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

Can the pharmaceutical industry reduce attrition rates?

Kola, I., & Landis, J. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1470 · Cited by 4,167

A systematic review of the associations between dose regimens and medication compliance

Claxton, A. J., Cramer, J., & Pierce, C. (2001) · Clinical Therapeutics · doi:10.1016/s0149-2918(01)80109-0 · Cited by 2,388

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

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

Identifying and Characterizing Binding Sites and Assessing Druggability

Halgren, T. A. (2009) · Journal of Chemical Information and Modeling · doi:10.1021/ci800324m · Cited by 1,808

The Bruton tyrosine kinase inhibitor PCI-32765 blocks B-cell activation and is efficacious in models of autoimmune disease and B-cell malignancy

Honigberg, L. A., Smith, A. M., Sirisawad, M., Verner, E., Loury, D., Chang, B., Li, S., Pan, Z., Thamm, D. H., Miller, R. A., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1004594107 · Cited by 1,561

ACETAMINOPHEN-INDUCED HEPATIC NECROSIS. II. ROLE OF COVALENT BINDING IN VIVO

Jollow, D. J., Mitchell, J. R., Potter, W. Z., Davis, D. C., Gillette, J. R., & Brodie, B. B. (1973) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(25)29664-1 · Cited by 1,203

Fumaric acid esters exert neuroprotective effects in neuroinflammation via activation of the Nrf2 antioxidant pathway

Linker, R. A., Lee, D.-H., Ryan, S., van Dam, A. M., Conrad, R., Bista, P., Zeng, W., Hronowsky, X., Buko, A., Chollate, S., et al. (2011) · Brain · doi:10.1093/brain/awq386 · Cited by 1,155

Acetaminophen-Induced Hepatic Necrosis

Jollow, D. J., Thorgeirsson, S. S., Potter, W. Z., Hashimoto, M., & Mitchell, J. R. (2008) · Pharmacology · doi:10.1159/000136547 · Cited by 1,091

The quest to overcome resistance to EGFR-targeted therapies in cancer

Chong, C. R., & Janne, P. A. (2013) · Nature Medicine · doi:10.1038/nm.3388 · Cited by 1,076

Covalent small-molecule inhibitors of SARS-CoV-2 Mpro: Insights into their design, classification, biological activity, and binding interactions

Shawky, A. M., Almalki, F. A., Alzahrani, H. A., Abdalla, A. N., Youssif, B. G. M., Ibrahim, N. A., Gamal, M., El-Sherief, H. A. M., Abdel‐Fattah, M. M., Hefny, A. A., et al. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116704 · Cited by 26

Repurposing existing drugs: identification of irreversible IMPDH inhibitors by high-throughput screening

Sarwono, A. E. Y., Mitsuhashi, S., Kabir, M. H. B., Shigetomi, K., Okada, T., Ohsaka, F., Otsuguro, S., Maenaka, K., Igarashi, M., Kato, K., et al. (2018) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2018.1540474 · Cited by 25

Tuning isoform selectivity and bortezomib sensitivity with a new class of alkenyl indene PDI inhibitor

Robinson, R. M., Reyes, L., Duncan, R. M., Bian, H., Strobel, E. D., Hyman, S. L., Reitz, A. B., & Dolloff, N. G. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.111906 · Cited by 25

Discovery of a novel covalent CDK4/6 inhibitor based on palbociclib scaffold

Shan, H., Ma, X., Yan, G., Luo, M., Zhong, X.-X., Lan, S., Yang, J., Liu, Y., Pu, C., Yu, T., et al. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113432 · Cited by 25

Prioritisation of Compounds for 3CLpro Inhibitor Development on SARS-CoV-2 Variants

Jukič, M., Škrlj, B., Tomšič, G., Pleško, S., Podlipnik, Č., & Bren, U. (2021) · Molecules · doi:10.3390/molecules26103003 · Cited by 28

Combined Biophysical Chemistry Reveals a New Covalent Inhibitor with a Low-Reactivity Alkyl Halide

Li, T., Maltais, R., Poirier, D., & Lin, S. (2018) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.8b02225 · Cited by 25

Phosphono Bisbenzguanidines as Irreversible Dipeptidomimetic Inhibitors and Activity‐Based Probes of Matriptase‐2

Häußler, D., Mangold, M., Furtmann, N., Braune, A., Blaut, M., Bajorath, J., Stirnberg, M., & Gütschow, M. (2016) · Chemistry - A European Journal · doi:10.1002/chem.201600206 · Cited by 25

Phenylthiomethyl Ketone-Based Fragments Show Selective and Irreversible Inhibition of Enteroviral 3C Proteases

Schulz, R., Atef, A., Becker, D., Gottschalk, F., Tauber, C., Wagner, S., Arkona, C., ABDEL‐HAFEZ, A. A., Farag, H. H. A., Rademann, J., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01440 · Cited by 25

Discovery of Michael acceptor containing 1,4-dihydropyridines as first covalent inhibitors of L-/T-type calcium channels

Cevher, H. A., Schaller, D., Gandini, M. A., Kaplan, O., Gambeta, E., Zhang, F. X., Çelebi̇er, M., Tahir, M. N., Zamponi, G. W., Wolber, G., et al. (2019) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2019.103187 · Cited by 25

Development of ERK1/2 inhibitors as a therapeutic strategy for tumour with MAPK upstream target mutations

Miao, L., & Tian, H. (2019) · Journal of drug targeting · doi:10.1080/1061186x.2019.1648477 · Cited by 24

Highly stereoselective organocatalytic synthesis of pyrrolidinyl spirooxindoles containing halogenated contiguous quaternary carbon stereocenters

Chen, F.-Y., Li, X., Zhan, G., Liu, H., Kang, B., Zhang, S.-C., Peng, C. Y., & Han, B. (2020) · Tetrahedron Letters · doi:10.1016/j.tetlet.2020.151806 · Cited by 24

Characterization of an aromatic trifluoromethyl ketone as a new warhead for covalently reversible kinase inhibitor design

Zhang, Z., Wang, Y., Chen, X., Song, X., Tu, Z., Chen, Y., Zhang, Z., & Ding, K. (2021) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2021.116457 · Cited by 24

Exploration of BAY 11-7082 as a Potential Antibiotic

Coles, V. E., Darveau, P., Zhang, X., Harvey, H., Henriksbo, B. D., Yang, A., Schertzer, J. D., Magolan, J., & Burrows, L. L. (2021) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.1c00522 · Cited by 25

Interactions between Microtubule-Associated Protein Tau (MAPT) and Small MoleculesPreprint

Rauch, J. N., Olson, S. H., & Gestwicki, J. E. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024034 · Cited by 22

Synthesis of Diverse N-Acryloyl Azetidines and Evaluation of Their Enhanced Thiol Reactivities

Palkowitz, M. D., Tan, B., Hu, H., Roth, K. D. W., & Bauer, R. A. (2017) · Organic Letters · doi:10.1021/acs.orglett.7b00788 · Cited by 23

Modulation of nuclear receptor function: Targeting the protein-DNA interface

Filho, H. V. R., Tambones, I., Dias, M. M. G., Videira, N. B., Bruder, M., Amato, A. A., & Figueira, A. C. M. (2019) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2019.01.023 · Cited by 24

Boosting the Discovery of Small Molecule Inhibitors of Glucose-6-Phosphate Dehydrogenase for the Treatment of Cancer, Infectious Diseases, and Inflammation

Koperniku, A., Garcia, A. A., & Mochly‐Rosen, D. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01577 · Cited by 23

Covalent inhibitors of bacterial peptidoglycan biosynthesis enzyme MurA with chloroacetamide warhead

Grabrijan, K., Hrast, M., Proj, M., Dolšak, A., Zdovc, I., Imre, T., Petri, L., Ábrányi‐Balogh, P., Keserű, G. M., & Gobec, S. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114752 · Cited by 24

Machine Learning Models to Interrogate Proteome-Wide Covalent Ligandabilities Directed at Cysteines

Liu, R., Clayton, J., Shen, M., Bhatnagar, S., & Shen, J. (2024) · JACS Au · doi:10.1021/jacsau.3c00749 · Cited by 23

Discovery of an Irreversible and Cell-Active BCL6 Inhibitor Selectively Targeting Cys53 Located at the Protein–Protein Interaction Interface

Sameshima, T., Yamamoto, T., Sano, O., Sogabe, S., Igaki, S., Sakamoto, K., Ida, K., Gotou, M., Imaeda, Y., Sakamoto, J., et al. (2018) · Biochemistry · doi:10.1021/acs.biochem.7b00732 · Cited by 23

Shining light on cysteine modification: connecting protein conformational dynamics to catalysis and regulation

van den Bedem, H., & Wilson, M. A. (2019) · Journal of Synchrotron Radiation · doi:10.1107/s160057751900568x · Cited by 25

A Simple Protocol for the Stereoselective Construction of Enaminyl Sulfonyl Fluorides

Leng, J., Tang, W., Fang, W., Zhao, C., & Qin, H. (2020) · Organic Letters · doi:10.1021/acs.orglett.0c01360 · Cited by 23

Covalent Kinase Inhibitors: An Overview

Gehringer, M. (2020) · Topics in medicinal chemistry · doi:10.1007/7355_2020_103 · Cited by 24

Histidine-Covalent Stapled Alpha-Helical Peptides Targeting hMcl-1

Alboreggia, G., Udompholkul, P., Baggio, C., Muzzarelli, K. M., Assar, Z., & Pellecchia, M. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c00277 · Cited by 22

Auf Lysin zielende, kovalente Inhibitoren

Pettinger, J., Jones, K., & Cheeseman, M. D. (2017) · Angewandte Chemie · doi:10.1002/ange.201707630 · Cited by 22

Design and SAR Analysis of Covalent Inhibitors Driven by Hybrid QM/MM Simulations

Lodola, A., Callegari, D., Scalvini, L., Rivara, S., & Mor, M. (2020) · Methods in molecular biology · doi:10.1007/978-1-0716-0282-9_19 · Cited by 24

Improved Electrophile Design for Exquisite Covalent Molecule Selectivity

Montaño, J. L., Wang, B. J., Volk, R. F., Warrington, S. E., Garda, V. G., Hofmann, K. L., Chen, L. C., & Zaro, B. W. (2022) · ACS Chemical Biology · doi:10.1021/acschembio.1c00980 · Cited by 21

Relative Nuclease Resistance of a DNA Aptamer Covalently Conjugated to a Target Protein

Tabuchi, Y., Yang, J., & Taki, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23147778 · Cited by 21

Technologies for Direct Detection of Covalent Protein–Drug Adducts

Mons, E., Kim, R. Q., & Mulder, M. P. C. (2023) · Pharmaceuticals · doi:10.3390/ph16040547 · Cited by 23

Discovery of reactive peptide inhibitors of human papillomavirus oncoprotein E6

Ye, X., Zhang, P., Tao, J., Wang, J. C. K., Mafi, A., Grob, N. M., Quartararo, A. J., Baddock, H. T., Chan, L. J. G., McAllister, F. E., et al. (2023) · Chemical Science · doi:10.1039/d3sc02782a · Cited by 25

Peptide-Based Covalent Inhibitors Bearing Mild Electrophiles to Target a Conserved His Residue of the Bacterial Sliding Clamp

Compain, G., Monsarrat, C., Blagojevic, J., Brillet, K., Dumas, P., Hammann, P., Kühn, L., Martiel, I., Engilberge, S., Oliéric, V., et al. (2024) · JACS Au · doi:10.1021/jacsau.3c00572 · Cited by 22

DUckCov: a Dynamic Undocking‐Based Virtual Screening Protocol for Covalent Binders

Rachman, M. M., Scarpino, A., Bajusz, D., Pálfy, G., Vida, I., Perczel, A., Barril, X., & Keserű, G. M. (2019) · ChemMedChem · doi:10.1002/cmdc.201900078 · Cited by 22

Discovery of Irreversible p97 Inhibitors

Ding, R., Zhang, T., Wilson, D. J., Xie, J., Williams, J. M., Xu, Y., Ye, Y., & Chen, L. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00144 · Cited by 22

Covalent Targeting of Histidine Residues with Aryl Fluorosulfates: Application to Mcl-1 BH3 Mimetics

Alboreggia, G., Udompholkul, P., Atienza, E. L., Muzzarelli, K. M., Assar, Z., & Pellecchia, M. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c01541 · Cited by 21

Covalent-Allosteric Inhibitors: Do We Get the Best of Both Worlds?

Tao, H., Yang, B., Farhangian, A., Xu, K., Li, T., Zhang, Z., & Li, J. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c02760 · Cited by 21

The NLRP3 Inflammasome in the Pathogenesis and Treatment of Alzheimer’s Disease

Golzari-Sorkheh, M., Brown, C. E., Weaver, D. F., & Reed, M. A. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210660 · Cited by 21

Systematic Exploration of Privileged Warheads for Covalent Kinase Drug Discovery

Zhao, Z., & Bourne, P. E. (2022) · Pharmaceuticals · doi:10.3390/ph15111322 · Cited by 19

Discovery and Preclinical Characterization of BIIB129, a Covalent, Selective, and Brain-Penetrant BTK Inhibitor for the Treatment of Multiple Sclerosis

Himmelbauer, M. K., Bajrami, B., Basile, R., Capacci, A. G., Chen, T., Choi, C. K., Gilfillan, R., de Turiso, F. G.-L., Gu, C., Hoemberger, M., et al. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c00220 · Cited by 22

Identification and characterization of the novel reversible and selective cathepsin X inhibitors

Fonović, U. P., Mitrović, A., Knez, D., Jakoš, T., Pišlar, A. H., Brus, B., Doljak, B., Stojan, J., Žakelj, S., Trontelj, J., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-11935-1 · Cited by 21

Multiscale Simulations of Clavulanate Inhibition Identify the Reactive Complex in Class A β-Lactamases and Predict the Efficiency of Inhibition

Fritz, R. A., Alzate‐Morales, J. H., SPENCER, J. M., Mulholland, A. J., & van der Kamp, M. W. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00480 · Cited by 20

Covalent Simulations of Covalent/Irreversible Enzyme Inhibition in Drug Discovery: A Reliable Technical Protocol

Khan, S., Bjij, I., Olotu, F. A., Agoni, C., Adeniji, E. A., & Soliman, M. E. S. (2018) · Future Medicinal Chemistry · doi:10.4155/fmc-2017-0304 · Cited by 20

Opportunities and challenges for the development of covalent chemical immunomodulators

Backus, K. M., Cao, J. X., & Maddox, S. M. (2019) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2019.05.050 · Cited by 21

Discovery and optimization of selective FGFR4 inhibitors via scaffold hopping

Wang, Y., Chen, Z., Dai, M., Sun, P., Wang, C., Gao, Y., Zhao, H., Zeng, W., Shen, L., Mao, W., et al. (2017) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2017.04.014 · Cited by 21

A perspective on the changing landscape of HTS

Lanne, A., Usselmann, L. E. J., Llowarch, P., Michaelides, I. N., Fillmore, M. C., & Holdgate, G. A. (2023) · Drug Discovery Today · doi:10.1016/j.drudis.2023.103670 · Cited by 20

Evaluation of a Covalent Library of Diverse Warheads (CovLib) Binding to JNK3, USP7, or p53

Klett, T., Schwer, M., Ernst, L. N., Engelhardt, M. U., Jaag, S., Masberg, B., Knappe, C., Lämmerhofer, M., Gehringer, M., & Boeckler, F. M. (2024) · Drug Design Development and Therapy · doi:10.2147/dddt.s466829 · Cited by 21

Does Size Really Matter? Probing the Efficacy of Structural Reduction in the Optimization of Bioderived Compounds – A Computational “Proof-of-Concept”

Olotu, F. A., Munsamy, G., & Soliman, M. E. S. (2018) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2018.11.005 · Cited by 20

Mass spectrometry based proteomic approach for the screening of butyrylcholinesterase adduct formation with organophosphates

Dubrovskii, Y. A., Murashko, E. A., Chuprina, O., Beltyukov, P. P., Radilov, A. S., Solovyev, N. D., & Babakov, V. (2019) · Talanta · doi:10.1016/j.talanta.2019.01.059 · Cited by 20

Discovery of Non-Cysteine-Targeting Covalent Inhibitors by Activity-Based Proteomic Screening with a Cysteine-Reactive Probe

Jung, Y., Noda, N., Takaya, J., Abo, M., Toh, K., Tajiri, K., Cui, C., Zhou, L., Sato, S., & Uesugi, M. (2022) · ACS Chemical Biology · doi:10.1021/acschembio.1c00824 · Cited by 20

A covalent strategy to target intrinsically disordered proteins: Discovery of novel tau aggregation inhibitors

Petri, L., Ábrányi‐Balogh, P., Vagrys, D., Imre, T., Varró, N., Mándity, I. M., Rácz, A., Wittner, L., Tóth, K., Tóth, E. Z., et al. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114163 · Cited by 21

Chemo- and Site-Selective Lysine Modification of Peptides and Proteins under Native Conditions Using the Water-Soluble Zolinium

Sun, H., Xi, M., Jin, Q., Zhu, Z., Zhang, Y., Jia, G., Zhu, G., Sun, M., Zhang, H., Ren, X., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00937 · Cited by 20

Discovering covalent cyclic peptide inhibitors of peptidyl arginine deiminase 4 (PADI4) using mRNA-display with a genetically encoded electrophilic warhead

Mathiesen, I. R., Calder, E. D. D., Kunzelmann, S., & Walport, L. J. (2024) · Communications Chemistry · doi:10.1038/s42004-024-01388-9 · Cited by 18

Selective alkylation of T–T mismatched DNA using vinyldiaminotriazine–acridine conjugate

Onizuka, K., Usami, A., Yamaoki, Y., Kobayashi, T., Hazemi, M. E., Chikuni, T., Sato, N., Sasaki, K., Katahira, M., & Nagatsugi, F. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx1278 · Cited by 18

Targeting HCV polymerase: a structural and dynamic perspective into the mechanism of selective covalent inhibition

Shunmugam, L., & Soliman, M. E. S. (2018) · RSC Advances · doi:10.1039/c8ra07346e · Cited by 18

Converting (E)‐(Hetero)arylethanesulfonyl Fluorides to (Z)‐(Hetero)arylethanesulfonyl Fluorides Under Light Irradiation

Huang, Y., Wang, S., Leng, J., Moku, B., Zhao, C., Alharbi, N. S., & Qin, H. (2019) · European Journal of Organic Chemistry · doi:10.1002/ejoc.201900799 · Cited by 20

Systematic Search for SARS-CoV-2 Main Protease Inhibitors for Drug Repurposing: Ethacrynic Acid as a Potential Drug

Isgrò, C., Sardanelli, A. M., & Palese, L. L. (2021) · Viruses · doi:10.3390/v13010106 · Cited by 18

Synthetic Methodology-driven Chemical Protein Modifications

Maruyama, K., & Kanai, M. (2019) · Chemistry Letters · doi:10.1246/cl.190652 · Cited by 18

Bis-Michael Acceptors as Novel Probes to Study the Keap1/Nrf2/ARE Pathway

Deny, L. J., Traboulsi, H., Cantin, A. M., Marsault, É., Richter, M. V., & Bélanger, G. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01132 · Cited by 17

Enantioselective assembly of 3,3-disubstituted succinimides via three-component reaction of vinyl diazosuccinimides with alcohols and imines

Yuan, H., Hong, K., Liu, X., Qian, Y., Xu, X., & Hu, W. (2021) · Chemical Communications · doi:10.1039/d1cc02876f · Cited by 17

Structural Insights into Notum Covalent Inhibition

Zhao, Y., Svensson, F., Steadman, D., Frew, S., Monaghan, A. E., Bictash, M., Moreira, T., Chalk, R., Lu, W., Fish, P. V., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00701 · Cited by 17

Computer simulation of molecular recognition in biomolecular system: from in silico screening to generalized ensembles

Fukunishi, Y., Higo, J., & Kasahara, K. (2022) · Biophysical Reviews · doi:10.1007/s12551-022-01015-8 · Cited by 18

Inhibition of SARS-CoV-2 main protease: a repurposing study that targets the dimer interface of the protein

Pekel, H., Ilter, M., & Şensoy, Ö. (2021) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2021.1910571 · Cited by 16

Dipeptide-Derived Alkynes as Potent and Selective Irreversible Inhibitors of Cysteine Cathepsins

Behring, L., Ruiz-Gómez, G., Trapp, C., Morales, M., Wodtke, R., Köckerling, M., Kopka, K., Pisabarro, M. T., Pietzsch, J., & Löser, R. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01360 · Cited by 11

Landscape of In Silico Tools for Modeling Covalent Modification of Proteins: A Review on Computational Covalent Drug Discovery

Hasan, M. N., Ray, M., & Saha, A. (2023) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.3c04710 · Cited by 16

Targeted degradation of Pin1 by protein-destabilizing compounds

Alboreggia, G., Udompholkul, P., Rodriguez, I., Blaha, G. M., & Pellecchia, M. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2403330121 · Cited by 15

Identification of a novel boronic acid as a potent, selective, and orally active hormone sensitive lipase inhibitor

Ogiyama, T., Yamaguchi, M., Kurikawa, N., Honzumi, S., Yamamoto, Y., Sugiyama, D., & Inoue, S. (2016) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2016.06.022 · Cited by 16

Importance of the Proximity and Orientation of Ligand-Linkage to the Design of Cinnamate-GW9662 Hybrid Compounds as Covalent PPARγ Agonists

Utsugi, Y., Kobuchi, H., Kawamura, Y., Atito, A. S. A., Nagao, M., Isoda, H., & Miyamae, Y. (2019) · Molecules · doi:10.3390/molecules24102019 · Cited by 16

Elucidating target specificity of the taccalonolide covalent microtubule stabilizers employing a combinatorial chemical approach

Du, L., Yee, S. S., Karthik, R., & Risinger, A. L. (2020) · Nature Communications · doi:10.1038/s41467-019-14277-w · Cited by 16

Synthesis of α-Aminophosphonic Acid Derivatives Through the Addition of O- and S-Nucleophiles to 2H-Azirines and Their Antiproliferative Effect on A549 Human Lung Adenocarcinoma Cells

Carramiñana, V., de Retana, A. M. O., Palácios, F., & Santos, J. M. D. L. (2020) · Molecules · doi:10.3390/molecules25153332 · Cited by 16

Convenient preparation of (E)-3-arylidene-4-diazopyrrolidine-2,5-diones in array format

Chupakhin, E. G., Kantin, G. P., Dar’in, D. V., & Krasavin, M. (2021) · Mendeleev Communications · doi:10.1016/j.mencom.2021.01.010 · Cited by 16

Inhibitors of rhomboid proteases

Wolf, E. V., & Verhelst, S. H. L. (2015) · Biochimie · doi:10.1016/j.biochi.2015.07.007 · Cited by 16

Guidelines for the Synthesis of Small‐Molecule Irreversible Probes Targeting G Protein‐Coupled Receptors

Jörg, M., & Scammells, P. J. (2016) · ChemMedChem · doi:10.1002/cmdc.201600066 · Cited by 16

Extended Applications of Small-Molecule Covalent Inhibitors toward Novel Therapeutic Targets

Lee, J., & Park, S. B. (2022) · Pharmaceuticals · doi:10.3390/ph15121478 · Cited by 16

Turn On, Tune In, Turnover! Target Biology Impacts In Vivo Potency, Efficacy, and Clearance

Gabrielsson, J., & Hjorth, S. (2023) · Pharmacological Reviews · doi:10.1124/pharmrev.121.000524 · Cited by 15

Integrated Synthetic, Biophysical, and Computational Investigations of Covalent Inhibitors of Prolyl Oligopeptidase and Fibroblast Activation Protein α

Plescia, J., Cesco, S. D., Patrascu, M. B., Kurian, J., Trani, J. M. D., Dufresne, C., Wahba, A. S., Janmamode, N., Mittermaier, A., & Moitessier, N. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00642 · Cited by 16

Selective Glucocorticoid Receptor Properties of GSK866 Analogs with Cysteine Reactive Warheads

Chirumamilla, C. S., Palagani, A., Kamaraj, B., Declerck, K., Verbeek, M. W. C., Oksana, R., Bosscher, K. D., Bougarne, N., Ruttens, B., Gevaert, K., et al. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01324 · Cited by 15

Exploiting Cysteine Residues of SLC Membrane Transporters as Targets for Drugs

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Discovery of Immunoproteasome Inhibitors Using Large-Scale Covalent Virtual Screening

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Covalent Probes for Carbohydrate-Active Enzymes: From Glycosidases to Glycosyltransferases

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