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

Can the pharmaceutical industry reduce attrition rates?

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

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

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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

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

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

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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

Triazine-Based Covalent DNA-Encoded Libraries for Discovery of Covalent Inhibitors of Target Proteins

Li, L., Su, M., Lu, W., Song, H., Liu, J., Wen, X., Suo, Y., Qi, J., Luo, X., Zhou, Y., et al. (2022) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.2c00127 · Cited by 54

Parthenolide Inhibits STAT3 Signaling by Covalently Targeting Janus Kinases

Liu, M., Xiao, C., Sun, M., Tan, M., Hu, L., & Yu, Q. (2018) · Molecules · doi:10.3390/molecules23061478 · Cited by 55

Docking covalent targets for drug discovery: stimulating the computer-aided drug design community of possible pitfalls and erroneous practices

Oyedele, A.-Q. K., Ogunlana, A. T., Boyenle, I. D., Adeyemi, A. O., Temionu, O. R., Adelusi, T. I., Abdul-Hammed, M., Elegbeleye, O. E., & Odunitan, T. T. (2022) · Molecular Diversity · doi:10.1007/s11030-022-10523-4 · Cited by 53

Design and synthesis of substituted dihydropyrimidinone derivatives as cytotoxic and tubulin polymerization inhibitors

Sana, S., Tokala, R., Bajaj, D. M., Nagesh, N., Bokara, K. K., Kiranmai, G., Lakshmi, U. J., Vadlamani, S., Talla, V., & Shankaraiah, N. (2019) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2019.103317 · Cited by 52

Designed covalent allosteric modulators: an emerging paradigm in drug discovery

Lu, S., & Zhang, J. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2016.11.013 · Cited by 53

An overview of potential inhibitors targeting non-structural proteins 3 (PL pro and Mac1) and 5 (3CL pro /M pro ) of SARS-CoV-2

Yan, F., & Gao, F. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.08.036 · Cited by 52

CovPDB: a high-resolution coverage of the covalent protein–ligand interactome

Gao, M., Moumbock, A. F. A., Qaseem, A., Xu, Q., & Günther, S. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab868 · Cited by 52

Discovery of Covalent Ligands via Noncovalent Docking by Dissecting Covalent Docking Based on a “Steric-Clashes Alleviating Receptor (SCAR)” Strategy

Ai, Y.-B., Yu, L.-L., Tan, X., Chai, X., & Liu, S. (2016) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.6b00334 · Cited by 52

Two‐Component Stapling of Biologically Active and Conformationally Constrained Peptides: Past, Present, and Future

Iegre, J., Gaynord, J. S., Robertson, N., Sore, H. F., Hyvönen, M., & Spring, D. R. (2018) · Advanced Therapeutics · doi:10.1002/adtp.201800052 · Cited by 54

Tunable Cysteine-Targeting Electrophilic Heteroaromatic Warheads Induce Ferroptosis

Karaj, E., Sindi, S. H., Kuganesan, N., Perera, L., Taylor, W. R., & Tillekeratne, L. M. V. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00909 · Cited by 52

Biospecific Chemistry for Covalent Linking of Biomacromolecules

Cao, L., & Wang, L. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00066 · Cited by 53

Discovery of N -Phenylpropiolamide as a Novel Succinate Dehydrogenase Inhibitor Scaffold with Broad-Spectrum Antifungal Activity on Phytopathogenic Fungi

Zhang, Y., Yang, S. S., Zhang, Q., Zhang, T., Zhang, T., Zhou, B., & Zhou, L. (2023) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.2c07712 · Cited by 51

Reactivity of Covalent Fragments and Their Role in Fragment Based Drug Discovery

McAulay, K., Bilsland, A. E., & Bon, M. (2022) · Pharmaceuticals · doi:10.3390/ph15111366 · Cited by 54

Medicinal Chemistry Insights in the Discovery of Novel LSD1 Inhibitors

Wang, X., Huang, B., Suzuki, T., Liu, X., & Zhan, P. (2015) · Epigenomics · doi:10.2217/epi.15.86 · Cited by 50

Coumaric acid derivatives as tyrosinase inhibitors: Efficacy studies through in silico, in vitro and ex vivo approaches

Varela, M. T., Ferrarini, M., Mercaldi, V. G., Sufi, B. D. S., Padovani, G., Nazato, L. I. S., & Fernandes, J. P. S. (2020) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2020.104108 · Cited by 50

An electrophilic warhead library for mapping the reactivity and accessibility of tractable cysteines in protein kinases

Petri, L., Egyed, A., Bajusz, D., Imre, T., Hetényi, A., Martinek, T. A., Ábrányi‐Balogh, P., & Keserű, G. M. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112836 · Cited by 48

Approaches to selective fibroblast growth factor receptor 4 inhibition through targeting the ATP-pocket middle-hinge region

Fairhurst, R. A., Knöpfel, T. F., Leblanc, C., Buschmann, N., Gaul, C., Blank, J., Galuba, I., Trappe, J., Zou, C., Voshol, J., et al. (2017) · MedChemComm · doi:10.1039/c7md00213k · Cited by 48

Ferrous Iron-Dependent Pharmacology

Gonciarz, R. L., Collisson, E. A., & Renslo, A. R. (2020) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2020.11.003 · Cited by 47

Fluorovinylsulfones and -Sulfonates as Potent Covalent Reversible Inhibitors of the Trypanosomal Cysteine Protease Rhodesain: Structure–Activity Relationship, Inhibition Mechanism, Metabolism, and In Vivo Studies

Jung, S., Fuchs, N. S., Johé, P., Wagner, A., Diehl, E., Yuliani, T., Zimmer, C., Barthels, F., Zimmermann, R. A., Klein, P., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01002 · Cited by 46

Covalent EGFR Inhibitors: Binding Mechanisms, Synthetic Approaches, and Clinical Profiles

Hossam, M., Lasheen, D. S., & Abouzid, K. A. M. (2016) · Archiv der Pharmazie · doi:10.1002/ardp.201600063 · Cited by 45

BIreactive: A Machine-Learning Model to Estimate Covalent Warhead Reactivity

Palazzesi, F., Hermann, M. R., Grundl, M. A., Pautsch, A., Seeliger, D., Tautermann, C. S., & Weber, A. (2020) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.9b01058 · Cited by 46

Design, Synthesis, and Structural Characterization of Lysine Covalent BH3 Peptides Targeting Mcl-1

Gambini, L., Udompholkul, P., Baggio, C., Muralidharan, A., Kenjić, N., Assar, Z., Perry, J. J. P., & Pellecchia, M. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00005 · Cited by 46

New drug design with covalent modifiers

Adeniyi, A. A., Ramesh, M., & Soliman, M. E. S. (2016) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2016.1115478 · Cited by 46

Predicting Antiviral Resistance Mutations in SARS-CoV-2 Main Protease with Computational and Experimental Screening

Sasi, V. M., Ullrich, S., Ton, J., Fry, S. E., Johansen‐Leete, J., Payne, R. J., Nitsche, C., & Jackson, C. J. (2022) · Biochemistry · doi:10.1021/acs.biochem.2c00489 · Cited by 45

Differential impact of BTK active site inhibitors on the conformational state of full-length BTK

Joseph, R. E., Amatya, N., Fulton, D. B., Engen, J. R., Wales, T. E., & Andreotti, A. H. (2020) · eLife · doi:10.7554/elife.60470 · Cited by 47

Discovery of anti-MERS-CoV small covalent inhibitors through pharmacophore modeling, covalent docking and molecular dynamics simulation

Alamri, M. A., Qamar, M. T. U., Afzal, O., Alabbas, A. B., Riadi, Y., & Alqahtani, S. M. (2021) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2021.115699 · Cited by 45

Targeting key proteins involved in transcriptional regulation for cancer therapy: Current strategies and future prospective

Pei, H., Guo, W., Peng, Y., Xiong, H., & Chen, Y. (2022) · Medicinal Research Reviews · doi:10.1002/med.21886 · Cited by 45

CHARMM-GUI PDB Reader and Manipulator: Covalent Ligand Modeling and Simulation

Kong, L., Park, S., & Im, W. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168554 · Cited by 47

Regio- and Stereospecific Synthesis of Oridonin D-Ring Aziridinated Analogues for the Treatment of Triple-Negative Breast Cancer via Mediated Irreversible Covalent Warheads

Ding, Y., Li, D., Ding, C., Wang, P., Liu, Z., Wold, E. A., Ye, N., Chen, H., White, M. A., Shen, Q., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01514 · Cited by 44

Reversible versus Irreversible Inhibition Modes of ERK2: A Comparative Analysis for ERK2 Protein Kinase in Cancer Therapy

Khan, S., Bjij, I., Betz, R. M., & Soliman, M. E. S. (2018) · Future Medicinal Chemistry · doi:10.4155/fmc-2017-0275 · Cited by 44

Target Identification of Bioactive Covalently Acting Natural Products

Nomura, D. K., & Maimone, T. J. (2018) · Current topics in microbiology and immunology · doi:10.1007/82_2018_121 · Cited by 44

The Emerging Therapeutic Potential of Nitro Fatty Acids and Other Michael Acceptor-Containing Drugs for the Treatment of Inflammation and Cancer

Piesche, M., Roos, J., Kuhn, B. R., Fettel, J., Hellmuth, N., Brat, C., Maucher, I. V., Awad, O., Matrone, C., Comerma-Steffensen, S., et al. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.01297 · Cited by 45

Covalently Engineered Protein Minibinders with Enhanced Neutralization Efficacy against Escaping SARS-CoV-2 Variants

Han, Y., Yang, Z., Hu, H., Zhang, H., Chen, L., Li, K., Kong, L., Wang, Q., Liu, B., Wang, M., et al. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.1c11554 · Cited by 44

A Fast Ab Initio Predictor Tool for Covalent Reactivity Estimation of Acrylamides

Palazzesi, F., Grundl, M. A., Pautsch, A., Weber, A., & Tautermann, C. S. (2019) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.9b00316 · Cited by 41

Relative Selectivity of Covalent Inhibitors Requires Assessment of Inactivation Kinetics and Cellular Occupancy: A Case Study of Ibrutinib and Acalabrutinib

Hopper, M. J., Gururaja, T. L., Kinoshita, T., Dean, J. P., Hill, R. J., & Mongan, A. M. (2019) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.119.262063 · Cited by 46

Structure-Based Design of a Dual-Targeted Covalent Inhibitor Against Papain-like and Main Proteases of SARS-CoV-2

Yu, W., Zhao, Y., Ye, H., Wu, N., Liao, Y., Chen, N., Li, Z., Wan, N., Hao, H., Honggao Yan, A., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00954 · Cited by 45

Advanced approaches of developing targeted covalent drugs

Gai, C., Harnor, S. J., Zhang, S., Cano, C., Zhuang, C., & Zhao, Q. (2022) · RSC Medicinal Chemistry · doi:10.1039/d2md00216g · Cited by 44

Applications of Reactive Cysteine Profiling

Backus, K. M. (2018) · Current topics in microbiology and immunology · doi:10.1007/82_2018_120 · Cited by 39

Selective and Effective: Current Progress in Computational Structure-Based Drug Discovery of Targeted Covalent Inhibitors

Bianco, G., Goodsell, D. S., & Forli, S. (2020) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2020.10.005 · Cited by 40

Docking Paradigm in Drug Design

Sulimov, V. B., Kutov, D. C., Taschilova, A. S., Ilin, I. S., Tyrtyshnikov, E. E., & Sulimov, A. V. (2020) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026620666201207095626 · Cited by 43

α-Aminoazoles/azines: key reaction partners for multicomponent reactions

Imtiaz, S., War, J. A., Banoo, S., & Khan, S. (2021) · RSC Advances · doi:10.1039/d1ra00392e · Cited by 41

Recent advances in the development of allosteric protein tyrosine phosphatase inhibitors for drug discovery

Elhassan, R. M., Hou, X., & Fang, H. (2021) · Medicinal Research Reviews · doi:10.1002/med.21871 · Cited by 40

Protein–protein interactions: developing small-molecule inhibitors/stabilizers through covalent strategies

Lucero, B., Francisco, K. R., Liu, L. J., Caffrey, C. R., & Ballatore, C. (2023) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2023.04.007 · Cited by 40

Spirocyclizations Involving Oxonium Ylides Derived from Cyclic α-Diazocarbonyl Compounds: An Entry into 6-Oxa-2-azaspiro[4.5]decane Scaffold

Dar’in, D. V., Kantin, G. P., Bakulina, O., Inyutina, A., Chupakhin, E. G., & Krasavin, M. (2020) · The Journal of Organic Chemistry · doi:10.1021/acs.joc.0c02356 · Cited by 39

A chemical perspective on the modulation of TEAD transcriptional activities: Recent progress, challenges, and opportunities

Lou, J., Lu, Y., Cheng, J., Zhou, F., Yan, Z., Zhang, D., Meng, X., & Zhao, Y. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114684 · Cited by 39

Covalent Proximity Inducers

London, N. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00570 · Cited by 37

Application of Dually Activated Michael Acceptor to the Rational Design of Reversible Covalent Inhibitor for Enterovirus 71 3C Protease

Ma, Y., Li, L., He, S., Shang, C., Sun, Y., Liu, N., Meek, T. D., Wang, Y., & Shang, L. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00387 · Cited by 38

Peptide-β-lactam Inhibitors of Dengue and West Nile Virus NS2B-NS3 Protease Display Two Distinct Binding Modes

Dražić, T., Kopf, S., Corridan, J., Leuthold, M. M., Bertoša, B., & Klein, C. D. P. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00759 · Cited by 38

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 39

Preclinical Characterization of 3β-(N-Acetyl l -cysteine methyl ester)-2aβ,3-dihydrogaliellalactone (GPA512), a Prodrug of a Direct STAT3 Inhibitor for the Treatment of Prostate Cancer

Escobar, Z., Bjartell, A. S., Canesin, G., Axelsson, S. E., Sterner, O., Hellsten, R., & Johansson, M. H. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01814 · Cited by 37

Development of covalent NLRP3 inflammasome inhibitors: Chemistry and biological activity

Bertinaria, M., Gastaldi, S., Marini, E., & Giorgis, M. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.11.013 · Cited by 38

Insights on the synthesis of asymmetric curcumin derivatives and their biological activities

Yen, K. P., Aluwi, M. F. F. M., Rullah, K., & Lam, K. W. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.111704 · Cited by 37

Reactive chemistry for covalent probe and therapeutic development

Grams, R. J., & Hsu, K. (2022) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2021.12.002 · Cited by 38

CovBinderInPDB: A Structure-Based Covalent Binder Database

Guo, X.-K., & Zhang, Y. (2022) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.2c01216 · Cited by 35

Development of a Selection Method for Discovering Irreversible (Covalent) Binders from a DNA-Encoded Library

Zhu, Z., Grady, L. C., Ding, Y., Lind, K. E., Davie, C. P., Phelps, C. B., & Evindar, G. (2018) · SLAS DISCOVERY · doi:10.1177/2472555218808454 · Cited by 36

Natural Product Synthesis through the Lens of Informatics

Woo, S., & Shenvi, R. A. (2021) · Accounts of Chemical Research · doi:10.1021/acs.accounts.0c00791 · Cited by 36

Modeling the Binding and Conformational Energetics of a Targeted Covalent Inhibitor to Bruton’s Tyrosine Kinase

Awoonor‐Williams, E., & Rowley, C. N. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.1c00897 · Cited by 37

Reactivities of the Front Pocket N-Terminal Cap Cysteines in Human Kinases

Liu, R., Zhan, S., Che, Y., & Shen, J. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01186 · Cited by 34

Covalent Inhibition Mechanism of Antidiabetic Drugs—Vildagliptin vs Saxagliptin

Wang, Y., Zhang, F., Diao, H., & Wu, R. (2019) · ACS Catalysis · doi:10.1021/acscatal.8b05051 · Cited by 35

Acceptor-Controlled Transfer Dehydration of Amides to Nitriles

Okabe, H., Naraoka, A., Isogawa, T., Oishi, S., & Naka, H. (2019) · Organic Letters · doi:10.1021/acs.orglett.9b01657 · Cited by 35

Naphthoquinones as Covalent Reversible Inhibitors of Cysteine Proteases—Studies on Inhibition Mechanism and Kinetics

Klein, P., Barthels, F., Johé, P., Wagner, A., Tenzer, S., Distler, U., Le, T. A., Schmid, P., Engel, V., Engels, B., et al. (2020) · Molecules · doi:10.3390/molecules25092064 · Cited by 35

Characterization of a Potent and Orally Bioavailable Lys-Covalent Inhibitor of Apoptosis Protein (IAP) Antagonist

Udompholkul, P., Garza-Granados, A., Alboreggia, G., Baggio, C., McGuire, J. R., Pegan, S. D., & Pellecchia, M. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00467 · Cited by 36

Electrophilic Compounds in the Human Diet and Their Role in the Induction of the Transcription Factor NRF2

Andrés, C. M. C., de la Lastra, J. M. P., Munguira, E. B., Andrés, C., Plou, F. J., & Lebeña, E. P. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25063521 · Cited by 34

A thiazole-derived oridonin analogue exhibits antitumor activity by directly and allosterically inhibiting STAT3

Shen, X., Zhao, L., Chen, P., Gong, Y., Liu, D., Zhang, X., Dai, L., Sun, Q., Lou, J., Jin, Z., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.009801 · Cited by 34

Ensemble Docking Coupled to Linear Interaction Energy Calculations for Identification of Coronavirus Main Protease (3CLpro) Non-Covalent Small-Molecule Inhibitors

Jukič, M., Janežič, D., & Bren, U. (2020) · Molecules · doi:10.3390/molecules25245808 · Cited by 35

Newly Emerging Strategies in Antiviral Drug Discovery: Dedicated to Prof. Dr. Erik De Clercq on Occasion of His 80th Anniversary

Xu, S., Ding, D., Zhang, X., Sun, L., Kang, D., Huang, B., Liu, X., & Zhan, P. (2022) · Molecules · doi:10.3390/molecules27030850 · Cited by 34

Inhibition of Zinc-Dependent Histone Deacetylases with a Chemically Triggered Electrophile

Bošković, Ž., Kemp, M. M., Freedy, A. M., Viswanathan, V. S., Pop, M. S., Fuller, J. H., Martínez, N. M., Figueroa-Lazú, S., Hong, J. A., Lewis, T. A., et al. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00012 · Cited by 34

Target identification of covalently binding drugs by activity-based protein profiling (ABPP)

Pichler, C. M., Krysiak, J. M., & Breinbauer, R. (2016) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2016.03.050 · Cited by 33

Electrophilic Helical Peptides That Bond Covalently, Irreversibly, and Selectively in a Protein–Protein Interaction Site

de Araujo, A. D., Lim, J., Good, A. C., Skerlj, R. T., & Fairlie, D. P. (2016) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.6b00395 · Cited by 34

Allenamide as a bioisostere of acrylamide in the design and synthesis of targeted covalent inhibitors

Chen, D., Guo, D., Yan, Z., & Zhao, Y. (2017) · MedChemComm · doi:10.1039/c7md00571g · Cited by 32

WIDOCK: a reactive docking protocol for virtual screening of covalent inhibitors

Scarpino, A., Petri, L., Knez, D., Imre, T., Ábrányi‐Balogh, P., Ferenczy, G. G., Gobec, S., & Keserű, G. M. (2021) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-020-00371-5 · Cited by 34

Nicotinamide N-Methyltransferase: An Emerging Protagonist in Cancer Macro(r)evolution

Parsons, R. B., & Facey, P. D. (2021) · Biomolecules · doi:10.3390/biom11101418 · Cited by 34

Mechanistic aspects of thiol additions to Michael acceptors: Insights from computations

Roseli, R. B., Keto, A. B., & Krenske, E. H. (2022) · Wiley Interdisciplinary Reviews Computational Molecular Science · doi:10.1002/wcms.1636 · Cited by 32

A Liquid Chromatography/Mass Spectrometry Method for Screening Disulfide Tethering Fragments

Hallenbeck, K. K., Davies, J. L., Merron, C., Ogden, P., Sijbesma, E., Ottmann, C., Renslo, A. R., Wilson, C., & Arkin, M. R. (2017) · SLAS DISCOVERY · doi:10.1177/2472555217732072 · Cited by 32

Stability and Cell Permeability of Sulfonyl Fluorides in the Design of Lys‐Covalent Antagonists of Protein‐Protein Interactions

Gambini, L., Udompholkul, P., Salem, A. F., Baggio, C., & Pellecchia, M. (2020) · ChemMedChem · doi:10.1002/cmdc.202000355 · Cited by 32

Design of SARS-CoV-2 Mpro, PLpro Dual-Target Inhibitors Based on Deep Reinforcement Learning and Virtual Screening

Zhang, L.-C., Zhao, H., Liu, J., He, L., Yu, R., & Kang, C. (2022) · Future Medicinal Chemistry · doi:10.4155/fmc-2021-0269 · Cited by 32

A covalent BTK ternary complex compatible with targeted protein degradation

Schiemer, J. S., Maxwell, A., Horst, R., Liu, S., Uccello, D. P., Borzilleri, K. A., Rajamohan, N., Brown, M. F., & Calabrese, M. F. (2023) · Nature Communications · doi:10.1038/s41467-023-36738-z · Cited by 30

Recent progress in targeting KRAS mutant cancers with covalent G12C-specific inhibitors

Rathod, L. S., Dabhade, P. S., & Mokale, S. N. (2023) · Drug Discovery Today · doi:10.1016/j.drudis.2023.103557 · Cited by 32

Identification of sulphonamide-tethered N -((triazol-4-yl)methyl)isatin derivatives as inhibitors of SARS-CoV-2 main protease

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cBinderDB: a covalent binding agent database

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