The Design of Covalent Allosteric Drugs

Acquired Resistance of Lung Adenocarcinomas to Gefitinib or Erlotinib Is Associated with a Second Mutation in the EGFR Kinase Domain

Pao, W., Miller, V. A., Politi, K. A., Riely, G. J., Somwar, R., Zakowski, M. F., Kris, M. G., & Varmus, H. (2005) · PLoS Medicine · doi:10.1371/journal.pmed.0020073 · Cited by 3,527

Targeting cancer with small molecule kinase inhibitors

Zhang, J., Yang, P. L., & Gray, N. S. (2008) · Nature reviews. Cancer · doi:10.1038/nrc2559 · Cited by 2,648

K-Ras(G12C) inhibitors allosterically control GTP affinity and effector interactions

Ostrem, J. M., Peters, U., Sos, M. L., Wells, J. A., & Shokat, K. M. (2013) · Nature · doi:10.1038/nature12796 · Cited by 2,557

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 role of dynamic conformational ensembles in biomolecular recognition

Boehr, D. D., Nussinov, R., & Wright, P. E. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.232 · Cited by 2,008

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

An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor

Zhang, X., Gureasko, J., Shen, K., Cole, P. A., & Kuriyan, J. (2006) · Cell · doi:10.1016/j.cell.2006.05.013 · Cited by 1,650

COT drives resistance to RAF inhibition through MAP kinase pathway reactivation

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Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex

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

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Allosteric modulators of GPCRs: a novel approach for the treatment of CNS disorders

Jeffrey Conn, P., Christopoulos, A., & Lindsley, C. W. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2760 · Cited by 1,063

Timing of new black box warnings and withdrawals for prescription medications

Lasser, K. E. (2002) · JAMA · doi:10.1001/jama.287.17.2215 · Cited by 1,005

Oxidant stress, mitochondria, and cell death mechanisms in drug-induced liver injury: Lessons learned from acetaminophen hepatotoxicity

Jaeschke, H., McGill, M. R., & Ramachandran, A. (2012) · Drug Metabolism Reviews · doi:10.3109/03602532.2011.602688 · Cited by 972

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

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Is allostery an intrinsic property of all dynamic proteins?

Gunasekaran, K., Ma, B., & Nussinov, R. (2004) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20232 · Cited by 896

Target Binding Properties and Cellular Activity of Afatinib (BIBW 2992), an Irreversible ErbB Family Blocker

Solca, F., Dahl, G., Zoephel, A., Bader, G., Sanderson, M., Klein, C., Kraemer, O., Himmelsbach, F., Haaksma, E., & Adolf, G. R. (2012) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.112.197756 · Cited by 865

The Behavior and Significance of Slow‐Binding Enzyme Inhibitors

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Inhibition of p38 MAP kinase by utilizing a novel allosteric binding site

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Induced fit, conformational selection and independent dynamic segments: an extended view of binding events

Csermely, P., Palotai, R., & Nussinov, R. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.04.009 · Cited by 821

The emerging complexity of protein ubiquitination

Komander, D. (2009) · Biochemical Society Transactions · doi:10.1042/bst0370937 · Cited by 821

Evolutionarily conserved networks of residues mediate allosteric communication in proteins

Süel, G. M., Lockless, S. W., Wall, M. A., & Ranganathan, R. (2002) · Nature Structural Biology · doi:10.1038/nsb881 · Cited by 816

Allostery in Disease and in Drug Discovery

Nussinov, R., & Tsai, C. (2013) · Cell · doi:10.1016/j.cell.2013.03.034 · Cited by 769

Structural Alert/Reactive Metabolite Concept as Applied in Medicinal Chemistry to Mitigate the Risk of Idiosyncratic Drug Toxicity: A Perspective Based on the Critical Examination of Trends in the Top 200 Drugs Marketed in the United States

Stepan, A. F., Walker, D. P., Bauman, J. N., Price, D. A., Baillie, T. A., Kalgutkar, A. S. S., & Aleo, M. D. (2011) · Chemical Research in Toxicology · doi:10.1021/tx200168d · Cited by 725

Structure and regulation of Src family kinases

Boggon, T. J., & Eck, M. J. (2004) · Oncogene · doi:10.1038/sj.onc.1208081 · Cited by 712

Allostery and cooperativity revisited

Cui, Q., & Karplus, M. (2008) · Protein Science · doi:10.1110/ps.03259908 · Cited by 684

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 670

Folding funnels, binding funnels, and protein function

Tsai, C., Kumar, S., Ma, B., & Nussinov, R. (1999) · Protein Science · doi:10.1110/ps.8.6.1181 · Cited by 648

Fragment-Based Drug Discovery

Erlanson, D. A., McDowell, R. S., & O'Brien, T. (2004) · Journal of Medicinal Chemistry · doi:10.1021/jm040031v · Cited by 645

Structural Basis of Aurora-A Activation by TPX2 at the Mitotic Spindle

Bayliss, R. W., Sardón, T., Vernos, I., & Conti, E. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00392-7 · Cited by 644

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

Walter, A. O., Sjin, R. T. T., Haringsma, H. J., Ohashi, K., Sun, J., Lee, K., Dubrovskiy, A., Labenski, M., Zhu, Z., Wang, Z., et al. (2013) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0314 · Cited by 620

Protein–protein interactions: Structurally conserved residues distinguish between binding sites and exposed protein surfaces

Ma, B., Elkayam, T., Wolfson, H., & Nussinov, R. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1030237100 · Cited by 595

Two-State Allosteric Behavior in a Single-Domain Signaling Protein

Volkman, B. F., Lipson, D., Wemmer, D. E., & Kern, D. (2001) · Science · doi:10.1126/science.291.5512.2429 · Cited by 594

Folding funnels and binding mechanisms

Ma, B., Kumar, S., Tsai, C.-J., & Nussinov, R. (1999) · Protein Engineering, Design and Selection · doi:10.1093/protein/12.9.713 · Cited by 594

Seven Transmembrane Receptors as Shapeshifting Proteins: The Impact of Allosteric Modulation and Functional Selectivity on New Drug Discovery

Kenakin, T., & Miller, L. J. (2010) · Pharmacological Reviews · doi:10.1124/pr.108.000992 · Cited by 584

Inhibition of drug-resistant mutants of ABL, KIT, and EGF receptor kinases

Carter, T. A., Wodicka, L. M., Shah, N. P., Velasco, A. M., Fabian, M. A., Treiber, D. K., Milanov, Z. V., Atteridge, C. E., Biggs, W., Edeen, P. T., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504952102 · Cited by 555

Reversible targeting of noncatalytic cysteines with chemically tuned electrophiles

Serafimova, I. M., Pufall, M. A., Krishnan, S., Duda, K., Cohen, M. S., Maglathlin, R. L., McFarland, J. M., Miller, R. M., Frödin, M., & Taunton, J. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.925 · Cited by 505

The two-state model of receptor activation

Leff, P. (1995) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(00)88989-0 · Cited by 492

Predicting Protein Ligand Binding Sites by Combining Evolutionary Sequence Conservation and 3D Structure

Capra, J. A., Laskowski, R. A., Thornton, J. M., Singh, M., & Funkhouser, T. A. (2009) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000585 · Cited by 469

Managing the challenge of chemically reactive metabolites in drug development

Park, B. K., Boobis, A. R., Clarke, S. E., Goldring, C. E., Jones, D., Kenna, J. G., Lambert, C., Laverty, H., Naisbitt, D. J., Nelson, S. D., et al. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3408 · Cited by 466

Mechanism of inhibition of HIV-1 reverse transcriptase by non-nucleoside inhibitors

Esnouf, R. M., Ren, J., Ross, C., Jones, E. Y., STAMMERS, D. K., & Stuart, D. I. (1995) · Nature Structural & Molecular Biology · doi:10.1038/nsb0495-303 · Cited by 442

Multiple diverse ligands binding at a single protein site: A matter of pre‐existing populations

Ma, B., Shatsky, M., Wolfson, H. J., & Nussinov, R. (2002) · Protein Science · doi:10.1110/ps.21302 · Cited by 420

Mechanism of selective inhibition of the inducible isoform of prostaglandin G/H synthase.

Copeland, R. A., Williams, J. M., Giannaras, J. V., Nurnberg, S., Covington, M., Pinto, D. J. P., Pick, S., & Trzaskos, J. M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.23.11202 · Cited by 409

A Unified View of “How Allostery Works”

Tsai, C.-J., & Nussinov, R. (2014) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003394 · Cited by 401

Relationship between daily dose of oral medications and idiosyncratic drug-induced liver injury: Search for signals

Lammert, C. S., Einarsson, S., Saha, C., Niklasson, A., Bjornsson, E. S., & Chalasani, N. (2008) · Hepatology · doi:10.1002/hep.22272 · Cited by 396

Tethering: Fragment-Based Drug Discovery

Erlanson, D. A., Wells, J. A., & Braisted, A. C. (2004) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.33.110502.140409 · Cited by 385

The structure of unliganded reverse transcriptase from the human immunodeficiency virus type 1.

Rodgers, D. W., Gamblin, S. J., Harris, B. A., Ray, S. S., Culp, J. S., Hellmig, B. D., Woolf, D. J., Debouck, C. M., & Harrison, S. C. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.4.1222 · Cited by 378

The application of discovery toxicology and pathology towards the design of safer pharmaceutical lead candidates

Kramer, J. A., Sagartz, J. E., & Morris, D. L. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2378 · Cited by 377

The spatial and temporal organization of ubiquitin networks

Grabbe, C., Husnjak, K., & Đikić, I. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3099 · Cited by 375

The Origin of Allosteric Functional Modulation: Multiple Pre-existing Pathways

del Sol, A., Tsai, C., Ma, B., & Nussinov, R. (2009) · Structure · doi:10.1016/j.str.2009.06.008 · Cited by 367

Discovery of Potent and Selective Covalent Inhibitors of JNK

Zhang, T., Iñesta-Vaquera, F., Niepel, M., Zhang, J., Ficarro, S. B., Machleidt, T., Xie, T., Marto, J. A., Kim, N., Sim, T., et al. (2012) · Chemistry & Biology · doi:10.1016/j.chembiol.2011.11.010 · Cited by 361

BRAF Gene Amplification Can Promote Acquired Resistance to MEK Inhibitors in Cancer Cells Harboring the BRAF V600E Mutation

Corcoran, R. B., Dias-Santagata, D., Bergethon, K., Iafrate, A. J., Settleman, J., & Engelman, J. A. (2010) · Science Signaling · doi:10.1126/scisignal.2001148 · Cited by 350

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

Crystal Structure of Human AKT1 with an Allosteric Inhibitor Reveals a New Mode of Kinase Inhibition

Wu, W., Voegtli, W. C., Sturgis, H. L., Dizon, F. P., Vigers, G. P. A., & Brandhuber, B. J. (2010) · PLoS ONE · doi:10.1371/journal.pone.0012913 · Cited by 337

Searching for new allosteric sites in enzymes

Hardy, J. A., & Wells, J. A. (2004) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2004.10.009 · Cited by 326

Protein allostery, signal transmission and dynamics: a classification scheme of allosteric mechanisms

Tsai, C., del Sol, A., & Nussinov, R. (2009) · Molecular BioSystems · doi:10.1039/b819720b · Cited by 324

Quantitative Detection of EGFR Mutations in Circulating Tumor DNA Derived from Lung Adenocarcinomas

Taniguchi, K., Uchida, J., Nishino, K., Kumagai, T., Okuyama, T., Okami, J., Higashiyama, M., Kodama, K., Imamura, F., & Kato, K. (2011) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-11-1712 · Cited by 315

Drugs for Allosteric Sites on Receptors

Wenthur, C. J., Gentry, P. R., Mathews, T. P., & Lindsley, C. W. (2011) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010611-134525 · Cited by 285

Covalent EGFR inhibitor analysis reveals importance of reversible interactions to potency and mechanisms of drug resistance

Schwartz, P. A., Kuzmic, P., Solowiej, J., Bergqvist, S., Bolanos, B., Almaden, C., Nagata, A., Ryan, K., Feng, J., Dalvie, D., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1313733111 · Cited by 281

Evidence for Irreversible Inhibition of Glycogen Synthase Kinase-3β by Tideglusib

Domı́nguez, J. M., Fuertes, A., Orozco, L., del Monte-Millán, M., Delgado, E., & Medina, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.306472 · Cited by 249

Mechanistic Basis of Enzyme-Targeted Drugs

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

Posttranslational Protein Modifications

Krueger, K. E., & Srivastava, S. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r600009-mcp200 · Cited by 217

Can In Vitro Metabolism-Dependent Covalent Binding Data in Liver Microsomes Distinguish Hepatotoxic from Nonhepatotoxic Drugs? An Analysis of 18 Drugs with Consideration of Intrinsic Clearance and Daily Dose

Obach, R. S., Kalgutkar, A. S. S., Soglia, J. R., & Zhao, S. X. (2008) · Chemical Research in Toxicology · doi:10.1021/tx800161s · Cited by 215

Allosteric post-translational modification codes

Nussinov, R., Tsai, C.-J., Xin, F., & Radivojac, P. (2012) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2012.07.001 · Cited by 211

The dynamics of drug-target interactions: drug-target residence time and its impact on efficacy and safety

Copeland, R. A. (2010) · Expert Opinion on Drug Discovery · doi:10.1517/17460441003677725 · Cited by 210

Cysteine Mapping in Conformationally Distinct Kinase Nucleotide Binding Sites: Application to the Design of Selective Covalent Inhibitors

Leproult, É., Barluenga, S., Moras, D., Wurtz, J., & Winssinger, N. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm101396q · Cited by 203

Multiple Mitogen-Activated Protein Kinase Signaling Pathways Connect the Cot Oncoprotein to the c- jun Promoter and to Cellular Transformation

Chiariello, M., Marinissen, M. J., & Gutkind, J. S. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.5.1747-1758.2000 · Cited by 198

Strategies for the Selective Regulation of Kinases with Allosteric Modulators: Exploiting Exclusive Structural Features

Fang, Z., Grütter, C., & Rauh, D. (2013) · ACS Chemical Biology · doi:10.1021/cb300663j · Cited by 197

Electrophilic Fragment-Based Design of Reversible Covalent Kinase Inhibitors

Miller, R. M., Paavilainen, V. O., Krishnan, S., Serafimova, I. M., & Taunton, J. (2013) · Journal of the American Chemical Society · doi:10.1021/ja401221b · Cited by 196

HIV-1 reverse transcriptase complex with DNA and nevirapine reveals non-nucleoside inhibition mechanism

Das, K., Martinez, S. E., Bauman, J. D., & Arnold, E. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2223 · Cited by 194

Allostery and population shift in drug discovery

Kar, G., Keskin, Ö., Gürsoy, A., & Nussinov, R. (2010) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2010.09.002 · Cited by 190

Novel Allosteric Sites on Ras for Lead Generation

Grant, B. J., Lukman, S., Hocker, H. J., Sayyah, J., Brown, J. H., McCammon, J. A., & Gorfe, A. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025711 · Cited by 180

High-throughput drug discovery: What can we expect from HTS?

Gribbon, P. M., & Andreas, S. (2005) · Drug Discovery Today · doi:10.1016/s1359-6446(04)03275-1 · Cited by 173

Mechanism-Based Inhibition: Deriving KI and kinact Directly from Time-Dependent IC50 Values

Krippendorff, B., Neuhaus, R., Lienau, P., Reichel, A., & Huisinga, W. (2009) · SLAS DISCOVERY · doi:10.1177/1087057109336751 · Cited by 160

Turning a protein kinase on or off from a single allosteric site via disulfide trapping

Sadowsky, J., Burlingame, M. A., Wolan, D. W., McClendon, C. L., Jacobson, M. P., & Wells, J. A. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1102376108 · Cited by 157

An allosteric inhibitor of substrate recognition by the SCFCdc4 ubiquitin ligase

Orlicky, S. M., Tang, X., Neduva, V., Elowe, N. H., Brown, E. D., Sicheri, F., & Tyers, M. (2010) · Nature Biotechnology · doi:10.1038/nbt.1646 · Cited by 150

The Different Ways through Which Specificity Works in Orthosteric and Allosteric Drugs

Nussinov, R., & Tsai, C. (2012) · Current Pharmaceutical Design · doi:10.2174/138161212799436377 · Cited by 149

Allo-network drugs: harnessing allostery in cellular networks

Nussinov, R., Tsai, C., & Csermely, P. (2011) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2011.08.004 · Cited by 144

‘7TM Receptor Allostery: Putting Numbers to Shapeshifting Proteins

Kenakin, T. (2009) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2009.06.007 · Cited by 129

Allosteric non-bisphosphonate FPPS inhibitors identified by fragment-based discovery

Jahnke, W., Rondeau, J., Cotesta, S., Marzinzik, A. L., Pellé, X., Geiser, M., Strauss, A., Götte, M., Bitsch, F., Hemmig, R., et al. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.421 · Cited by 129

Inhibition of the Hepatitis C Virus NS3/4A Protease

Marco, S. D., Rizzi, M., Volpari, C., Walsh, M. A., Narjes, F., Colarusso, S., Francesco, R. D., Matassa, V. G., & Sollazzo, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.10.7152 · Cited by 127

Direct Observation of the Dynamic Process Underlying Allosteric Signal Transmission

Brüschweiler, S., Schanda, P., Kloiber, K., Brutscher, B., Kontaxis, G., Konrat, R., & Tollinger, M. (2009) · Journal of the American Chemical Society · doi:10.1021/ja809947w · Cited by 124

Propagating conformational changes over long (and short) distances in proteins

Yu, E. W., & Koshland, D. E. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.161239298 · Cited by 124

Unraveling structural mechanisms of allosteric drug action

Nussinov, R., & Tsai, C.-J. (2014) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2014.03.006 · Cited by 119

Selective Targeting of Distinct Active Site Nucleophiles by Irreversible Src-Family Kinase Inhibitors

Gushwa, N. N., Kang, S., Chen, J., & Taunton, J. (2012) · Journal of the American Chemical Society · doi:10.1021/ja310659j · Cited by 101

Allosteric effects in the marginally stable von Hippel–Lindau tumor suppressor protein and allostery-based rescue mutant design

Liu, J., & Nussinov, R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707401105 · Cited by 95

Selective irreversible inhibition of a protease by targeting a noncatalytic cysteine

Hagel, M., Niu, D., St Martin, T., Sheets, M. P., Qiao, L., Bernard, H., Karp, R. M., Zhu, Z., Labenski, M. T., Chaturvedi, P., et al. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.492 · Cited by 95

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

Lining the pockets of kinases and phosphatases

Gold, M. G., Barford, D., & Komander, D. (2006) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2006.10.006 · Cited by 85

Disulfide trapping to localize small-molecule agonists and antagonists for a G protein-coupled receptor

Buck, E. A., & Wells, J. A. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500016102 · Cited by 73

Discovery of a Novel Chemical Class of mGlu 5 Allosteric Ligands with Distinct Modes of Pharmacology

Hammond, A. S., Rodriguez, A. L., Townsend, S. D., Niswender, C. M., Gregory, K. J., Lindsley, C. W., & Conn, P. J. (2010) · ACS Chemical Neuroscience · doi:10.1021/cn100051m · Cited by 72

Acylating drugs: redesigning natural covalent inhibitors

Kluge, A. F., & Petter, R. C. (2010) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2010.03.035 · Cited by 71

The Mechanism of Ubiquitination in the Cullin-RING E3 Ligase Machinery: Conformational Control of Substrate Orientation

Liu, J., & Nussinov, R. (2009) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000527 · Cited by 55

Diverse Heterocyclic Scaffolds as Allosteric Inhibitors of AKT

Kettle, J. G., Brown, S. J., Crafter, C., Davies, B. R., Dudley, P., Fairley, G., Faulder, P., Fillery, S. M., Greenwood, H., Hawkins, J. L., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm201394e · Cited by 53

NMR reveals novel mechanisms of protein activity regulation

Kalodimos, C. G. (2011) · Protein Science · doi:10.1002/pro.614 · Cited by 48

Irreversible Inhibitors of c-Src Kinase That Target a Nonconserved Cysteine

Kwarcinski, F. E., Fox, C. C., Steffey, M. E., & Soellner, M. B. (2012) · ACS Chemical Biology · doi:10.1021/cb300337u · Cited by 46

The Role of Irreversible EGFR Inhibitors in the Treatment of Non-Small Cell Lung Cancer: Overcoming Resistance to Reversible EGFR Inhibitors

Belani, C. P. (2010) · Cancer Investigation · doi:10.3109/07357901003631072 · Cited by 41

Analytical pharmacology: the impact of numbers on pharmacology

Kenakin, T., & Christopoulos, A. (2011) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2011.01.002 · Cited by 39

Filling and mining the reactive metabolite target protein database

Hanzlik, R. P., Fang, J., & Koen, Y. M. (2008) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2008.08.016 · Cited by 37

Orthosteric- and allosteric-induced ligand-directed trafficking at GPCRs.

Digby, G. J., Conn, P. J., & Lindsley, C. W. (2010) · PubMed · Cited by 36

Assay Principle for Modulators of Protein−Protein Interactions and Its Application to Non-ATP-Competitive Ligands Targeting Protein Kinase A

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Superiority of a novel EGFR targeted covalent inhibitor over its reversible counterpart in overcoming drug resistance

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