Advances in covalent kinase inhibitors

Understanding the Warburg Effect: The Metabolic Requirements of Cell Proliferation

Vander Heiden, M. G., Cantley, L. C., & Thompson, C. B. (2009) · Science · doi:10.1126/science.1160809 · Cited by 16,197

Cancer drug resistance: an evolving paradigm

Holohan, C., Van Schaeybroeck, S., Longley, D. B., & Johnston, P. G. (2013) · Nature Reviews Cancer · doi:10.1038/nrc3599 · Cited by 4,681

New Substructure Filters for Removal of Pan Assay Interference Compounds (PAINS) from Screening Libraries and for Their Exclusion in Bioassays

Baell, J. B., & Holloway, G. A. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm901137j · Cited by 3,944

Osimertinib or Platinum–Pemetrexed in EGFR T790M–Positive Lung Cancer

Mok, T. S., Wu, Y.-L., Ahn, M.-J., Garassino, M. C., Kim, H. R., Ramalingam, S. S., Shepherd, F. A., He, Y., Akamatsu, H., Theelen, W. S. M. E., et al. (2017) · New England Journal of Medicine · doi:10.1056/nejmoa1612674 · Cited by 3,379

Epidermal growth factor receptor mutations in lung cancer

Sharma, S. V., Bell, D. W., Settleman, J., & Haber, D. A. (2007) · Nature Reviews Cancer · doi:10.1038/nrc2088 · Cited by 3,170

A STUDY OF THE ADRENOTROPIC RECEPTORS

Ahlquist, R. P. (1948) · American Journal of Physiology-Legacy Content · doi:10.1152/ajplegacy.1948.153.3.586 · Cited by 2,893

Principles of early drug discovery

Hughes, J., Rees, S., Kalindjian, S., & Philpott, K. (2011) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2010.01127.x · Cited by 2,859

The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth

Christofk, H. R., Vander Heiden, M. G., Harris, M. H., Ramanathan, A., Gerszten, R. E., Wei, R., Fleming, M. D., Schreiber, S. L., & Cantley, L. C. (2008) · Nature · doi:10.1038/nature06734 · Cited by 2,820

The PI3K Pathway in Human Disease

Fruman, D. A., Chiu, H., Hopkins, B. D., Bagrodia, S., Cantley, L. C., & Abraham, R. T. (2017) · Cell · doi:10.1016/j.cell.2017.07.029 · Cited by 2,749

The Spliceosome: Design Principles of a Dynamic RNP Machine

Wahl, M. C., Will, C. L., & Lührmann, R. (2009) · Cell · doi:10.1016/j.cell.2009.02.009 · Cited by 2,665

Targeting cancer with small molecule kinase inhibitors

Zhang, J., Yang, P. L., & Gray, N. S. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2559 · Cited by 2,576

Clinical development success rates for investigational drugs

Hay, M., Thomas, D. W., Craighead, J. L., Economides, C., & Rosenthal, J. (2014) · Nature Biotechnology · doi:10.1038/nbt.2786 · Cited by 2,536

Targeting PI3K signalling in cancer: opportunities, challenges and limitations

Engelman, J. A. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2664 · Cited by 2,445

Transforming gene product of Rous sarcoma virus phosphorylates tyrosine

Hunter, T., & Sefton, B. M. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.3.1311 · Cited by 2,332

Targeting BTK with Ibrutinib in Relapsed Chronic Lymphocytic Leukemia

Byrd, J. C., Furman, R. R., Coutre, S. E., Flinn, I. W., Burger, J. A., Blum, K. A., Grant, B., Sharman, J. P., Coleman, M., Wierda, W. G., et al. (2013) · New England Journal of Medicine · doi:10.1056/nejmoa1215637 · Cited by 2,270

AZD9291, an Irreversible EGFR TKI, Overcomes T790M-Mediated Resistance to EGFR Inhibitors in Lung Cancer

Cross, D. A. E., Ashton, S. E., Ghiorghiu, S., Eberlein, C., Nebhan, C. A., Spitzler, P. J., Orme, J. P., Finlay, M. R. V., Ward, R. A., Mellor, M. J., et al. (2014) · Cancer Discovery · doi:10.1158/2159-8290.cd-14-0337 · Cited by 2,246

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 Fibroblast Growth Factor signaling pathway

Ornitz, D. M., & Itoh, N. (2015) · WIREs Developmental Biology · doi:10.1002/wdev.176 · Cited by 2,050

Epidermal growth factor receptor (EGFR) signaling in cancer

Normanno, N., De Luca, A., Bianco, C., Strizzi, L., Mancino, M., Maiello, M. R., Carotenuto, A., De Feo, G., Caponigro, F., & Salomon, D. S. (2006) · Gene · doi:10.1016/j.gene.2005.10.018 · Cited by 2,038

A Randomized Trial of Low-Dose Aspirin in the Primary Prevention of Cardiovascular Disease in Women

Ridker, P. M., Cook, N. R., Lee, I.-M., Gordon, D., Gaziano, J. M., Manson, J. E., Hennekens, C. H., & Buring, J. E. (2005) · New England Journal of Medicine · doi:10.1056/nejmoa050613 · Cited by 1,945

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

Quantitative reactivity profiling predicts functional cysteines in proteomes

Weerapana, E., Wang, C., Simon, G. M., Richter, F., Khare, S., Dillon, M. B. D., Bachovchin, D. A., Mowen, K., Baker, D., & Cravatt, B. F. (2010) · Nature · doi:10.1038/nature09472 · Cited by 1,684

Aspirin Use and Reduced Risk of Fatal Colon Cancer

Thun, M. J., Namboodiri, M. M., & Heath, C. W. (1991) · New England Journal of Medicine · doi:10.1056/nejm199112053252301 · Cited by 1,673

Electrophilicity Index

Chattaraj, P. K., Sarkar, U., & Roy, D. R. (2006) · Chemical Reviews · doi:10.1021/cr040109f · Cited by 1,670

ERK1/2 MAP kinases: Structure, function, and regulation

Roskoski, R. (2012) · Pharmacological Research · doi:10.1016/j.phrs.2012.04.005 · Cited by 1,650

Ibrutinib versus Ofatumumab in Previously Treated Chronic Lymphoid Leukemia

Byrd, J. C., Brown, J. R., O'Brien, S., Barrientos, J. C., Kay, N. E., Reddy, N. M., Coutre, S., Tam, C. S., Mulligan, S. P., Jaeger, U., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1400376 · Cited by 1,639

Multiple BCR-ABL kinase domain mutations confer polyclonal resistance to the tyrosine kinase inhibitor imatinib (STI571) in chronic phase and blast crisis chronic myeloid leukemia

Shah, N. P., Nicoll, J. M., Nagar, B., Gorre, M. E., Paquette, R. L., Kuriyan, J., & Sawyers, C. L. (2002) · Cancer Cell · doi:10.1016/s1535-6108(02)00096-x · Cited by 1,612

Estimation of clinical trial success rates and related parameters

Wong, C. H., Siah, K. W., & Lo, A. W. (2019) · Biostatistics · doi:10.1093/biostatistics/kxx069 · Cited by 1,585

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

Medicinal chemical properties of successful central nervous system drugs

Pajouhesh, H., & Lenz, G. R. (2005) · NeuroRX · doi:10.1602/neurorx.2.4.541 · Cited by 1,535

Emerging functions of the EGFR in cancer

Sigismund, S., Avanzato, D., & Lanzetti, L. (2018) · Molecular Oncology · doi:10.1002/1878-0261.12155 · Cited by 1,469

BIBW2992, an irreversible EGFR/HER2 inhibitor highly effective in preclinical lung cancer models

Li, D., Ambrogio, L., Shimamura, T., Kubo, S., Takahashi, M., Chirieac, L. R., Padera, R. F., Shapiro, G. I., Baum, A., Himmelsbach, F., et al. (2008) · Oncogene · doi:10.1038/onc.2008.109 · Cited by 1,447

Review of epidermal growth factor receptor biology

Herbst, R. S. (2004) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/j.ijrobp.2003.11.041 · Cited by 1,390

Glivec (STI571, imatinib), a rationally developed, targeted anticancer drug

Capdeville, R., Buchdunger, E., Zimmermann, J., & Matter, A. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd839 · Cited by 1,389

Current Protocols in Molecular Biology

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Selective Modification of Glutathione Metabolism

Meister, A. (1983) · Science · doi:10.1126/science.6836290 · Cited by 1,267

CAST: randomised placebo-controlled trial of early aspirin use in 20 000 patients with acute ischaemic stroke

Chen, Z.-M. (1997) · The Lancet · doi:10.1016/s0140-6736(97)04010-5 · Cited by 1,232

The mechanism of action of aspirin

Vane, J. R., & Botting, R. M. (2003) · Thrombosis Research · doi:10.1016/s0049-3848(03)00379-7 · Cited by 1,225

Mechanisms and consequences of Jak–STAT signaling in the immune system

Villarino, A. V., Kanno, Y., & O'Shea, J. J. (2017) · Nature Immunology · doi:10.1038/ni.3691 · Cited by 1,221

Dacomitinib versus gefitinib as first-line treatment for patients with EGFR-mutation-positive non-small-cell lung cancer (ARCHER 1050): a randomised, open-label, phase 3 trial

Wu, Y.-L., Cheng, Y., Zhou, X., Lee, K. H., Nakagawa, K., Niho, S., Tsuji, F., Linke, R., Rosell, R., Corral, J., et al. (2017) · The Lancet Oncology · doi:10.1016/s1470-2045(17)30608-3 · Cited by 1,216

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) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/s0022-3565(25)29664-1 · Cited by 1,204

Protein Kinase Inhibitors: Insights into Drug Design from Structure

Noble, M. E. M., Endicott, J. A., & Johnson, L. N. (2004) · Science · doi:10.1126/science.1095920 · Cited by 1,198

Afatinib versus gefitinib as first-line treatment of patients with EGFR mutation-positive non-small-cell lung cancer (LUX-Lung 7): a phase 2B, open-label, randomised controlled trial

Park, K., Tan, E.-H., O'Byrne, K., Zhang, L., Boyer, M., Mok, T., Hirsh, V., Yang, J. C.-H., Lee, K. H., Lu, S., et al. (2016) · The Lancet Oncology · doi:10.1016/s1470-2045(16)30033-x · Cited by 1,183

Mechanisms and functions of eph and ephrin signalling

Kullander, K., & Klein, R. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm856 · Cited by 1,156

The origins of protein phosphorylation

Cohen, P. (2002) · Nature Cell Biology · doi:10.1038/ncb0502-e127 · Cited by 1,139

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

Advances in Chemical Protein Modification

Boutureira, O., & Bernardes, G. J. L. (2015) · Chemical Reviews · doi:10.1021/cr500399p · Cited by 1,132

Bruton Tyrosine Kinase Inhibitor Ibrutinib (PCI-32765) Has Significant Activity in Patients With Relapsed/Refractory B-Cell Malignancies

Advani, R. H., Buggy, J. J., Sharman, J. P., Smith, S. M., Boyd, T. E., Grant, B., Kolibaba, K. S., Furman, R. R., Rodriguez, S., Chang, B. Y., et al. (2013) · Journal of Clinical Oncology · doi:10.1200/jco.2012.42.7906 · Cited by 1,128

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

Inhibition of the Abl protein-tyrosine kinase in vitro and in vivo by a 2-phenylaminopyrimidine derivative.

Buchdunger, E., Zimmermann, J., Mett, H., Meyer, T., Müller, M., Druker, B. J., & Lydon, N. (1996) · PubMed · Cited by 1,057

Defective lymphoid development in mice lacking expression of the common cytokine receptor γ chain

Cao, X., Shores, E. W., Hu-Li, J., Anver, M. R., Kelsail, B. L., Russell, S. M., Drago, J., Noguchi, M., Grinberg, A., Bloom, E. T., et al. (1995) · Immunity · doi:10.1016/1074-7613(95)90047-0 · Cited by 1,038

cGMP-Dependent Protein Kinases and cGMP Phosphodiesterases in Nitric Oxide and cGMP Action

Francis, S. H., Busch, J. L., & Corbin, J. D. (2010) · Pharmacological Reviews · doi:10.1124/pr.110.002907 · Cited by 1,028

Novel mutant-selective EGFR kinase inhibitors against EGFR T790M

Zhou, W., Ercan, D., Chen, L., Yun, C.-H., Li, D., Capelletti, M., Cortot, A. B., Chirieac, L., Iacob, R. E., Padera, R., et al. (2009) · Nature · doi:10.1038/nature08622 · Cited by 1,013

Selective growth stimulating effects of mouse sarcoma on the sensory and sympathetic nervous system of the chick embryo

Levi‐Montalcini, R., & Hamburger, V. (1951) · Journal of Experimental Zoology · doi:10.1002/jez.1401160206 · Cited by 955

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., Lynch, T. J., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502860102 · Cited by 952

Pyridoxal Phosphate Enzymes: Mechanistic, Structural, and Evolutionary Considerations

Eliot, A. C., & Kirsch, J. F. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.074021 · Cited by 950

Proteome-wide covalent ligand discovery in native biological systems

Backus, K. M., Correia, B. E., Lum, K. M., Forli, S., Horning, B. D., González-Páez, G. E., Chatterjee, S., Lanning, B. R., Teijaro, J. R., Olson, A. J., et al. (2016) · Nature · doi:10.1038/nature18002 · Cited by 940

The IKKβ Subunit of IκB Kinase (IKK) is Essential for Nuclear Factor κB Activation and Prevention of Apoptosis

Li, Z.-W., Chu, W., Hu, Y., Delhase, M., Deerinck, T., Ellisman, M., Johnson, R., & Karin, M. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.189.11.1839 · Cited by 926

The Epidermal Growth Factor Receptor Pathway: A Model for Targeted Therapy

Scaltriti, M., & Baselga, J. (2006) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-05-1554 · Cited by 913

Therapeutic strategies for rheumatoid arthritis

Smolen, J. S., & Steiner, G. (2003) · Nature Reviews Drug Discovery · doi:10.1038/nrd1109 · Cited by 911

Acalabrutinib (ACP-196) in Relapsed Chronic Lymphocytic Leukemia

Byrd, J. C., Harrington, B., O’Brien, S., Jones, J. A., Schuh, A., Devereux, S., Chaves, J., Wierda, W. G., Awan, F. T., Brown, J. R., et al. (2016) · New England Journal of Medicine · doi:10.1056/nejmoa1509981 · Cited by 897

Hard and soft acids and bases—The evolution of a chemical concept

Pearson, R. G. (1990) · Coordination Chemistry Reviews · doi:10.1016/0010-8545(90)85016-l · Cited by 886

Targeting transcription regulation in cancer with a covalent CDK7 inhibitor

Kwiatkowski, N., Zhang, T., Rahl, P. B., Abraham, B. J., Reddy, J., Ficarro, S. B., Dastur, A., Amzallag, A., Ramaswamy, S., Tesar, B., et al. (2014) · Nature · doi:10.1038/nature13393 · Cited by 855

Focal adhesion kinase and its signaling pathways in cell migration and angiogenesis

Zhao, X., & Guan, J.-L. (2011) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2010.11.001 · Cited by 835

Pyruvate kinase M2 activators promote tetramer formation and suppress tumorigenesis

Anastasiou, D., Yu, Y., Israelsen, W. J., Jiang, J.-K., Boxer, M. B., Hong, B. S., Tempel, W., Dimov, S., Shen, M., Jha, A., et al. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1060 · Cited by 816

Bruton tyrosine kinase represents a promising therapeutic target for treatment of chronic lymphocytic leukemia and is effectively targeted by PCI-32765

Herman, S. E. M., Gordon, A. L., Hertlein, E., Ramanunni, A., Zhang, X., Jaglowski, S., Flynn, J., Jones, J., Blum, K. A., Buggy, J. J., et al. (2011) · Blood · doi:10.1182/blood-2011-01-328484 · Cited by 807

Mammalian cell-cycle regulation: several Cdks, numerous cyclins and diverse compensatory mechanisms

Satyanarayana, A., & Kaldis, P. (2009) · Oncogene · doi:10.1038/onc.2009.170 · Cited by 774

The protein tyrosine kinase JAK1 complements defects in interferon-α/β and -γ signal transduction

Müller, M., Briscoe, J., Laxton, C., Guschin, D., Ziemiecki, A., Silvennoinen, O., Harpur, A. G., Barbieri, G., Witthuhn, B. A., Schindler, C., et al. (1993) · Nature · doi:10.1038/366129a0 · Cited by 760

Off-target toxicity is a common mechanism of action of cancer drugs undergoing clinical trials

Lin, A., Giuliano, C. J., Palladino, A., John, K. M., Abramowicz, C., Yuan, M. L., Sausville, E. L., Lukow, D. A., Liu, L., Chait, A. R., et al. (2019) · Science Translational Medicine · doi:10.1126/scitranslmed.aaw8412 · Cited by 754

The epidermal growth factor receptor family: Biology driving targeted therapeutics

Wieduwilt, M. J., & Moasser, M. M. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-7440-8 · Cited by 751

Scales of Nucleophilicity and Electrophilicity: A System for Ordering Polar Organic and Organometallic Reactions

Mayr, H., & Patz, M. (1994) · Angewandte Chemie International Edition in English · doi:10.1002/anie.199409381 · Cited by 739

PF00299804, an Irreversible Pan-ERBB Inhibitor, Is Effective in Lung Cancer Models with EGFR and ERBB2 Mutations that Are Resistant to Gefitinib

Engelman, J. A., Zejnullahu, K., Gale, C.-M., Lifshits, E., Gonzales, A. J., Shimamura, T., Zhao, F., Vincent, P. W., Naumov, G. N., Bradner, J. E., et al. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-1885 · Cited by 730

Role of Bruton’s tyrosine kinase in B cells and malignancies

Pal Singh, S., Dammeijer, F., & Hendriks, R. W. (2018) · Molecular Cancer · doi:10.1186/s12943-018-0779-z · Cited by 726

Emerging and Re-Emerging Warheads for Targeted Covalent Inhibitors: Applications in Medicinal Chemistry and Chemical Biology

Gehringer, M., & Laufer, S. A. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01153 · Cited by 714

Structure−Brain Exposure Relationships

Hitchcock, S. A., & Pennington, L. D. (2006) · Journal of Medicinal Chemistry · doi:10.1021/jm060642i · Cited by 698

Discovery of Selective Irreversible Inhibitors for Bruton’s Tyrosine Kinase

Pan, Z., Scheerens, H., Li, S., Schultz, B. E., Sprengeler, P. A., Burrill, L. C., Mendonca, R. V., Sweeney, M. D., Scott, K. C. K., Grothaus, P. G., et al. (2007) · ChemMedChem · doi:10.1002/cmdc.200600221 · Cited by 674

Developing Irreversible Inhibitors of the Protein Kinase Cysteinome

Liu, Q., Sabnis, Y., 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 652

Seven Year Itch: Pan-Assay Interference Compounds (PAINS) in 2017—Utility and Limitations

Baell, J. B., & Nissink, J. W. M. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.7b00903 · Cited by 648

Direct Evidence for the Presence of Histidine in the Active Center of Chymotrypsin*

Schoellmann, G., & Shaw, E. (1963) · Biochemistry · doi:10.1021/bi00902a008 · Cited by 643

Antitumor Activity of HKI-272, an Orally Active, Irreversible Inhibitor of the HER-2 Tyrosine Kinase

Rabindran, S. K., Discafani, C. M., Rosfjord, E. C., Baxter, M., Floyd, M. B., Golas, J., Hallett, W. A., Johnson, B. D., Nilakantan, R., Overbeek, E., et al. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-2868 · Cited by 639

The role of JAK/STAT signalling in the pathogenesis, prognosis and treatment of solid tumours

Thomas, S. J., Snowden, J. A., Zeidler, M. P., & Danson, S. J. (2015) · British Journal of Cancer · doi:10.1038/bjc.2015.233 · Cited by 637

Discovery of a Mutant-Selective Covalent Inhibitor of EGFR that Overcomes T790M-Mediated Resistance in NSCLC

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On the reaction of cells and of nerve‐endings to certain poisons, chiefly as regards the reaction of striated muscle to nicotine and to curari

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Discovery and Development of Janus Kinase (JAK) Inhibitors for Inflammatory Diseases: Miniperspective

Clark, J. D., Flanagan, M. E., & Telliez, J.-B. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm401490p · Cited by 601

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

Targeted Covalent Inhibitors for Drug Design

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The Vinylogous Aldol Reaction: A Valuable, Yet Understated Carbon−Carbon Bond-Forming Maneuver

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Neratinib after trastuzumab-based adjuvant therapy in patients with HER2-positive breast cancer (ExteNET): a multicentre, randomised, double-blind, placebo-controlled, phase 3 trial

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Sulfonyl fluorides as privileged warheads in chemical biology

Narayanan, A., & Jones, L. H. (2015) · Chemical Science · doi:10.1039/c5sc00408j · Cited by 546

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 544

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

Through the “Gatekeeper Door”: Exploiting the Active Kinase Conformation

Zuccotto, F., Ardini, E., Casale, E., & Angiolini, M. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm901443h · Cited by 518

Bruton’s tyrosine kinase (Btk): function, regulation, and transformation with special emphasis on the PH domain

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Structural Bioinformatics-Based Design of Selective, Irreversible Kinase Inhibitors

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Reversible targeting of noncatalytic cysteines with chemically tuned electrophiles

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Global profiling of lysine reactivity and ligandability in the human proteome

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