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 · see citing works

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 2,586 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

COT drives resistance to RAF inhibition through MAP kinase pathway reactivation

Johannessen, C. M., Boehm, J. S., Kim, S. Y., Thomas, S. R., Wardwell, L., Johnson, L. A., Emery, C. M., Stransky, N., Cogdill, A. P., Barretina, J., et al. (2010) · Nature · doi:10.1038/nature09627 · Cited by 1,460 · see citing works

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 · see citing works

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

Jeffrey, P. D., Russo, A. A., Polyák, K., Gibbs, E., Hurwitz, J., Massagué, J., & Pavletich, N. P. (1995) · Nature · doi:10.1038/376313a0 · Cited by 1,441 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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. M., Lynch, T. J., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502860102 · Cited by 950 · see citing works

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 882 · see citing works

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 · see citing works

The Behavior and Significance of Slow‐Binding Enzyme Inhibitors

Morrison, J. F., & Walsh, C. T. (1988) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470123072.ch5 · Cited by 843 · see citing works

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

Pargellis, C., Tong, L., Churchill, L., Cirillo, P. F., Gilmore, T., Graham, A. G., Grob, P. M., Hickey, E. R., Moss, N., Pav, S., et al. (2002) · Nature Structural Biology · doi:10.1038/nsb770 · Cited by 834 · see citing works

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 · see citing works

The emerging complexity of protein ubiquitination

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

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 · see citing works

Allostery in Disease and in Drug Discovery

Nussinov, R., & Tsai, C. (2013) · Cell · doi:10.1016/j.cell.2013.03.034 · Cited by 758 · see citing works

Structure and regulation of Src family kinases

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

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 711 · see citing works

Allostery and cooperativity revisited

Cui, Q., & Karplus, M. (2008) · Protein Science · doi:10.1110/ps.03259908 · Cited by 672 · see citing works

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 662 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 573 · see citing works

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 550 · see citing works

The two-state model of receptor activation

Leff, P. (1995) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(00)88989-0 · Cited by 500 · see citing works

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 496 · see citing works

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 · see citing works

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 459 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 389 · see citing works

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 · see citing works

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 · see citing works

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 370 · see citing works

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 368 · see citing works

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 365 · see citing works

<i>BRAF</i> 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 · see citing works

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 · see citing works

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 348 · see citing works

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 · see citing works

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 330 · see citing works

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 · see citing works

Quantitative Detection of <i>EGFR</i> 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 · see citing works

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 · see citing works

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 274 · see citing works

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 · see citing works

Mechanistic Basis of Enzyme-Targeted Drugs

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

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 217 · see citing works

Posttranslational Protein Modifications

Krueger, K. E., & Srivastava, S. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.r600009-mcp200 · Cited by 215 · see citing works

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 · see citing works

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 208 · see citing works

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 · see citing works

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 · see citing works

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 196 · see citing works

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 195 · see citing works

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 191 · see citing works

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 · see citing works

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 178 · see citing works

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 · see citing works

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 · see citing works

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 154 · see citing works

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 · see citing works

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 143 · see citing works

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 139 · see citing works

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 · see citing works

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 · see citing works

‘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 126 · see citing works

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 · see citing works

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 123 · see citing works

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 · see citing works

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 97 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 83 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 51 · see citing works

NMR reveals novel mechanisms of protein activity regulation

Kalodimos, C. G. (2011) · Protein Science · doi:10.1002/pro.614 · Cited by 47 · see citing works

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 45 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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

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

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

Saldanha, S. A., Kaler, G. V., Cottam, H. B., Abagyan, R. A., & Taylor, S. S. (2006) · Analytical Chemistry · doi:10.1021/ac061104g · Cited by 28 · see citing works

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

Singh, J., Evans, E. K., Hagel, M., Labinski, M., Dubrovskiy, A., Nacht, M., Petter, R. C., Prasad, A., Sheets, M. P., Martin, T. S., et al. (2012) · MedChemComm · doi:10.1039/c2md20017a · Cited by 27 · see citing works

Winning the Arms Race by Improving Drug Discovery against Mutating Targets

Anderson, A. C. (2011) · ACS Chemical Biology · doi:10.1021/cb200394t · Cited by 16 · see citing works

Mechanism of Inhibition of Fatty Acid Amide Hydrolase by Sulfonamide-Containing Benzothiazoles: Long Residence Time Derived from Increased Kinetic Barrier and Not Exclusively from Thermodynamic Potency

Tian, G., Paschetto, K. A., Gharahdaghi, F., Gordon, E., Wilkins, D. E., Luo, X., & Scott, C. W. (2011) · Biochemistry · doi:10.1021/bi200552p · Cited by 16 · see citing works

High throughput glutathione and Nrf2 assays to assess chemical and biological reactivity of cysteine-reactive compounds

Naven, R. T., Kantesaria, S., Nadanaciva, S., Schroeter, T., & Leach, K. L. (2013) · Toxicology Research · doi:10.1039/c3tx50027f · Cited by 14 · see citing works

Interactive design and synthesis of a novel antibacterial agent

Wolfe, S., Jin, H., Yang, K., Kim, C.-K., & McEachern, E. J. (1994) · Canadian Journal of Chemistry · doi:10.1139/v94-133 · Cited by 12 · see citing works

Targeted Covalent Inhibitors for Drug Design

Baillie, T. A. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201601091 · Cited by 578 · see citing works

Ras Conformational Ensembles, Allostery, and Signaling

Lu, S., Jang, H., Muratcioglu, S., Gursoy, A., Keskin, O., Nussinov, R., & Zhang, J. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00542 · Cited by 355 · see citing works

AlphaFold, Artificial Intelligence (AI), and Allostery

Nussinov, R., Zhang, M., Liu, Y., & Jang, H. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c04346 · Cited by 190 · see citing works

PI3K inhibitors: review and new strategies

Zhang, M., Jang, H., & Nussinov, R. (2020) · Chemical Science · doi:10.1039/d0sc01676d · Cited by 182 · see citing works

Allosteric Methods and Their Applications: Facilitating the Discovery of Allosteric Drugs and the Investigation of Allosteric Mechanisms

Lu, S., Shen, Q., & Zhang, J. (2019) · Accounts of Chemical Research · doi:10.1021/acs.accounts.8b00570 · Cited by 166 · see citing works

Protein contact network topology: a natural language for allostery

Paola, L. D., & Giuliani, A. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2015.03.001 · Cited by 163 · see citing works

Fragment-based covalent ligand discovery

Lu, W., Kostic, M., Zhang, T., Che, J., Patricelli, M. P., Jones, L. H., Chouchani, E. T., & Gray, N. S. (2021) · RSC Chemical Biology · doi:10.1039/d0cb00222d · Cited by 136 · see citing works

Review: Precision medicine and driver mutations: Computational methods, functional assays and conformational principles for interpreting cancer drivers

Nussinov, R., Jang, H., Tsai, C., & Cheng, F. (2019) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1006658 · Cited by 129 · see citing works

Existing and future drugs for the treatment of the dark side of addiction

Koob, G. F., & Mason, B. J. (2016) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010715-103143 · Cited by 121 · see citing works

Discovery of hidden allosteric sites as novel targets for allosteric drug design

Lu, S., Ji, M., Ni, D., & Zhang, J. (2017) · Drug Discovery Today · doi:10.1016/j.drudis.2017.10.001 · Cited by 118 · see citing works

A lysine–cysteine redox switch with an NOS bridge regulates enzyme function

Wensien, M., von Pappenheim, F. R., Funk, L.-M., Kloskowski, P., Curth, U., Diederichsen, U., Uranga, J., Ye, J., Fang, P., Pan, K., et al. (2021) · Nature · doi:10.1038/s41586-021-03513-3 · Cited by 111 · see citing works

Integrated Computational Approaches and Tools for Allosteric Drug Discovery

Amamuddy, O. S., Veldman, W., Manyumwa, C. V., Khairallah, A., Agajanian, S., Odeyemi, O., Verkhivker, G. M., & Bishop, Ö. T. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21030847 · Cited by 105 · see citing works

Emergence of allosteric drug-resistance mutations: new challenges for allosteric drug discovery

Lu, S., Qiu, Y., Ni, D., He, X., Pu, J., & Zhang, J. (2019) · Drug Discovery Today · doi:10.1016/j.drudis.2019.10.006 · Cited by 94 · see citing works

Drug Design Strategies to Avoid Resistance in Direct-Acting Antivirals and Beyond

Matthew, A. N., Leidner, F., Lockbaum, G. J., Henes, M., Zephyr, J., Hou, S., Rao, D. N., Timm, J., Rusere, L. N., Ragland, D. A., et al. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00648 · Cited by 93 · see citing works

Advances in NMR Methods To Map Allosteric Sites: From Models to Translation

Boulton, S., & Melacini, G. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00718 · Cited by 89 · see citing works

Rational design of allosteric modulators: Challenges and successes

Chatzigoulas, A., & Cournia, Z. (2021) · Wiley Interdisciplinary Reviews Computational Molecular Science · doi:10.1002/wcms.1529 · Cited by 87 · see citing works

Proteomic discovery of chemical probes that perturb protein complexes in human cells

Lazear, M. R., Remsberg, J. R., Jaeger, M. G., Rothamel, K. L., Her, H.-L., DeMeester, K. E., Njomen, E., Hogg, S. J., Rahman, J. A., Whitby, L. R., et al. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.03.026 · Cited by 84 · see citing works

The Key Role of Calmodulin in KRAS-Driven Adenocarcinomas

Nussinov, R., Muratcioğlu, S., Tsai, C., Jang, H., Gürsoy, A., & Keskin, Ö. (2015) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-15-0165 · Cited by 77 · see citing works

The Mechanism of ATP-Dependent Allosteric Protection of Akt Kinase Phosphorylation

Lu, S., Deng, R., Jiang, H., Song, H., Li, S., Shen, Q., Huang, W., Nussinov, R., Yu, J., & Zhang, J. (2015) · Structure · doi:10.1016/j.str.2015.06.027 · Cited by 69 · see citing works

Allostery: Allosteric Cancer Drivers and Innovative Allosteric Drugs

Nussinov, R., Zhang, M., Maloney, R., Liu, Y., Tsai, C.-J., & Jang, H. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167569 · Cited by 66 · see citing works

Aryl-fluorosulfate-based Lysine Covalent Pan-Inhibitors of Apoptosis Protein (IAP) Antagonists with Cellular Efficacy

Baggio, C., Udompholkul, P., Gambini, L., Salem, A. F., Jossart, J. N., Perry, J. J. P., & Pellecchia, M. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01108 · Cited by 66 · see citing works

The Role of Conformational Dynamics and Allostery in the Disease Development of Human Ferritin

Kumar, A., Glembo, T. J., & Ozkan, S. B. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.06.060 · Cited by 66 · see citing works

In silico design of low molecular weight protein–protein interaction inhibitors: Overall concept and recent advances

Kuenemann, M. A., Spérandio, O., Labbé, C. M., Lagorce, D., Miteva, M. A., & Villoutreix, B. O. (2015) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2015.02.006 · Cited by 61 · see citing works

Allosteric inhibition of antiapoptotic MCL-1

Lee, S., Wales, T. E., Escudero, S., Cohen, D. T., Luccarelli, J., Gallagher, C. G., Cohen, N. A., Huhn, A. J., Bird, G. H., Engen, J. R., et al. (2016) · Nature Structural &amp; Molecular Biology · doi:10.1038/nsmb.3223 · Cited by 59 · see citing works

Personal Mutanomes Meet Modern Oncology Drug Discovery and Precision Health

Cheng, F., Liang, H., Butte, A. J., Eng, C., & Nussinov, R. (2018) · Pharmacological Reviews · doi:10.1124/pr.118.016253 · Cited by 58 · see citing works

Drug design targeting active posttranslational modification protein isoforms

Meng, F., Liang, Z. T., Zhao, K., & Luo, C. (2020) · Medicinal Research Reviews · doi:10.1002/med.21774 · Cited by 56 · see citing works

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 · see citing works

Approaches to mitigate the risk of serious adverse reactions in covalent drug design

Baillie, T. A. (2020) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2021.1832079 · Cited by 53 · see citing works

Does Ras Activate Raf and PI3K Allosterically?

Nussinov, R., Tsai, C., & Jang, H. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.01231 · Cited by 50 · see citing works

Simultaneous analysis of enzyme structure and activity by kinetic capillary electrophoresis–MS

Mironov, G. G., Clouthier, C. M., Akbar, A., Keillor, J. W., & Berezovski, M. V. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2170 · Cited by 48 · see citing works

Allosteric inhibition explained through conformational ensembles sampling distinct “mixed” states

Byun, J. A., VanSchouwen, B., Akimoto, M., & Melacini, G. (2020) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2020.10.026 · Cited by 48 · see citing works

Emerging pharmacotherapies for alcohol use disorder

Mason, B. J. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.04.032 · Cited by 46 · see citing works

Engineered control of enzyme structural dynamics and function

Boehr, D. D., D’Amico, R. N., & O’Rourke, K. F. (2018) · Protein Science · doi:10.1002/pro.3379 · Cited by 45 · see citing works

Mapping the Free Energy Landscape of PKA Inhibition and Activation: A Double-Conformational Selection Model for the Tandem cAMP-Binding Domains of PKA RIα

Akimoto, M., McNicholl, E. T., Ramkissoon, A., Moleschi, K., Taylor, S. S., & Melacini, G. (2015) · PLoS Biology · doi:10.1371/journal.pbio.1002305 · Cited by 43 · see citing works

Harnessing Reversed Allosteric Communication: A Novel Strategy for Allosteric Drug Discovery

Fan, J., Liu, Y., Kong, R., Ni, D., Yu, Z., Lu, S., & Zhang, J. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01695 · Cited by 41 · see citing works

Zielgerichtete kovalente Inhibitoren für das Wirkstoffdesign

Baillie, T. A. (2016) · Angewandte Chemie · doi:10.1002/ange.201601091 · Cited by 42 · see citing works

Mapping Cannabinoid 1 Receptor Allosteric Site(s): Critical Molecular Determinant and Signaling Profile of GAT100, a Novel, Potent, and Irreversibly Binding Probe

Laprairie, R. B., Kulkarni, A., Kulkarni, P. M., Hurst, D. P., Lynch, D. L., Reggio, P. H., Janero, D. R., Pertwee, R. G., Stevenson, L., Kelly, M. E. M., et al. (2016) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6b00041 · Cited by 39 · see citing works

Bcr-Abl Allosteric Inhibitors: Where We Are and Where We Are Going to

Carofiglio, F., Trisciuzzi, D., Gambacorta, N., Leonetti, F., Stefanachi, A., & Nicolotti, O. (2020) · Molecules · doi:10.3390/molecules25184210 · Cited by 38 · see citing works

Exploring a Non-ATP Pocket for Potential Allosteric Modulation of PI3Kα

Gkeka, P., Papafotika, A., Christoforidis, S., & Cournia, Z. (2014) · The Journal of Physical Chemistry B · doi:10.1021/jp506423e · Cited by 36 · see citing works

Statistical Analysis and Prediction of Covalent Ligand Targeted Cysteine Residues

Zhang, W., Pei, J., & Lai, L. (2017) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.7b00163 · Cited by 34 · see citing works

Autoinhibition can identify rare driver mutations and advise pharmacology

Nussinov, R., Tsai, C., & Jang, H. (2019) · The FASEB Journal · doi:10.1096/fj.201901341r · Cited by 35 · see citing works

Engineering an Allosteric Control of Protein Function

Vishweshwaraiah, Y. L., Chen, J., & Dokholyan, N. V. (2021) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c11640 · Cited by 33 · see citing works

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 34 · see citing works

Identification of the New Covalent Allosteric Binding Site of Fructose-1,6-bisphosphatase with Disulfiram Derivatives toward Glucose Reduction

Huang, Y., Xu, Y., Song, R., Ni, S., Liu, J., Xu, Y., Ren, Y., Rao, L., Wang, Y., Wei, L., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00699 · Cited by 33 · see citing works

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 · see citing works

Pioneer in Molecular Biology: Conformational Ensembles in Molecular Recognition, Allostery, and Cell Function

Nussinov, R. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169044 · Cited by 33 · see citing works

Covalent allosteric modulation: An emerging strategy for GPCRs drug discovery

Bian, Y., Jun, J. J., Cuyler, J., & Xie, X. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112690 · Cited by 31 · see citing works

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 31 · see citing works

Covalent Inhibition of Wild-Type HIV-1 Reverse Transcriptase Using a Fluorosulfate Warhead

Ippolito, J. A., Niu, H., Bertoletti, N., Carter, Z. J., Jin, S., Spasov, K. A., Cisneros, J. A., Valhondo, M., Cutrona, K. J., Anderson, K. S., et al. (2021) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.0c00612 · Cited by 31 · see citing works

K-Ras4B/calmodulin/PI3Kα: A promising new adenocarcinoma-specific drug target?

Nussinov, R., Muratcioğlu, S., Tsai, C., Jang, H., Gürsoy, A., & Keskin, Ö. (2015) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2016.1135131 · Cited by 30 · see citing works

Computational Tools for Allosteric Drug Discovery: Site Identification and Focus Library Design

Huang, W., Nussinov, R., & Zhang, J. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6637-0_23 · Cited by 31 · see citing works

cBinderDB: a covalent binding agent database

Du, J., Yan, X., Liu, Z., Cui, L., Ding, P., Tan, X., Li, X., Zhou, H., Gu, Q., & Xu, J. (2016) · Bioinformatics · doi:10.1093/bioinformatics/btw801 · Cited by 30 · see citing works

Molecular Dynamics Simulations and Dynamic Network Analysis Reveal the Allosteric Unbinding of Monobody to H-Ras Triggered by R135K Mutation

Ni, D., Song, K., Zhang, J., & Lu, S. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18112249 · Cited by 30 · see citing works

Mechanism of activation and the rewired network: New drug design concepts

Nussinov, R., Zhang, M., Maloney, R., Tsai, C., Yavuz, B. R., Tunçbağ, N., & Jang, H. (2021) · Medicinal Research Reviews · doi:10.1002/med.21863 · Cited by 30 · see citing works

Inhibition of Nonfunctional Ras

Nussinov, R., Jang, H., Gürsoy, A., Keskin, Ö., & Gaponenko, V. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2020.12.012 · Cited by 29 · see citing works

Lysine Covalent Antagonists of Melanoma Inhibitors of Apoptosis Protein

Udompholkul, P., Baggio, C., Gambini, L., Alboreggia, G., & Pellecchia, M. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01459 · Cited by 29 · see citing works

Danshensu for Myocardial Ischemic Injury: Preclinical Evidence and Novel Methodology of Quality Assessment Tool

Bao, X., Zheng, Q., Tong, Q., Zhu, P.-C., Zhuang, Z., Zheng, G., & Wang, Y. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01445 · Cited by 28 · see citing works

Chemical Tools for Studying Lipid-Binding Class A G Protein–Coupled Receptors

Cooper, A. G., Singh, S., Hook, S. M., Tyndall, J. D. A., & Vernall, A. J. (2017) · Pharmacological Reviews · doi:10.1124/pr.116.013243 · Cited by 26 · see citing works

Perspective: The promises of a holistic view of proteins—impact on antibody engineering and drug discovery

Phua, S.-X., Chan, K.-F., Su, C. T.-T., Poh, J.-J., & Gan, S. K. (2019) · Bioscience Reports · doi:10.1042/bsr20181958 · Cited by 27 · see citing works

Identification of Cysteine 270 as a Novel Site for Allosteric Modulators of SARS‐CoV‐2 Papain‐Like Protease**

Hu, H., Wang, Q., Su, H., Shao, Q., Zhao, W., Chen, G., Li, M., & Xu, Y. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202212378 · Cited by 21 · see citing works

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 · see citing works

Characteristics of Allosteric Proteins, Sites, and Modulators

He, X., Ni, D., Lu, S., & Zhang, J. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-8719-7_6 · Cited by 22 · see citing works

Mechanistic insights into the clinical Y96D mutation with acquired resistance to AMG510 in the KRASG12C

Zhuang, H., Fan, J., Li, M., Zhang, H., Yang, X., Lin, L., Lu, S., Wang, Q., & Liu, Y. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.915512 · Cited by 23 · see citing works

An allosteric cyclin E-CDK2 site mapped by paralog hopping with covalent probes

Zhang, Y., Liu, Z., Hirschi, M., Brodsky, O., Johnson, E., Won, S. J., Nagata, A., Bezwada, D., Petroski, M. D., Majmudar, J. D., et al. (2024) · Nature Chemical Biology · doi:10.1038/s41589-024-01738-7 · Cited by 21 · see citing works

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 · see citing works

The STING antagonist SN-011 ameliorates cisplatin induced acute kidney injury via suppression of STING/NF-κB-mediated inflammation

Li, Z., Mao, C., Zhao, Y., Zhao, Y., Yi, H., Liu, J., & Liang, J. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.113876 · Cited by 21 · see citing works

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 · see citing works

Leveraging allostery to improve G protein-coupled receptor (GPCR)-directed therapeutics: cannabinoid receptor 1 as discovery target

Janero, D. R., & Thakur, G. A. (2016) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2016.1245289 · Cited by 21 · see citing works

Calmodulin and IQGAP1 activation of PI3Kα and Akt in KRAS, HRAS and NRAS-driven cancers

Nussinov, R., Zhang, M., Tsai, C., & Jang, H. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2017.10.032 · Cited by 20 · see citing works

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 20 · see citing works

Allostery in Disease: Anticancer Drugs, Pockets, and the Tumor Heterogeneity Challenge

Nussinov, R., Yavuz, B. R., & Jang, H. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169050 · Cited by 19 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Information flow and protein dynamics: the interplay between nuclear magnetic resonance spectroscopy and molecular dynamics simulations

Pastor, N., & Amero, C. (2015) · Frontiers in Plant Science · doi:10.3389/fpls.2015.00306 · Cited by 14 · see citing works

Substitution of a Surface-Exposed Residue Involved in an Allosteric Network Enhances Tryptophan Synthase Function in Cells

D’Amico, R. N., Bosken, Y. K., O’Rourke, K. F., Murray, A. M., Admasu, W., Chang, C. A., & Boehr, D. D. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.679915 · Cited by 13 · see citing works

Understanding the P-Loop Conformation in the Determination of Inhibitor Selectivity Toward the Hepatocellular Carcinoma-Associated Dark Kinase STK17B

Liu, C., Li, Z., Liu, Z., Yang, S., Wang, Q., & Chai, Z. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.901603 · Cited by 13 · see citing works

Decoding protein structures with residue interaction networks

Begue, S. C., Leonardi, E., & Tosatto, S. C. E. (2025) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2025.08.006 · Cited by 13 · see citing works

High‐throughput tandem‐microwell assay for ammonia repositions FDA‐Approved drugs to inhibit <i>Helicobacter pylori</i> urease

Liu, F., Yu, J., Zhang, Y., Li, F., Liu, Q., Zhou, Y., Huang, S., Fang, H., Xiao, Z., Liao, L., et al. (2021) · The FASEB Journal · doi:10.1096/fj.202100465rr · Cited by 12 · see citing works

Allosteric Inhibition of Bacterial Targets: An Opportunity for Discovery of Novel Antibacterial Classes

Meisel, J. E., Fisher, J. F., Chang, M., & Mobashery, S. (2017) · Topics in medicinal chemistry · doi:10.1007/7355_2017_21 · Cited by 13 · see citing works

Allosteric regulation of metabolism in cancer: endogenous mechanisms and considerations for drug design

Macpherson, J. A., & Anastasiou, D. (2017) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2017.03.022 · Cited by 12 · see citing works

Strategies for Conditional Regulation of Proteins

Nadendla, K., Simpson, G. G., Becher, J. B., Journeaux, T., Cabeza-Cabrerizo, M., & Bernardes, G. J. L. (2023) · JACS Au · doi:10.1021/jacsau.2c00654 · Cited by 11 · see citing works

Allosteric modulation of SHP2: Quest from known to unknown

Wang, N., Zhu, S., Lv, D., Wang, Y., Khawar, M. B., & Sun, H. (2023) · Drug Development Research · doi:10.1002/ddr.22100 · Cited by 11 · see citing works

Reversible Covalent Reaction of Levosimendan with Cardiac Troponin C in Vitro and in Situ

Klein, B. A., Reiz, B., Robertson, I. M., Irving, M., Li, L., Sun, Y., & Sykes, B. D. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b00109 · Cited by 10 · see citing works

Allosteric Modulators

Lu, S., & Zhang, J. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-409547-2.12324-8 · Cited by 9 · see citing works

Covalent and noncovalent strategies for targeting Lys102 in HIV-1 reverse transcriptase

Prucha, G. R., Henry, S., Hollander, K., Carter, Z. J., Spasov, K. A., Jorgensen, W. L., & Anderson, K. S. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115894 · Cited by 8 · see citing works

Allosteric pluripotency: challenges and opportunities

Akimoto, M., Pomier, K. M., VanSchouwen, B., Byun, J. A., Khamina, M., & Melacini, G. (2022) · Biochemical Journal · doi:10.1042/bcj20210528 · Cited by 8 · see citing works

Allosteric Pathways Originating at Cysteine Residues in Regulators of G-Protein Signaling Proteins

Liu, Y., & Vashisth, H. (2020) · Biophysical Journal · doi:10.1016/j.bpj.2020.12.010 · Cited by 7 · see citing works

Design, synthesis, and biological testing of biphenylmethyloxazole inhibitors targeting HIV-1 reverse transcriptase

Carter, Z. J., Hollander, K., Spasov, K. A., Anderson, K. S., & Jorgensen, W. L. (2023) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2023.129216 · Cited by 6 · see citing works

From covalent bonds to eco-physiological pharmacology of secondary plant metabolites

Chatterjee, S. S. (2015) · Biochemical Pharmacology · doi:10.1016/j.bcp.2015.07.037 · Cited by 6 · see citing works

The m⁶A epitranscriptome: A regulatory nexus linking cellular senescence and oncogenesis

Xu, Y., Zhou, X., Su, X., Xie, W., Huang, Z., Yu, S., Tan, J., He, J., & Zhang, J. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103032 · Cited by 5 · see citing works

Progress in Allosteric Database

Song, K., Zhang, J., & Lu, S. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-8719-7_4 · Cited by 5 · see citing works

Adverse Events

Tridente, G. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-809400-6.00004-4 · Cited by 5 · see citing works

Allosteric drugs in biomolecular condensates: ways forward

Nussinov, R., Regev, C., & Jang, H. (2026) · Drug Discovery Today · doi:10.1016/j.drudis.2026.104632 · Cited by 3 · see citing works

The structural basis of the autoinhibition mechanism of glycogen synthase kinase 3β (GSK3β): molecular modeling and molecular dynamics simulation studies

Mou, L., Dou, W., Meng, G., Sun, K., & Chen, X. (2019) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2019.1615988 · Cited by 3 · see citing works

The Search for Covalently Ligandable Proteins in Biological Systems

Badshah, S. L., & Mabkhot, Y. N. (2016) · Molecules · doi:10.3390/molecules21091170 · Cited by 2 · see citing works

The alternative strategy for designing covalent drugs through kinetic effects of pi-stacking on the self-assembled nanoparticles: a model study with antibiotics

Du, L., Suo, S., Zhang, H., Jia, H., Liu, K. J., Zhang, X. J., & Liu, Y. (2016) · Nanotechnology · doi:10.1088/0957-4484/27/44/445101 · Cited by 2 · see citing works

Single Binding Pockets Versus Allosteric Binding

Song, K., & Zhang, J. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8639-2_9 · Cited by 2 · see citing works

Mapping the SHP2 Allosteric Pocket With Target‐Biased Covalent Fragments

Efrém, N., Csorba, N., Amoussa, M., Ábrányi‐Balogh, P., Guo, Z., Petri, L., Bo, F., di Lorenzo, V., Roske, Y., Szalai, T. V., et al. (2026) · ChemBioChem · doi:10.1002/cbic.70310 · Cited by 1 · see citing works

Target Validation—Prosecuting the Target

Jones, L. H. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820472-6.00014-1 · Cited by 1 · see citing works

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 · see citing works

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 139 · see citing works

Allosteric solution to the problems of undruggable targets, drug toxicity, and emerging resistance

Tee, W.-V., & Berezovsky, I. N. (2025) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2025.103172 · Cited by 16 · see citing works

Approach in Improving Potency and Selectivity of Kinase Inhibitors: Allosteric Kinase Inhibitors

Wei, S., Zhao, T., Wang, J., & Zhai, X. (2020) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557521666201222144355 · Cited by 11 · see citing works

Toward the Design of Allosteric Effectors: Gaining Comprehensive Control of Drug Properties and Actions

Tee, W.-V., Lim, S. J. M., & Berezovsky, I. N. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c01043 · Cited by 23 · see citing works