Dynamic Protein Allosteric Regulation and Disease

Mutations of the BRAF gene in human cancer

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The protein kinase complement of the human genome

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Cell Signaling by Receptor Tyrosine Kinases

Lemmon, M. A., & Schlessinger, J. (2010) · Cell · doi:10.1016/j.cell.2010.06.011 · Cited by 7,929 · see citing works

Untangling the ErbB signalling network

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The Energy Landscapes and Motions of Proteins

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Mechanism of Activation of the RAF-ERK Signaling Pathway by Oncogenic Mutations of B-RAF

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

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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

GEFs and GAPs: Critical Elements in the Control of Small G Proteins

Bos, J. L., Rehmann, H., & Wittinghofer, A. (2007) · Cell · doi:10.1016/j.cell.2007.05.018 · Cited by 1,903 · see citing works

RAF inhibitors transactivate RAF dimers and ERK signalling in cells with wild-type BRAF

Poulikakos, P. I., Zhang, C., Bollag, G. E., Shokat, K. M., & Rosen, N. X. (2010) · Nature · doi:10.1038/nature08902 · Cited by 1,818 · see citing works

The Conformational Plasticity of Protein Kinases

Huse, M., & Kuriyan, J. (2002) · Cell · doi:10.1016/s0092-8674(02)00741-9 · Cited by 1,760 · 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

RAF inhibitors prime wild-type RAF to activate the MAPK pathway and enhance growth

Hatzivassiliou, G., Song, K. W., Yen, I., Brandhuber, B. J., Anderson, D. J., Alvarado, R., Ludlam, M. J. C., Stokoe, D., Gloor, S. L., Vigers, G. P. A., et al. (2010) · Nature · doi:10.1038/nature08833 · Cited by 1,614 · see citing works

Pten is essential for embryonic development and tumour suppression

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Kinase-Dead BRAF and Oncogenic RAS Cooperate to Drive Tumor Progression through CRAF

Heidorn, S. J., Milagre, C. S., Whittaker, S. R., Nourry, A., Niculescu‐Duvaz, I., Dhomen, N. S., Hussain, J., Reis-Filho, J. S., Springer, C. J., Pritchard, C. A., et al. (2010) · Cell · doi:10.1016/j.cell.2009.12.040 · Cited by 1,468 · see citing works

Regulation of Small GTPases by GEFs, GAPs, and GDIs

Cherfils, J., & Zeghouf, M. (2013) · Physiological Reviews · doi:10.1152/physrev.00003.2012 · Cited by 1,245 · see citing works

Structures of Lung Cancer-Derived EGFR Mutants and Inhibitor Complexes: Mechanism of Activation and Insights into Differential Inhibitor Sensitivity

Yun, C.-H., Boggon, T. J., Li, Y., Woo, M. S., Greulich, H., Meyerson, M., & Eck, M. J. (2007) · Cancer Cell · doi:10.1016/j.ccr.2006.12.017 · Cited by 1,192 · see citing works

Regulation of Protein Kinases

Nolen, B. J., Taylor, S. S., & Ghosh, G. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.08.024 · Cited by 1,171 · see citing works

Molecular Switch for Signal Transduction: Structural Differences Between Active and Inactive Forms of Protooncogenic ras Proteins

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ErbB receptors and signaling pathways in cancer

Hynes, N. E., & MacDonald, G. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.12.010 · Cited by 956 · see citing works

Protein kinases: evolution of dynamic regulatory proteins

Taylor, S. S., & Kornev, A. P. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.09.006 · Cited by 940 · 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

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

Allostery in Disease and in Drug Discovery

Nussinov, R., & Tsai, C. (2013) · Cell · doi:10.1016/j.cell.2013.03.034 · Cited by 764 · see citing works

Principles of Protein−Protein Interactions: What are the Preferred Ways For Proteins To Interact?

Keskin, O., Gursoy, A., Ma, B., & Nussinov, R. (2008) · Chemical Reviews · doi:10.1021/cr040409x · Cited by 697 · see citing works

Regulation of RAF protein kinases in ERK signalling

Lavoie, H., & Therrien, M. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3979 · Cited by 695 · 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

Epidermal growth factor induces rapid, reversible aggregation of the purified epidermal growth factor receptor

Yarden, Y., & Schlessinger, J. (1987) · Biochemistry · doi:10.1021/bi00379a035 · Cited by 627 · see citing works

Mechanism for Activation of the EGF Receptor Catalytic Domain by the Juxtamembrane Segment

Jura, N., Endres, N., Engel, K., Deindl, S., Das, R., Lamers, M. H., Wemmer, D. E., Zhang, X., & Kuriyan, J. (2009) · Cell · doi:10.1016/j.cell.2009.04.025 · Cited by 609 · see citing works

Crystal Structure and Functional Analysis of Ras Binding to Its Effector Phosphoinositide 3-Kinase γ

Pacold, M. E., Suire, S., Perišić, O., Lara‐González, S., Davis, C. T., Walker, E. H., Hawkins, P. T., Stephens, L., Eccleston, J. F., & Williams, R. L. (2000) · Cell · doi:10.1016/s0092-8674(00)00196-3 · Cited by 603 · see citing works

Folding and binding cascades: Dynamic landscapes and population shifts

Kumar, S., Ma, B., Tsai, C., Sinha, N., & Nussinov, R. (2000) · Protein Science · doi:10.1110/ps.9.1.10 · Cited by 595 · 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

Spatial control of EGF receptor activation by reversible dimerization on living cells

Chung, I., Akita, R. W., VANDLEN, R. L., Toomre, D. K., Schlessinger, J., & Mellman, I. (2010) · Nature · doi:10.1038/nature08827 · Cited by 538 · see citing works

Hot Regions in Protein–Protein Interactions: The Organization and Contribution of Structurally Conserved Hot Spot Residues

Keskin, O., Ma, B., & Nussinov, R. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.10.077 · Cited by 519 · see citing works

Self-phosphorylation of epidermal growth factor receptor: evidence for a model of intermolecular allosteric activation

Yarden, Y., & Schlessinger, J. (1987) · Biochemistry · doi:10.1021/bi00379a034 · Cited by 506 · see citing works

Mutation of the PIK3CA oncogene in human cancers

Karakas, B., Bachman, K. E., & Park, B. H. (2006) · British Journal of Cancer · doi:10.1038/sj.bjc.6602970 · Cited by 505 · see citing works

A dimerization-dependent mechanism drives RAF catalytic activation

Rajakulendran, T., Sahmi, M., Lefrançois, M., Sicheri, F., & Therrien, M. (2009) · Nature · doi:10.1038/nature08314 · Cited by 492 · see citing works

Serum-, TPA-, and Ras-induced expression from Ap-1/Ets-driven promoters requires Raf-1 kinase.Preprint

Bruder, J. T., Heidecker, G., & Rapp, U. R. (1992) · Genes & Development · doi:10.1101/gad.6.4.545 · Cited by 444 · see citing works

Protein Ensembles: How Does Nature Harness Thermodynamic Fluctuations for Life? The Diverse Functional Roles of Conformational Ensembles in the Cell

Wei, G., Xi, W., Nussinov, R., & Ma, B. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00562 · Cited by 436 · 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

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

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

Folding and binding cascades: Shifts in energy landscapes

Tsai, C.-J., Ma, B., & Nussinov, R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.9970 · Cited by 365 · see citing works

Oncogenic Mutations Counteract Intrinsic Disorder in the EGFR Kinase and Promote Receptor Dimerization

Shan, Y., Eastwood, M. P., Zhang, X., Kim, E. T., Arkhipov, A. S., Dror, R. O., Jumper, J., Kuriyan, J., & Shaw, D. E. (2012) · Cell · doi:10.1016/j.cell.2012.02.063 · Cited by 360 · 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

Thematic review series: Lipid Posttranslational Modifications CAAX modification and membrane targeting of Ras

Wright, L. P., & Philips, M. R. (2006) · Journal of Lipid Research · doi:10.1194/jlr.r600004-jlr200 · Cited by 340 · see citing works

Structural Analysis of Autoinhibition in the Ras Activator Son of Sevenless

Sondermann, H., Soisson, S. M., Boykevisch, S., Yang, S., Bar‐Sagi, D., & Kuriyan, J. (2004) · Cell · doi:10.1016/j.cell.2004.10.005 · Cited by 315 · see citing works

The Juxtamembrane Region of the EGF Receptor Functions as an Activation Domain

Brewer, M. R., Choi, S. H., Alvarado, D., Moravcevic, K., Pozzi, A., Lemmon, M. A., & Carpenter, G. F. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.04.034 · Cited by 314 · see citing works

Catalytic Control in the EGF Receptor and Its Connection to General Kinase Regulatory Mechanisms

Jura, N., Zhang, X., Endres, N. F., Seeliger, M. A., Schindler, T., & Kuriyan, J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.03.004 · Cited by 310 · see citing works

Allosteric Activation of Functionally Asymmetric RAF Kinase Dimers

Hu, J., Stites, E. C., Yu, H., Germino, E., Meharena, H. S., Stork, P. A., Kornev, A. P., Taylor, S. S., & Shaw, A. S. (2013) · Cell · doi:10.1016/j.cell.2013.07.046 · Cited by 302 · see citing works

Lipid-Sorting Specificity Encoded in K-Ras Membrane Anchor Regulates Signal Output

Zhou, Y., Prakash, P., Hong, L., Cho, K., Gorfe, A. A., & Hancock, J. F. (2016) · Cell · doi:10.1016/j.cell.2016.11.059 · Cited by 283 · see citing works

Ras-GTP dimers activate the Mitogen-Activated Protein Kinase (MAPK) pathway

Nan, X., Tamgüney, T. M., Collisson, E. A., Lin, L.-J., Pitt, C., Galeas, J., Lewis, S., Gray, J. W., McCormick, F., & Chu, S. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1509123112 · Cited by 273 · see citing works

A conserved protonation-dependent switch controls drug binding in the Abl kinase

Shan, Y., Seeliger, M. A., Eastwood, M. P., Frank, F., Xu, H., Jensen, M. Ø., Dror, R. O., Kuriyan, J., & Shaw, D. E. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811223106 · Cited by 264 · see citing works

Protein Frustratometer 2: a tool to localize energetic frustration in protein molecules, now with electrostatics

Parra, R. G., Schafer, N. P., Radusky, L., Tsai, M., Guzovsky, A. B., Wolynes, P. G., & Ferreiro, D. U. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw304 · Cited by 263 · see citing works

The Src, Syk, and Tec family kinases: Distinct types of molecular switches

Bradshaw, J. M. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.03.001 · Cited by 257 · see citing works

Structural basis for the interaction of Ras with RaIGDS

Huang, L., Hofer, F., Martin, G. S., & Kim, S. (1998) · Nature Structural Biology · doi:10.1038/nsb0698-422 · Cited by 248 · see citing works

Activation of B‐Raf kinase requires phosphorylation of the conserved residues Thr598 and Ser601

Zhang, B., & Guan, K. (2000) · The EMBO Journal · doi:10.1093/emboj/19.20.5429 · Cited by 247 · see citing works

Mutational Activation of c- raf- 1 and Definition of the Minimal Transforming Sequence

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Definition of the human raf amino-terminal regulatory region by deletion mutagenesis.

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Quantifying Correlations Between Allosteric Sites in Thermodynamic Ensembles

McClendon, C. L., Friedland, G. D., Mobley, D. L., Amirkhani, H., & Jacobson, M. P. (2009) · Journal of Chemical Theory and Computation · doi:10.1021/ct9001812 · Cited by 227 · see citing works

Allosteric Effects of the Oncogenic RasQ61L Mutant on Raf-RBD

Fetics, S., Guterres, H., Kearney, B. M., Buhrman, G., Ma, B., Nussinov, R., & Mattos, C. (2015) · Structure · doi:10.1016/j.str.2014.12.017 · Cited by 225 · see citing works

The Structural Basis of Oncogenic Mutations G12, G13 and Q61 in Small GTPase K-Ras4B

Lu, S., Jang, H., Nussinov, R., & Zhang, J. (2016) · Scientific Reports · doi:10.1038/srep21949 · Cited by 219 · see citing works

3D clusters of somatic mutations in cancer reveal numerous rare mutations as functional targets

Gao, J., Chang, M. T., Johnsen, H. C., Gao, S. P., Sylvester, B. E., Sümer, S. O., Zhang, H., Solit, D. B., Taylor, B. S., Schultz, N. D., et al. (2017) · Genome Medicine · doi:10.1186/s13073-016-0393-x · Cited by 218 · see citing works

Mapping the Nucleotide and Isoform-Dependent Structural and Dynamical Features of Ras Proteins

Gorfe, A. A., Grant, B. J., & McCammon, J. A. (2008) · Structure · doi:10.1016/j.str.2008.03.009 · Cited by 216 · see citing works

Mutations in LZTR1 drive human disease by dysregulating RAS ubiquitination

Steklov, M. Y., Pandolfi, S., Baietti, M. F., Batiuk, A., Carai, P., Najm, P., Zhang, M., Jang, H., Renzi, F., Cai, Y., et al. (2018) · Science · doi:10.1126/science.aap7607 · Cited by 216 · see citing works

Ras/Rap effector specificity determined by charge reversal

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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

GTP-Dependent K-Ras Dimerization

Muratcioglu, S., Chavan, T. S., Freed, B. C., Jang, H., Khavrutskii, L., Freed, R. N., Dyba, M. A., Stefanisko, K., Tarasov, S. G., Gursoy, A., et al. (2015) · Structure · doi:10.1016/j.str.2015.04.019 · Cited by 202 · see citing works

Allostery without a conformational change? Revisiting the paradigm

Nussinov, R., & Tsai, C.-J. (2015) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2014.11.005 · Cited by 202 · see citing works

Structured disorder and conformational selection

Tsai, C., Ma, B., Sham, Y. Y., Kumar, S., & Nussinov, R. (2001) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.1107 · Cited by 202 · see citing works

Effects of Raf Dimerization and Its Inhibition on Normal and Disease-Associated Raf Signaling

Freeman, A. K., Ritt, D. A., & Morrison, D. K. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.12.018 · Cited by 201 · see citing works

Autoregulation of the Raf-1 serine/threonine kinase

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Processive phosphorylation of ERK MAP kinase in mammalian cells

Aoki, K., Yamada, M., Kunida, K., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1104030108 · Cited by 195 · 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

Ras-Mediated Activation of the Raf Family KinasesPreprint

Terrell, E. M., & Morrison, D. K. (2018) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a033746 · Cited by 189 · see citing works

Inhibitors that stabilize a closed RAF kinase domain conformation induce dimerization

Lavoie, H., Thevakumaran, N., Gavory, G., Li, J. J., Padeganeh, A., Guiral, S., Duchaine, J., Mao, D. Y. L., Bouvier, M., Sicheri, F., et al. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1257 · Cited by 176 · see citing works

The Underappreciated Role of Allostery in the Cellular Network

Nussinov, R., Tsai, C., & Ma, B. (2013) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-083012-130257 · Cited by 174 · see citing works

Selected‐fit versus induced‐fit protein binding: Kinetic differences and mutational analysis

Weikl, T. R., & von Deuster, C. I. E. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22223 · Cited by 169 · see citing works

Systematic Functional Interrogation of Rare Cancer Variants Identifies Oncogenic Alleles

Kim, E., Ilić, N., Shrestha, Y., Zou, L., Kamburov, A., Zhu, C., Yang, X., Lubonja, R., Tran, N. H., Nguyen, C., et al. (2016) · Cancer Discovery · doi:10.1158/2159-8290.cd-16-0160 · Cited by 168 · see citing works

The structural basis for the transition from Ras-GTP to Ras-GDP

Hall, B. E., Bar‐Sagi, D., & Nassar, N. N. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.192453199 · Cited by 164 · see citing works

Crystal structure of a BRAF kinase domain monomer explains basis for allosteric regulation

Thevakumaran, N., Lavoie, H., Critton, D., Tebben, A. J., Marinier, A., Sicheri, F., & Therrien, M. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2924 · Cited by 162 · see citing works

Single-molecule superresolution imaging allows quantitative analysis of RAF multimer formation and signaling

Nan, X., Collisson, E. A., Lewis, S., Huang, J., Tamgüney, T., Liphardt, J., McCormick, F. P., Gray, J. W., & Chu, S. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1318188110 · Cited by 159 · see citing works

Structure-based model of allostery predicts coupling between distant sites

Weinkam, P., Pons, J., & Šali, A. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1116274109 · Cited by 157 · see citing works

Molecular switch in signal transduction: Reaction paths of the conformational changes in ras p21

Ma, J., & Karplus, M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.22.11905 · Cited by 156 · see citing works

B-Raf and Raf-1 Are Regulated by Distinct Autoregulatory Mechanisms

Tran, N. H., Wu, X., & Frost, J. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501185200 · Cited by 153 · see citing works

Improved Method for the Identification and Validation of Allosteric Sites

Song, K., Liu, X., Huang, W., Lu, S., Shen, Q., Zhang, L., & Zhang, J. (2017) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.7b00014 · Cited by 152 · see citing works

Eph, a Protein Family Coming of Age: More Confusion, Insight, or Complexity?

Lackmann, M., & Boyd, A. (2008) · Science Signaling · doi:10.1126/stke.115re2 · Cited by 150 · see citing works

Modeling Signal Propagation Mechanisms and Ligand-Based Conformational Dynamics of the Hsp90 Molecular Chaperone Full-Length Dimer

Morra, G., Verkhivker, G. M., & Colombo, G. (2009) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000323 · Cited by 148 · see citing works

Harnessing Allostery: A Novel Approach to Drug Discovery

Lu, S., Li, S., & Zhang, J. (2014) · Medicinal Research Reviews · doi:10.1002/med.21317 · Cited by 146 · see citing works

Simultaneous visualization of the extracellular and cytoplasmic domains of the epidermal growth factor receptor

Mi, L.-Z., Lu, C., Li, Z., Nishida, N., Walz, T., & Springer, T. A. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2092 · Cited by 145 · see citing works

Frustration, function and folding

Ferreiro, D. U., Komives, E. A., & Wolynes, P. G. (2017) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2017.09.006 · Cited by 142 · 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

Computational approaches to mapping allosteric pathways

Feher, V. A., Durrant, J. D., Wart, A. T. V., & Amaro, R. E. (2014) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2014.02.004 · Cited by 138 · see citing works

Protein–protein interaction networks: how can a hub protein bind so many different partners?

Tsai, C.-J., Ma, B., & Nussinov, R. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.07.007 · Cited by 138 · see citing works

Oncogenic Ras Isoforms Signaling Specificity at the Membrane

Nussinov, R., Tsai, C., & Jang, H. (2017) · Cancer Research · doi:10.1158/0008-5472.can-17-2727 · Cited by 122 · 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

Phosphorylation of Raf-1 by p21-activated Kinase 1 and Src Regulates Raf-1 Autoinhibition

Tran, N. H., & Frost, J. A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210318200 · Cited by 116 · see citing works

Transformation Efficiency of RasQ61 Mutants Linked to Structural Features of the Switch Regions in the Presence of Raf

Buhrman, G., Wink, G., & Mattos, C. (2007) · Structure · doi:10.1016/j.str.2007.10.011 · Cited by 116 · see citing works

Regulation of Raf through Phosphorylation and N Terminus-C Terminus Interaction

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Transient Non-native Hydrogen Bonds Promote Activation of a Signaling Protein

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P-loop Conformation Governed Crizotinib Resistance in G2032R-Mutated ROS1 Tyrosine Kinase: Clues from Free Energy Landscape

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Mechanistic insights into the activation of oncogenic forms of EGF receptor

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Investigating the Structure and Dynamics of the PIK3CA Wild-Type and H1047R Oncogenic Mutant

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The molecular basis of targeting protein kinases in cancer therapeutics

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Regulation of the catalytic activity of the EGF receptor

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Proteome-Scale Investigation of Protein Allosteric Regulation Perturbed by Somatic Mutations in 7,000 Cancer Genomes

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‘Latent drivers’ expand the cancer mutational landscape

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Revealing the favorable dissociation pathway of type II kinase inhibitors via enhanced sampling simulations and two-end-state calculations

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Sequence and Structure Signatures of Cancer Mutation Hotspots in Protein Kinases

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Raf-1 Cysteine-Rich Domain Increases the Affinity of K-Ras/Raf at the Membrane, Promoting MAPK Signaling

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Allostery Wiring Diagrams in the Transitions that Drive the GroEL Reaction Cycle

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The higher level of complexity of K‐Ras4B activation at the membrane

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

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

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Oncogenic exon 2 mutations in Mediator subunit MED12 disrupt allosteric activation of cyclin C-CDK8/19

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Allosteric Conformational Barcodes Direct Signaling in the Cell

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Mapping the Conformation Space of Wildtype and Mutant H-Ras with a Memetic, Cellular, and Multiscale Evolutionary Algorithm

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Differential dynamics of RAS isoforms in GDP- and GTP-bound states

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The structural basis for cancer treatment decisions

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Membrane curvature allosterically regulates the phosphatidylinositol cycle, controlling its rate and acyl-chain composition of its lipid intermediates

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Phosphorylation of RAF Kinase Dimers Drives Conformational Changes that Facilitate Transactivation

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Ras Dimer Formation as a New Signaling Mechanism and Potential Cancer Therapeutic Target

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Regulation of K-Ras4B Membrane Binding by Calmodulin

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Autoinhibition in Ras effectors Raf, PI3Kα, and RASSF5: a comprehensive review underscoring the challenges in pharmacological intervention

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The free energy landscape in translational science: how can somatic mutations result in constitutive oncogenic activation?

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Modeling the Role of G12V and G13V Ras Mutations in the Ras-GAP-Catalyzed Hydrolysis Reaction of Guanosine Triphosphate

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Nucleotide Binding Switches the Information Flow in Ras GTPases

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Communication Routes in ARID Domains between Distal Residues in Helix 5 and the DNA-Binding Loops

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Plasma membrane phosphatidylinositol 4-phosphate and 4,5-bisphosphate determine the distribution and function of K-Ras4B but not H-Ras proteins

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Allosteric KRas4B Can Modulate SOS1 Fast and Slow Ras Activation Cycles

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Insights into the key interactions between human protein phosphatase 5 and cantharidin using molecular dynamics and site-directed mutagenesis bioassays

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Molecular mechanisms of asymmetric RAF dimer activation

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Alloscore: a method for predicting allosteric ligand–protein interactions

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Molecular cloning and characterization of an activated human c-raf-1 gene.

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Free Energy Diagrams for Protein Function

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Identification of a transforming activity suppressing sequence in the c-raf oncogene.

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Allosteric activation of RAF in the MAPK signaling pathway

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Towards a Stochastic Paradigm: From Fuzzy Ensembles to Cellular Functions

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Conformational dynamics of cancer-associated MyD88-TIR domain mutant L252P (L265P) allosterically tilts the landscape toward homo-dimerization

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Stability of Iowa mutant and wild type Aβ-peptide aggregates

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Protein dynamics at Eph receptor-ligand interfaces as revealed by crystallography, NMR and MD simulations

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Benchmarking predictions of allostery in liver pyruvate kinase in CAGI4

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Molecular Basis for Allosteric Inhibition of GTP-Bound H-Ras Protein by a Small-Molecule Compound Carrying a Naphthalene Ring

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Allostery modulates the beat rate of a cardiac pacemaker

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AlphaFold, Artificial Intelligence (AI), and Allostery

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Allostery: Allosteric Cancer Drivers and Innovative Allosteric Drugs

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Is allostery an intrinsic property of all dynamic proteins?

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Basic Concepts of Allosteric Control

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Allostery in enzyme catalysis

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Allosteric Type and Pathways Are Governed by the Forces of Protein–Ligand Binding

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