Advances in covalent kinase inhibitors

Targeted covalent inactivation of protein kinases by resorcylic acid lactone polyketides

Schirmer, A., Kennedy, J., Murli, S., Reid, R., & Santi, D. V. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600445103 · Cited by 169

Systematic Study of the Glutathione (GSH) Reactivity ofN-Arylacrylamides: 1. Effects of Aryl Substitution

Cee, V. J., Volak, L. P., Chen, Y., Bartberger, M. D., Tegley, C. M., Arvedson, T., McCarter, J. D., Tasker, A. S., & Fotsch, C. H. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01018 · Cited by 167

A study of the reactivity of S(VI)–F containing warheads with nucleophilic amino-acid side chains under physiological conditions

Mukherjee, H., Debreczeni, J., Breed, J., Tentarelli, S., Aquila, B., Dowling, J. E., Whitty, A., & Grimster, N. P. (2017) · Organic & Biomolecular Chemistry · doi:10.1039/c7ob02028g · Cited by 167

The EGFR odyssey – from activation to destruction in space and time

Bakker, J., Spits, M., Neefjes, J., & Berlin, I. (2017) · Journal of Cell Science · doi:10.1242/jcs.209197 · Cited by 160

Role of the JNK Pathway in Human Diseases

Sabapathy, K. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-396456-4.00013-4 · Cited by 159

Comparison of Acalabrutinib, A Selective Bruton Tyrosine Kinase Inhibitor, with Ibrutinib in Chronic Lymphocytic Leukemia Cells

Patel, V. M., Balakrishnan, K., Бибикова, Е., Ayres, M., Keating, M. J., Wierda, W. G., & Gandhi, V. V. (2016) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-16-1446 · Cited by 158

Pharmacologic inhibition of STAT5 in acute myeloid leukemia

Wingelhofer, B., Maurer, B., Heyes, E. C., Cumaraswamy, A. A., Berger‐Becvar, A., de Araujo, E. D., Orlova, A., Freund, P., Ruge, F., Park, J., et al. (2018) · Leukemia · doi:10.1038/s41375-017-0005-9 · Cited by 157

Natural Product Micheliolide (MCL) Irreversibly Activates Pyruvate Kinase M2 and Suppresses Leukemia

Li, J., Li, S., Guo, J., Li, Q., Long, J., Ma, C., Ding, Y., Yan, C., Li, L., Wu, Z., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00241 · Cited by 157

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 156

Matched Molecular Pair Analysis in drug discovery

Dossetter, A. G., Griffen, E., & Leach, A. G. (2013) · Drug Discovery Today · doi:10.1016/j.drudis.2013.03.003 · Cited by 156

Isothiocyanates: mechanism of cancer chemopreventive action

Thornalley, P. J. (2002) · Anti-Cancer Drugs · doi:10.1097/00001813-200204000-00001 · Cited by 152

Kinase selectivity potential for inhibitors targeting the ATP binding site: a network analysis

Danzhi Huang, A., Zhou, T., Lafleur, K., Nevado, C., & Caflisch, A. (2009) · Bioinformatics · doi:10.1093/bioinformatics/btp650 · Cited by 151

Jak family of kinases in cancer

Verma, A., Kambhampati, S., Parmar, S., & Platanias, L. C. (2003) · Cancer and Metastasis Reviews · doi:10.1023/a:1023805715476 · Cited by 149

Takinib, a Selective TAK1 Inhibitor, Broadens the Therapeutic Efficacy of TNF-α Inhibition for Cancer and Autoimmune Disease

Totzke, J., Gurbani, D., Raphemot, R., Hughes, P. F., Bodoor, K., Carlson, D. A., Loiselle, D. R., Bera, A. K., Eibschutz, L. S., Perkins, M. M., et al. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.07.011 · Cited by 146

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 145

Targeting biomolecules with reversible covalent chemistry

Bandyopadhyay, A., & Gao, J. (2016) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2016.08.011 · Cited by 143

The EGF Receptor System as a Target for Antitumor Therapy

Ennis, B. W., Lippman, M. E., & Dickson, R. B. (1991) · Cancer Investigation · doi:10.3109/07357909109018953 · Cited by 143

Clinical experience with CD64-directed immunotherapy. An overview

Curnow, R. T. (1997) · Cancer Immunology, Immunotherapy · doi:10.1007/s002620050435 · Cited by 141

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 140

Covalent inhibitors: an opportunity for rational target selectivity

Lagoutte, R., Patouret, R., & Winssinger, N. (2017) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2017.05.008 · Cited by 138

A new avian erythroblastosis virus, AEV-H, carries erbB gene responsible for the induction of both erythroblastosis and sarcomas

Yamamoto, T. S., Hihara, H., Nishida, T., et al. (1983) · Cell · doi:10.1016/0092-8674(83)90153-8 · Cited by 137

2017 FDA drug approvals

Mullard, A. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.4 · Cited by 137

Bruton tyrosine kinase is commonly overexpressed in mantle cell lymphoma and its attenuation by Ibrutinib induces apoptosis

Cinar, M., Hamedani, F. S., Mo, Z., Cinar, B., Amin, H. M., & Alkan, S. (2013) · Leukemia Research · doi:10.1016/j.leukres.2013.07.028 · Cited by 136

A Structure-Guided Approach to Creating Covalent FGFR Inhibitors

Zhou, W., Hur, W., McDermott, U., Dutt, A., Xian, W., Ficarro, S. B., Zhang, J., Sharma, S. V., Brugge, J. S., Meyerson, M. M., et al. (2010) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.02.007 · Cited by 135

SRPKIN-1: A Covalent SRPK1/2 Inhibitor that Potently Converts VEGF from Pro-angiogenic to Anti-angiogenic Isoform

Hatcher, J. M., Wu, G., Zeng, C., Zhu, J., Fan, M., Patel, S. H., Wang, W., Ficarro, S. B., Leggett, A. L., Powell, C. E., et al. (2018) · Cell chemical biology · doi:10.1016/j.chembiol.2018.01.013 · Cited by 135

Alpha-kinases: analysis of the family and comparison with conventional protein kinases

Drennan, D., & Ryazanov, A. G. (2003) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(03)00060-9 · Cited by 134

Identification and Characterization of an Irreversible Inhibitor of CDK2

Anscombe, E., Meschini, E., Mora-Vidal, R., Martin, M. P., Staunton, D., Geitmann, M., Danielson, U. H., Stanley, W. A., Wang, L.-Z., Reuillon, T. D., et al. (2015) · Chemistry & Biology · doi:10.1016/j.chembiol.2015.07.018 · Cited by 134

Phospholipase C-γ2 Couples Bruton's Tyrosine Kinase to the NF-κB Signaling Pathway in B Lymphocytes

Petro, J. B., & Khan, W. N. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009137200 · Cited by 133

Selective JAK3 Inhibitors with a Covalent Reversible Binding Mode Targeting a New Induced Fit Binding Pocket

Förster, M., Chaikuad, A., Bauer, S. M., Holstein, J., Robers, M. B., Corona, C. R., Gehringer, M., Pfaffenrot, E., Ghoreschi, K., Knapp, S., et al. (2016) · Cell chemical biology · doi:10.1016/j.chembiol.2016.10.008 · Cited by 133

Selectively Targeting the Kinome-Conserved Lysine of PI3Kδ as a General Approach to Covalent Kinase Inhibition

Dalton, S. E., Dittus, L., Thomas, D. A., Convery, M. A., Nunes, J., Bush, J. T., Evans, J. P., Werner, T., Bantscheff, M., Murphy, J. A., et al. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b08979 · Cited by 131

Characterising covalent warhead reactivity

Martin, J. S., Mackenzie, C. J., Fletcher, D., & Gilbert, I. H. (2019) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2019.04.002 · Cited by 129

Ainsliadimer A selectively inhibits IKKα/β by covalently binding a conserved cysteine

Dong, T., Li, C., Wang, X., Dian, L., Zhang, X., Li, L., Chen, S., Cao, R., Li, L., Huang, N., et al. (2015) · Nature Communications · doi:10.1038/ncomms7522 · Cited by 128

Determining Cysteines Available for Covalent Inhibition Across the Human Kinome

Zhao, Z., Liu, Q., Bliven, S. E., Xie, L., & Bourne, P. E. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01815 · Cited by 128

A conceptual framework for predicting the toxicity of reactive chemicals: modeling soft electrophilicity

Schultz, T. W., Carlson, R. E., Cronin, M., Hermens, J. L. M., Johnson, R. D., O'Brien, P. J., Roberts, D. W., Siraki, A. G., Wallace, K. B., & Veith, G. D. (2006) · SAR and QSAR in environmental research · doi:10.1080/10629360600884371 · Cited by 127

Covalent‐Allosteric Kinase Inhibitors

Weisner, J., Gontla, R., Westhuizen, L. V. D., Oeck, S., Ketzer, J., Janning, P., Richters, A., Mühlenberg, T., Fang, Z., Taher, A., et al. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201502142 · Cited by 125

Versatility of the Curcumin Scaffold: Discovery of Potent and Balanced Dual BACE-1 and GSK-3β Inhibitors

Martino, R. M. C. D., Simone, A. D., Andrisano, V., Bisignano, P., Bisi, A., Gobbi, S., Rampa, A., Fato, R., Bergamini, C., Pérez, D. I., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00894 · Cited by 124

DNA-encoded chemical libraries: foundations and applications in lead discovery

Zimmermann, G., & Neri, D. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2016.07.013 · Cited by 124

Development of Selective Covalent Janus Kinase 3 Inhibitors

Tan, L., Akahane, K., McNally, R., Reyskens, K. M. S. E., Ficarro, S. B., Liu, S., Herter-Sprie, G. S., Koyama, S., Pattison, M. J., Labella, K., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00710 · Cited by 122

Inhibition of dipeptidyl-peptidase IV catalyzed peptide truncation by Vildagliptin ((2S)-{[(3-hydroxyadamantan-1-yl)amino]acetyl}-pyrrolidine-2-carbonitrile)

Brandt, I., Joossens, J., Chen, X., Maes, M., Scharpé, S., Meester, I. D., & Lambeir, A. (2005) · Biochemical Pharmacology · doi:10.1016/j.bcp.2005.04.009 · Cited by 118

The Design of Drug Candidate Molecules as Selective Inhibitors of Therapeutically Relevant Protein Kinases

Fischer, P. M. (2004) · Current Medicinal Chemistry · doi:10.2174/0929867043365062 · Cited by 116

The Bmx Tyrosine Kinase Induces Activation of the Stat Signaling Pathway, Which Is Specifically Inhibited by Protein Kinase Cδ

Saharinen, P., Ekman, N., Sarvas, K., Parker, P. J., Alitalo, K. K., & Silvennoinen, O. (1997) · Blood · doi:10.1182/blood.v90.11.4341 · Cited by 115

Phosphatidylinositol‐4 kinase III beta and oxysterol‐binding protein accumulate unesterified cholesterol on poliovirus‐induced membrane structure

Arita, M. (2014) · Microbiology and Immunology · doi:10.1111/1348-0421.12144 · Cited by 115

Role of Bruton′s Tyrosine Kinase in B Cell Development

Maas, A., & Hendriks, R. W. (2001) · Journal of Immunology Research · doi:10.1155/2001/28962 · Cited by 114

6-Ethynylthieno[3,2-d]- and 6-ethynylthieno[2,3-d]pyrimidin-4-anilines as tunable covalent modifiers of ErbB kinases

Wood, E. R., Shewchuk, L. M., Ellis, B., Brignola, P. S., Brashear, R. L., Caferro, T. R., Dickerson, S. H., Dickson, H. D., Donaldson, K. H., Gaul, M. D., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708281105 · Cited by 113

Role of Bruton's tyrosine kinase in immunodeficiency

Tsukada, S., Rawlings, D. J., & Witte, O. N. (1994) · Current Opinion in Immunology · doi:10.1016/0952-7915(94)90151-1 · Cited by 111

Trisubstituted Pyridinylimidazoles as Potent Inhibitors of the Clinically Resistant L858R/T790M/C797S EGFR Mutant: Targeting of Both Hydrophobic Regions and the Phosphate Binding Site

Günther, M., Lategahn, J., Juchum, M., Döring, E., Keul, M., Engel, J., Tumbrink, H. L., Rauh, D., & Laufer, S. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00316 · Cited by 110

Interleukin-2-Inducible T-Cell Kinase (ITK) Deficiency - Clinical and Molecular Aspects

Ghosh, S., Bienemann, K., Boztuǧ, K., & Borkhardt, A. (2014) · Journal of Clinical Immunology · doi:10.1007/s10875-014-0110-8 · Cited by 108

Potential clinical applications of siRNA technique: benefits and limitations

Chen, S., & Zhaori, G. (2010) · European Journal of Clinical Investigation · doi:10.1111/j.1365-2362.2010.02400.x · Cited by 107

Type II Kinase Inhibitors: An Opportunity in Cancer for Rational Design

Blanc, J., Geney, R., & Menet, C. J. (2013) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/1871520611313050008 · Cited by 105

An allosteric kinase inhibitor binds the p21-activated kinase autoregulatory domain covalently

Viaud, J., & Peterson, J. R. (2009) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-09-0102 · Cited by 104

Progress in the Preclinical Discovery and Clinical Development of Class I and Dual Class I/IV Phosphoinositide 3-Kinase (PI3K) Inhibitors

Shuttleworth, S. J., Silva, F. A., Cecil, A., Tomassi, C., Hill, T., Raynaud, F. I., Clarke, P. A., & Workman, P. (2011) · Current Medicinal Chemistry · doi:10.2174/092986711796011229 · Cited by 104

Emerging Roles of the Mitogen and Stress Activated Kinases MSK1 and MSK2

Reyskens, K. M. S. E., & Arthur, J. S. C. (2016) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2016.00056 · Cited by 104

An Acquired HER2 T798I Gatekeeper Mutation Induces Resistance to Neratinib in a Patient with HER2 Mutant–Driven Breast Cancer

Hanker, A. B., Brewer, M. R., Sheehan, J. H., Koch, J. P., Sliwoski, G. R., Nagy, R. J., Lanman, R. B., Berger, M. F., Hyman, D. M., Solit, D. B., et al. (2017) · Cancer Discovery · doi:10.1158/2159-8290.cd-16-1431 · Cited by 104

Discovery of the Irreversible Covalent FGFR Inhibitor 8-(3-(4-Acryloylpiperazin-1-yl)propyl)-6-(2,6-dichloro-3,5-dimethoxyphenyl)-2-(methylamino)pyrido[2,3-d]pyrimidin-7(8H)-one (PRN1371) for the Treatment of Solid Tumors

Brameld, K. A., Owens, T. D., Verner, E. J., Venetsanakos, E., Bradshaw, J. M., Phan, V. T., Tam, D., Leung, K., Shu, J., LaStant, J., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00360 · Cited by 104

Cyclin-Dependent Kinase Inhibitors as Anticancer Therapeutics

Law, M. E., Corsino, P. E., Narayan, S., & Law, B. K. (2015) · Molecular Pharmacology · doi:10.1124/mol.115.099325 · Cited by 103

Type II Inhibitors Targeting CDK2

Alexander, L. T., Möbitz, H., Drueckes, P., Savitsky, P. A., Fedorov, O., Elkins, J. M., Deane, C. M., Cowan‐Jacob, S. W., & Knapp, S. (2015) · ACS Chemical Biology · doi:10.1021/acschembio.5b00398 · Cited by 103

Structure-Guided Design of Highly Selective and Potent Covalent Inhibitors of ERK1/2

Ward, R. A., Colclough, N., Challinor, M., Debreczeni, J. E., Eckersley, K., Fairley, G., Feron, L. J. L., Flemington, V., Graham, M. A., Greenwood, R. D. R., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00466 · Cited by 102

Tricyclic Covalent Inhibitors Selectively Target Jak3 through an Active Site Thiol

Goedken, E. R., Argiriadi, M. A., Banach, D. L., Fiamengo, B. A., Foley, S. E., Frank, K. E., George, J. S., Harris, C. M., Hobson, A. D., Ihle, D. C., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.595181 · Cited by 101

Resistance is futile: overcoming resistance to targeted therapies in lung adenocarcinoma

Neel, D. S., & Bivona, T. G. (2017) · npj Precision Oncology · doi:10.1038/s41698-017-0007-0 · Cited by 98

JAK Kinases in Health and Disease: An Update

Laurence, A. D. J., Pesu, M., Silvennoinen, O., & O’Shea, J. J. (2012) · The Open Rheumatology Journal · doi:10.2174/1874312901206010232 · Cited by 96

Irreversible Nek2 Kinase Inhibitors with Cellular Activity

Henise, J., & Taunton, J. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm200222m · Cited by 96

Osimertinib (AZD9291)—a science-driven, collaborative approach to rapid drug design and development

Yver, A. (2016) · Annals of Oncology · doi:10.1093/annonc/mdw129 · Cited by 96

Discovery of (R,E)-N-(7-Chloro-1-(1-[4-(dimethylamino)but-2-enoyl]azepan-3-yl)-1 H-benzo[d]imidazol-2-yl)-2-methylisonicotinamide (EGF816), a Novel, Potent, and WT Sparing Covalent Inhibitor of Oncogenic (L858R, ex19del) and Resistant (T790M) EGFR Mutants for the Treatment of EGFR Mutant Non-Small-Cell Lung Cancers

Lelais, G., Epple, R., Marsilje, T. H., Long, Y. O., McNeill, M., Chen, B., Lu, W., Anumolu, J., Badiger, S., Bursulaya, B., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01985 · Cited by 95

17-Hydroxy-jolkinolide B Inhibits Signal Transducers and Activators of Transcription 3 Signaling by Covalently Cross-Linking Janus Kinases and Induces Apoptosis of Human Cancer Cells

Wang, Y., Ma, X., Yan, S., Shen, S., Zhu, H., Gu, Y. J., Wang, H., Qin, G., & Yu, Q. (2009) · Cancer Research · doi:10.1158/0008-5472.can-09-0462 · Cited by 95

TAK1 regulates hepatic cell survival and carcinogenesis

Roh, Y. S., Song, J., & Seki, E. (2014) · Journal of Gastroenterology · doi:10.1007/s00535-013-0931-x · Cited by 95

CIMAvax-EGF: A New Therapeutic Vaccine for Advanced Non-Small Cell Lung Cancer Patients

Saavedra, D., & Crombet, T. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00269 · Cited by 95

A Chemoproteomic Strategy for Direct and Proteome-Wide Covalent Inhibitor Target-Site Identification

Browne, C. M., Jiang, B., Ficarro, S. B., Doctor, Z. M., Johnson, J. L., Card, J. D., Sivakumaren, S. C., Alexander, W. M., Yaron, T. M., Murphy, C. J., et al. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b07911 · Cited by 94

Identification of Imidazo-Pyrrolopyridines as Novel and Potent JAK1 Inhibitors

Kulagowski, J. J., Blair, W., Bull, R. J., Chang, C. C., Deshmukh, G., Dyke, H. J., Eigenbrot, C. W., Ghilardi, N., Gibbons, P., Harrison, T., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300438j · Cited by 93

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 93

CYP3A Time-Dependent Inhibition Risk Assessment Validated with 400 Reference Drugs

Zimmerlin, A. G., Trunzer, M., & Faller, B. (2011) · Drug Metabolism and Disposition · doi:10.1124/dmd.110.037911 · Cited by 93

Discovery of a Covalent Kinase Inhibitor from a DNA-Encoded Small-Molecule Library × Protein Library Selection

Chan, A. I., McGregor, L. M., Jain, T., & Liu, D. R. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b04880 · Cited by 92

Chemical genetic strategy for targeting protein kinases based on covalent complementarity

Garske, A. L., Peters, U., Cortesi, A. T., Perez, J. L., & Shokat, K. M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1111239108 · Cited by 91

Discovery of a Potent and Isoform-Selective Targeted Covalent Inhibitor of the Lipid Kinase PI3Kα

Nacht, M., Qiao, L., Sheets, M. P., Martin, T. S., Labenski, M., Mazdiyasni, H., Karp, R., Zhu, Z., Chaturvedi, P., Bhavsar, D., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm3008745 · Cited by 90

Development of the First Generation of Disulfide-Based Subtype-Selective and Potent Covalent Pyruvate Dehydrogenase Kinase 1 (PDK1) Inhibitors

Liu, Y., Xie, Z., Zhao, D., Zhu, J., Mao, F., Tang, S., Xu, H., Luo, C., Geng, M., Huang, M., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01245 · Cited by 90

JX06 Selectively Inhibits Pyruvate Dehydrogenase Kinase PDK1 by a Covalent Cysteine Modification

Sun, W., Xie, Z., Liu, Y., Zhao, D., Wu, Z., Zhang, D., Lv, H., Tang, S., Jin, N., Jiang, H., et al. (2015) · Cancer Research · doi:10.1158/0008-5472.can-15-1023 · Cited by 89

Covalent tethering of fragments for covalent probe discovery

Kathman, S. G., & Statsyuk, A. V. (2016) · MedChemComm · doi:10.1039/c5md00518c · Cited by 88

Essential biphasic role for JAK3 catalytic activity in IL-2 receptor signaling

Smith, G. A., Uchida, K., Weiss, A., & Taunton, J. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2056 · Cited by 88

Identification of Ligand–Target Pairs from Combined Libraries of Small Molecules and Unpurified Protein Targets in Cell Lysates

McGregor, L. M., Jain, T., & Liu, D. R. (2014) · Journal of the American Chemical Society · doi:10.1021/ja412934t · Cited by 87

Design, Synthesis, and Biological Evaluation of Novel Conformationally Constrained Inhibitors Targeting Epidermal Growth Factor Receptor Threonine790 → Methionine790 Mutant

Chang, S., Zhang, L., Xu, S., Luo, J., Lu, X., Zhang, Z., Xu, T., Liu, Y., Tu, Z., Xu, Y., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm201591k · Cited by 85

Antisense oligonucleotides targeting the epidermal growth factor receptor inhibit proliferation, induce apoptosis, and cooperate with cytotoxic drugs in human cancer cell lines

Ciardiello, F., Caputo, R., Troiani, T., et al. (2001) · International Journal of Cancer · doi:10.1002/ijc.1335 · Cited by 84

Targeting group II PAKs in cancer and metastasis

Eswaran, J., Soundararajan, M., & Knapp, S. (2009) · Cancer and Metastasis Reviews · doi:10.1007/s10555-008-9181-4 · Cited by 82

Inhibition of Btk by Btk-specific concentrations of ibrutinib and acalabrutinib delays but does not block platelet aggregation mediated by glycoprotein VI

Nicolson, P. L. R., Hughes, C. E., Watson, S., Nock, S. H., Hardy, A. T., Watson, C. N., Montague, S. J., Clifford, H., Huissoon, A. P., Malcor, J.-D. M., et al. (2018) · Haematologica · doi:10.3324/haematol.2018.193391 · Cited by 81

Switching Reversibility to Irreversibility in Glycogen Synthase Kinase 3 Inhibitors: Clues for Specific Design of New Compounds

Pérez, D. I., Palomo, V., Pérez, C., Gil, C., Dans, P. D., Luque, F. J., Conde, S., & Martínez, A. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm1016279 · Cited by 80

Small Molecule JNK (c-Jun N-Terminal Kinase) Inhibitors

Siddiqui, M. A., & Reddy, P. A. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm9003279 · Cited by 77

Reversible Covalent Inhibition of a Protein Target

Lee, C., & Grossmann, T. N. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201203341 · Cited by 77

Discovery of a Potent, Covalent BTK Inhibitor for B-Cell Lymphoma

Wu, H., Wang, W., Liu, F., Weisberg, E., Tian, B., Chen, Y., Li, B., Wang, A., Wang, B., Zhao, Z., et al. (2014) · ACS Chemical Biology · doi:10.1021/cb4008524 · Cited by 77

Rational Tuning of Fluorobenzene Probes for Cysteine‐Selective Protein Modification

Embaby, A. M., Schoffelen, S., Kofoed, C., Meldal, M., & Diness, F. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201712589 · Cited by 77

Dual irreversible kinase inhibitors: Quinazoline-based inhibitors incorporating two independent reactive centers with each targeting different cysteine residues in the kinase domains of EGFR and VEGFR-2

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