, M., Watari, K., Shibata, T., Kuwata, K., Miura, C., Okamoto, K., Hatsuyama, Y., Tokunaga, K., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-018-0204-3 · Cited by 137 · see citing works

Proteome-Wide Reactivity Profiling Identifies Diverse Carbamate Chemotypes Tuned for Serine Hydrolase Inhibition

Chang, J. W., Cognetta, A. B., Niphakis, M. J., & Cravatt, B. F. (2013) · ACS Chemical Biology · doi:10.1021/cb400261h · Cited by 134 · see citing works

A road map for prioritizing warheads for cysteine targeting covalent inhibitors

Ábrányi‐Balogh, P., Petri, L., Imre, T., Szijj, P. A., Scarpino, A., Hrast, M., Mitrović, A., Fonović, U. P., Németh, K., Barreteau, H., et al. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.10.010 · Cited by 132 · see citing works

Preclinical Efficacy and Anti-Inflammatory Mechanisms of Action of the Bruton Tyrosine Kinase Inhibitor Rilzabrutinib for Immune-Mediated Disease

Langrish, C. L., Bradshaw, J. M., Francesco, M. R., Owens, T. D., Xing, Y., Shu, J., LaStant, J., Bisconte, A. R., Outerbridge, C. A., White, S. D., et al. (2021) · The Journal of Immunology · doi:10.4049/jimmunol.2001130 · Cited by 132 · see citing works

Producing irreversible topoisomerase II-mediated DNA breaks by site-specific Pt(II)-methionine coordination chemistry

Wang, Y.-R., Chen, S.-F., Wu, C.-C., Liao, Y.-W., Lin, T.-S., Liu, K.-T., Chen, Y.-S., Li, T., Chien, T., & Chan, N. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx742 · Cited by 129 · see citing works

Diacylfuroxans Are Masked Nitrile Oxides That Inhibit GPX4 Covalently

Eaton, J. K., Ruberto, R. A., Kramm, A., Viswanathan, V. S., & Schreiber, S. L. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b10769 · Cited by 129 · see citing works

Small Molecule Binding Sites on the Ras:SOS Complex Can Be Exploited for Inhibition of Ras Activation

Winter, J., Anderson, M., Blades, K., Brassington, C., Breeze, A. L., Chresta, C. M., Embrey, K. J., Fairley, G., Faulder, P., Finlay, M. R. V., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/jm501660t · Cited by 126 · see citing works

Discovery of Branebrutinib (BMS-986195): A Strategy for Identifying a Highly Potent and Selective Covalent Inhibitor Providing Rapid in Vivo Inactivation of Bruton’s Tyrosine Kinase (BTK)

Watterson, S. H., Liu, Q., Bertrand, M. B., Batt, D. G., Li, L., Pattoli, M. A., Skala, S., Cheng, L., Obermeier, M. T., Moore, R., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00167 · Cited by 120 · see citing works

A Comprehensive Guide for Assessing Covalent Inhibition in Enzymatic Assays Illustrated with Kinetic Simulations

Mons, E., Roet, S., Kim, R. Q., & Mulder, M. P. C. (2022) · Current Protocols · doi:10.1002/cpz1.419 · Cited by 123 · see citing works

Recent Advances in Pro-PROTAC Development to Address On-Target Off-Tumor Toxicity

Chen, C., Yang, Y., Wang, Z., Li, H., Dong, C., & Zhang, X. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00302 · Cited by 117 · see citing works

Identification of Selective and Potent Inhibitors of Fibroblast Activation Protein and Prolyl Oligopeptidase

Poplawski, S. E., Lai, J. H.-S., Li, Y., Jin, Z., Liu, Y., Wu, W., Wu, Y. H., Zhou, Y., Sudmeier, J. L., Sanford, D. G., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400351a · Cited by 117 · see citing works

Development of a covalent inhibitor of gut bacterial bile salt hydrolases

Adhikari, A. A., Seegar, T. C. M., Ficarro, S. B., McCurry, M. D., Ramachandran, D., Yao, L., Chaudhari, S. N., Ndousse-Fetter, S., Banks, A. S., Marto, J. A., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0467-3 · Cited by 115 · see citing works

Potent and selective covalent inhibition of the papain-like protease from SARS-CoV-2

Sanders, B., Pokhrel, S., Labbe, A. D., Mathews, I. I., Cooper, C. J., Davidson, R. B., Phillips, G., Weiss, K. L., Zhang, Q., O’Neill, H., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-37254-w · Cited by 114 · see citing works

Targeting bacteria via iminoboronate chemistry of amine-presenting lipids

Bandyopadhyay, A., McCarthy, K. A., Kelly, M. A., & Gao, J. (2015) · Nature Communications · doi:10.1038/ncomms7561 · Cited by 113 · see citing works

A Genetically Encoded aza-Michael Acceptor for Covalent Cross-Linking of Protein–Receptor Complexes

Furman, J. L., Kang, M., Choi, S., Cao, Y. J., Wold, E. D., Sun, S. B., Smider, V. V., Schultz, P. G., & Kim, C. H. (2014) · Journal of the American Chemical Society · doi:10.1021/ja502851h · Cited by 111 · see citing works

Activity-based protein profiling for mapping and pharmacologically interrogating proteome-wide ligandable hotspots

Roberts, A. M., Ward, C. C., & Nomura, D. K. (2017) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2016.08.003 · Cited by 108 · see citing works

JDQ443, a Structurally Novel, Pyrazole-Based, Covalent Inhibitor of KRAS ^G12C for the Treatment of Solid Tumors

Lorthiois, E., Gerspacher, M., Beyer, K. S., Vaupel, A., Leblanc, C., Stringer, R., Weiss, A., Wilcken, R., Guthy, D. A., Lingel, A., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01438 · Cited by 110 · see citing works

New Electrophiles and Strategies for Mechanism-Based and Targeted Covalent Inhibitor Design

Ray, S., & Murkin, A. S. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00293 · Cited by 108 · see citing works

Proteome-wide Map of Targets of T790M-EGFR-Directed Covalent Inhibitors

Niessen, S., Dix, M. M., Barbas, S., Potter, Z. E., Lu, S., Brodsky, O., Planken, S., Behenna, D. C., Almaden, C., Gajiwala, K. S., et al. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.08.017 · Cited by 99 · see citing works

A Review of Small Molecule Inhibitors and Functional Probes of Human Cathepsin L

Dana, D., & Pathak, S. K. (2020) · Molecules · doi:10.3390/molecules25030698 · Cited by 82 · see citing works

Privileged scaffolds in lead generation

Zhao, H., & Dietrich, J. D. (2015) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2015.1041496 · Cited by 99 · see citing works

The design and development of covalent protein-protein interaction inhibitors for cancer treatment

Cheng, S.-S., Yang, G.-J., Wang, W., Leung, C.-H., & Ma, D.-L. (2020) · Journal of Hematology &amp; Oncology · doi:10.1186/s13045-020-00850-0 · Cited by 98 · see citing works

Versatile Bioconjugation Chemistries of ortho-Boronyl Aryl Ketones and Aldehydes

Cambray, S., & Gao, J. (2018) · Accounts of Chemical Research · doi:10.1021/acs.accounts.8b00154 · Cited by 93 · see citing works

Protein degradation technology: a strategic paradigm shift in drug discovery

Li, H., Dong, J., Cai, M., Xu, Z., Cheng, X., & Qin, J. (2021) · Journal of Hematology & Oncology · doi:10.1186/s13045-021-01146-7 · Cited by 94 · see citing works

Electrophilic warheads in covalent drug discovery: an overview

Péczka, N., Orgován, Z., Ábrányi‐Balogh, P., & Keserű, G. M. (2022) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2022.2034783 · Cited by 92 · see citing works

Modeling covalent-modifier drugs.

Awoonor-Williams, E., Walsh, A. G., & Rowley, C. N. (2017) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2017.05.009 · Cited by 90 · see citing works

Discovery of Brain-Penetrant, Irreversible Kynurenine Aminotransferase II Inhibitors for Schizophrenia

Dounay, A. B., Anderson, M. D., Bechle, B. M., Campbell, B. M., Claffey, M. M., Evdokimov, A. G., Evrard, E., Fonseca, K. R., Gan, X., Ghosh, S., et al. (2012) · ACS Medicinal Chemistry Letters · doi:10.1021/ml200204m · Cited by 89 · see citing works

Quantum Chemical-Based Protocol for the Rational Design of Covalent Inhibitors

Schirmeister, T., Kesselring, J., Jung, S., Schneider, T. H., Weickert, A., Becker, J., Lee, W., Bamberger, D., Wich, P. R., Distler, U., et al. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b03052 · Cited by 89 · see citing works

Discovery of Trifluoromethyl Glycol Carbamates as Potent and Selective Covalent Monoacylglycerol Lipase (MAGL) Inhibitors for Treatment of Neuroinflammation

McAllister, L. A., Butler, C. R., Mente, S., O’Neil, S. V., Fonseca, K. R., Piro, J. R., Cianfrogna, J. A., Foley, T. L., Gilbert, A. M., Harris, A. R., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00070 · Cited by 84 · see citing works

Strategic Design of Catalytic Lysine‐Targeting Reversible Covalent BCR‐ABL Inhibitors**

Quach, D., Tang, G., Anantharajan, J., Baburajendran, N., Poulsen, A., Wee, J. L. K., Retna, P., Li, R., Liu, B., Tee, D. H. Y., et al. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202105383 · Cited by 83 · see citing works

Selective inhibitors of JAK1 targeting an isoform-restricted allosteric cysteine

Kavanagh, M. E., Horning, B. D., Khattri, R., Roy, N., Lu, J. P., Whitby, L. R., Ye, E., Brannon, J. C., Parker, A., Chick, J. M., et al. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-01098-0 · Cited by 82 · see citing works

Vibralactone as a Tool to Study the Activity and Structure of the ClpP1P2 Complex from Listeria monocytogenes

Zeiler, E., Braun, N., Böttcher, T., Kastenmüller, A., Weinkauf, S., & Sieber, S. A. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201104391 · Cited by 82 · see citing works

Privileged Electrophile Sensors: A Resource for Covalent Drug Development

Long, M. J. C., & Aye, Y. (2017) · Cell Chemical Biology · doi:10.1016/j.chembiol.2017.05.023 · Cited by 81 · see citing works

Identification of Cys255 in HIF‐1α as a novel site for development of covalent inhibitors of HIF‐1α/ARNT PasB domain protein–protein interaction

Cardoso, R., Love, R., Nilsson, C. L., Bergqvist, S., Nowlin, D., Yan, J., Liu, K. K. ‐., Zhu, J., Chen, P., Deng, Y., et al. (2012) · Protein Science · doi:10.1002/pro.2172 · Cited by 79 · see citing works

Covalent Versus Non-covalent Enzyme Inhibition: Which Route Should We Take? A Justification of the Good and Bad from Molecular Modelling Perspective

Aljoundi, A., Bjij, I., El-Rashedy, A. A. E., & Soliman, M. E. S. (2020) · The Protein Journal · doi:10.1007/s10930-020-09884-2 · Cited by 78 · see citing works

Azetidine and Piperidine Carbamates as Efficient, Covalent Inhibitors of Monoacylglycerol Lipase

Butler, C. R., Beck, E. M., Harris, A. R., Huang, Z., McAllister, L. A., Ende, C. W. A., Fennell, K. F., Foley, T. L., Fonseca, K. R., Hawrylik, S. J., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01531 · Cited by 76 · see citing works

Intrinsic reactivity profile of electrophilic moieties to guide covalent drug design: N-α-acetyl- l -lysine as an amine nucleophile

Dahal, U. P., Gilbert, A. M., Obach, R. S., Flanagan, M. E., Chen, J. M., García-Irizarry, C. N., Starr, J. T., Schuff, B. P., Uccello, D. P., & Young, J. A. (2016) · MedChemComm · doi:10.1039/c6md00017g · Cited by 75 · see citing works

Designing Irreversible Inhibitors—Worth the Effort?

González‐Bello, C. (2016) · ChemMedChem · doi:10.1002/cmdc.201500469 · Cited by 74 · see citing works

Molecular Docking: A Structure-Based Approach for Drug Repurposing

Kumar, S., & Kumar, S. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-816125-8.00006-7 · Cited by 77 · see citing works

Targeting Non-Catalytic Cysteine Residues Through Structure-Guided Drug Discovery

Hallenbeck, K. K., Turner, D., Renslo, A. R., & Arkin, M. R. (2016) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026616666160719163839 · Cited by 71 · see citing works

Current Status and Perspectives of Protease Inhibitors and Their Combination with Nanosized Drug Delivery Systems for Targeted Cancer Therapy

Rudzińska, M., Dağlıoğlu, C., Savvateeva, L. V., Kacı, F. N., Antoine, R., & Zamyatnin, A. A. (2021) · Drug Design Development and Therapy · doi:10.2147/dddt.s285852 · Cited by 71 · see citing works

Discovery and structure–activity relationship studies of irreversible benzisothiazolinone-based inhibitors against Staphylococcus aureus sortase A transpeptidase

Zhulenkovs, D., Rudevica, Z., Jaudzems, K., Turks, M., & Leonchiks, A. (2014) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2014.09.011 · Cited by 71 · see citing works

Benchmarking in Vitro Covalent Binding Burden As a Tool To Assess Potential Toxicity Caused by Nonspecific Covalent Binding of Covalent Drugs

Dahal, U. P., Obach, R. S., & Gilbert, A. M. (2013) · Chemical Research in Toxicology · doi:10.1021/tx400301q · Cited by 71 · see citing works

Identification of Novel Malarial Cysteine Protease Inhibitors Using Structure-Based Virtual Screening of a Focused Cysteine Protease Inhibitor Library

Shah, F., Mukherjee, P., Gut, J., Legac, J., Rosenthal, P., Tekwani, B., & Avery, M. (2011) · Journal of Chemical Information and Modeling · doi:10.1021/ci200029y · Cited by 67 · see citing works

Design, Synthesis, and Evaluation of Piperazinyl Pyrrolidin-2-ones as a Novel Series of Reversible Monoacylglycerol Lipase Inhibitors

Aida, J., Fushimi, M., Kusumoto, T., Sugiyama, H., Arimura, N., Ikeda, S., Sasaki, M., Sogabe, S., Aoyama, K., & Koike, T. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00824 · Cited by 70 · see citing works

The Increasing Impact of Activity-Based Protein Profiling in Plant Science

Morimoto, K., & van der Hoorn, R. A. L. (2016) · Plant and Cell Physiology · doi:10.1093/pcp/pcw003 · Cited by 68 · see citing works

Toward the First Class of Suicide Inhibitors of Kallikreins Involved in Skin Diseases

Tan, X., Soualmia, F., Furio, L., Renard, J.-F., Kempen, I., Qin, L., Pagano, M., Pirotte, B., Amri, C. E., Hovnanian, A., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm500988d · Cited by 64 · see citing works

Discovery of a Series of 2,5-Diaminopyrimidine Covalent Irreversible Inhibitors of Bruton’s Tyrosine Kinase with in Vivo Antitumor Activity

Li, X., Zuo, Y., Tang, G., Wang, Y., Zhou, Y., Wang, X., Guo, T., Xia, M., Ding, N., & Pan, Z. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm4017762 · Cited by 64 · see citing works

Assigning functionality to cysteines by base editing of cancer dependency genes

Li, H., Ma, T., Remsberg, J. R., Won, S. J., DeMeester, K. E., Njomen, E., Ogasawara, D., Zhao, K. T., Huang, T. P., Lu, B., et al. (2023) · Nature Chemical Biology · doi:10.1038/s41589-023-01428-w · Cited by 62 · see citing works

Enhancing the anti-inflammatory activity of chalcones by tuning the Michael acceptor site

Rücker, H., Al‐Rifai, N., Rascle, A., Gottfried, E., Brodziak‐Jarosz, L., Gerhäuser, C., Dick, T. P., & Amslinger, S. (2015) · Organic & Biomolecular Chemistry · doi:10.1039/c4ob02301c · Cited by 60 · see citing works

Structure, mechanism, and dynamics of UDP-galactopyranose mutase

Tanner, J. J., Boechi, L., McCammon, J. A., & Sobrado, P. (2013) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2013.09.017 · Cited by 60 · see citing works

Kinetic Optimization of Lysine-Targeting Covalent Inhibitors of HSP72

Pettinger, J., Carter, M., Jones, K., & Cheeseman, M. D. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01709 · Cited by 59 · see citing works

Covalent peptides and proteins for therapeutics

Berdan, V. Y., Klauser, P. C., & Wang, L. (2020) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2020.115896 · Cited by 59 · see citing works

Lessons in Organic Fluorescent Probe Discovery

Wagh, S. B., Maslivetc, V. A., Clair, J. J. L., & Kornienko, A. (2021) · ChemBioChem · doi:10.1002/cbic.202100171 · Cited by 57 · see citing works

The perception of strigolactones in vascular plants

Lumba, S., Holbrook‐Smith, D., & McCourt, P. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2340 · Cited by 55 · see citing works

The Proteome‐Wide Potential for Reversible Covalency at Cysteine

Senkane, K., Vinogradova, E. V., Suciu, R. M., Crowley, V. M., Zaro, B. W., Bradshaw, J. M., Brameld, K. A., & Cravatt, B. F. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201905829 · Cited by 57 · see citing works

O-Hydroxyacetamide Carbamates as a Highly Potent and Selective Class of Endocannabinoid Hydrolase Inhibitors

Niphakis, M. J., Johnson, D. S., Ballard, T. E., Stiff, C. M., & Cravatt, B. F. (2011) · ACS Chemical Neuroscience · doi:10.1021/cn200089j · Cited by 56 · see citing works

Targeted Covalent Enzyme Inhibitors

Noe, M. C., & Gilbert, A. M. (2012) · Annual reports in medicinal chemistry · doi:10.1016/b978-0-12-396492-2.00027-8 · Cited by 39 · see citing works

Drug discovery for a new generation of covalent drugs

Kalgutkar, A. S. S., & Dalvie, D. (2012) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2012.688744 · Cited by 169 · see citing works

The Current Toolbox for Covalent Inhibitors: From Hit Identification to Drug Discovery

You, M., Liu, H. S., & Li, C. (2025) · JACS Au · doi:10.1021/jacsau.5c01134 · Cited by 17 · see citing works

The Taxonomy of Covalent Inhibitors

Tuley, A., & Fast, W. L. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00315 · Cited by 163 · see citing works

Global Assessment of Drug Target Engagement and Selectivity of Covalent Cysteine-Reactive Inhibitors Using Alkyne-Functionalized Probes

Rothweiler, E. M., & Huber, K. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-3397-7_14 · Cited by 1 · see citing works