Ras Conformational Ensembles, Allostery, and Signaling

G proteins, effectors and GAPs: structure and mechanism

Sprang, S. R. (1997) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(97)80157-1 · Cited by 150

Harnessing Allostery: A Novel Approach to Drug Discovery

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Phospholipase C epsilon: linking second messengers and small GTPases

Bunney, T. D., & Katan, M. (2006) · Trends in Cell Biology · doi:10.1016/j.tcb.2006.10.007 · Cited by 148

Conformational states of human rat sarcoma (RAS) protein complexed with its natural ligand GTP and their role for effector interaction and GTP hydrolysis

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N-Ras Forms Dimers at POPC Membranes

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Structural Basis for Conformational Dynamics of GTP-bound Ras Protein

Shima, F., Ijiri, Y., Muraoka, S., Liao, J., Ye, M., Araki, M., Matsumoto, K., Yamamoto, N., Sugimoto, T., Yoshikawa, Y., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.125161 · Cited by 148

Protein frustratometer: a tool to localize energetic frustration in protein molecules

Jenik, M., Parra, R. G., Radusky, L., Turjanski, A. G., Wolynes, P. G., & Ferreiro, D. U. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks447 · Cited by 148

Guanosine triphosphatase stimulation of oncogenic Ras mutants

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The importance of being K-Ras

Ellis, C. A., & Clark, G. (2000) · Cellular Signalling · doi:10.1016/s0898-6568(00)00084-x · Cited by 144

Andrographolide derivatives inhibit guanine nucleotide exchange and abrogate oncogenic Ras function

Hocker, H. J., Cho, K.-J., Chen, C.-Y. K., Rambahal, N., Sagineedu, S. R., Shaari, K., Stanslas, J., Hancock, J. F., & Gorfe, A. A. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1300016110 · Cited by 144

Membrane-Mediated Induction and Sorting of K-Ras Microdomain Signaling Platforms

Weise, K., Kapoor, S., Denter, C., Nikolaus, J., Opitz, N., Koch, S., Triola, G., Herrmann, A., Waldmann, H., & Winter, R. (2010) · Journal of the American Chemical Society · doi:10.1021/ja107532q · Cited by 143

K-Ras Nanoclustering Is Subverted by Overexpression of the Scaffold Protein Galectin-3

Shalom‐Feuerstein, R., Plowman, S. J., Rotblat, B., Ariotti, N., Tian, T., Hancock, J. F., & Kloog, Y. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-1117 · Cited by 141

Ras Interaction with Two Distinct Binding Domains in Raf-1 5 Be Required for Ras Transformation

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The interaction of Ras with GTPase‐activating proteins

Wittinghofer, A., Scheffzek, K., & Ahmadian, M. R. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00321-9 · Cited by 135

Ras pathway signaling on endomembranes

Bivona, T. G., & Philips, M. R. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(03)00016-4 · Cited by 134

Structural and Mechanistic Insights into Ras Association Domains of Phospholipase C Epsilon

Bunney, T. D., Harris, R., Gandarillas, N. L., Josephs, M. B., Roe, S. M., Sorli, S., Paterson, H. F., Rodrigues‐Lima, F., Esposito, D., Ponting, C. P., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.008 · Cited by 134

The RalGEF-Ral Effector Signaling Network: The Road Less Traveled for Anti-Ras Drug Discovery

Neel, N. F., Martin, T. D., Stratford, J. K., Zand, T. P., Reiner, D. J., & Der, C. J. (2011) · Genes & Cancer · doi:10.1177/1947601911407329 · Cited by 134

Signal Integration by Lipid-Mediated Spatial Cross Talk between Ras Nanoclusters

Zhou, Y., Hong, L., Rodkey, T. L., Ariotti, N., Parton, R. G., & Hancock, J. F. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01227-13 · Cited by 133

REGULATION OF PHOSPHOLIPASE C ISOZYMES BY RAS SUPERFAMILY GTPASES

Harden, T. K., & Sondek, J. (2006) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.46.120604.141223 · Cited by 133

Improved glucose homeostasis and enhanced insulin signalling in Grb14‐deficient mice

Cooney, G. J., Lyons, R. J., Crew, A. J., Jensen, T. E., Molero, J. C., Mitchell, C. J., Biden, T. J., Ormandy, C. J., James, D. E., & Daly, R. J. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600082 · Cited by 132

Structure-based Mutagenesis Reveals Distinct Functions for Ras Switch 1 and Switch 2 in Sos-catalyzed Guanine Nucleotide Exchange

Hall, B. E., Yang, S. S., Boriack‐Sjodin, P. A., Kuriyan, J., & Bar‐Sagi, D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101727200 · Cited by 132

X-ray crystal structures of transforming p21 ras mutants suggest a transition-state stabilization mechanism for GTP hydrolysis.

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Palmitoylation and localisation of RAS isoforms are modulated by the hypervariable linker domain

Laude, A., & Prior, I. A. (2008) · Journal of Cell Science · doi:10.1242/jcs.020107 · Cited by 131

Ras/MAPK signaling from endomembranes

Fehrenbacher, N., Bar-Sagi, D., & Philips, M. (2009) · Molecular Oncology · doi:10.1016/j.molonc.2009.06.004 · Cited by 131

NORE1A, a homologue of RASSF1A tumour suppressor gene is inactivated in human cancers

Hesson, L. B., Dallol, A., Minna, J. D., Maher, E. R., & Latif, F. (2003) · Oncogene · doi:10.1038/sj.onc.1206191 · Cited by 130

Probing the Structure and Mechanism of Ras Protein with an Expanded Genetic Code

Chung, H., Benson, D. R., & Schultz, P. G. (1993) · Science · doi:10.1126/science.8430333 · Cited by 129

Small Molecule Binding Sites on the Ras:SOS Complex Can Be Exploited for Inhibition of Ras Activation

Winter, J., Anderson, M., Blades, K., Brassington, C., Breeze, A. L., Chresta, C. M., Embrey, K. J., Fairley, G., Faulder, P., Finlay, M. R. V., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/jm501660t · Cited by 127

The GAP arginine finger movement into the catalytic site of Ras increases the activation entropy

Kötting, C., Kallenbach‐Thieltges, A., Suveyzdis, Y., Wittinghofer, A., & Gerwert, K. B. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0712095105 · Cited by 126

The advantages and limitations of protein crystal structures

Acharya, K. R., & Lloyd, M. D. (2004) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2004.10.011 · Cited by 126

Cancer: The Ras renaissance

Ledford, H. K. (2015) · Nature · doi:10.1038/520278a · Cited by 126

Regulation of Ras Signaling Dynamics by Sos-Mediated Positive Feedback

Boykevisch, S., Zhao, C., Sondermann, H., Philippidou, P., Halegoua, S., Kuriyan, J., & Bar‐Sagi, D. (2006) · Current Biology · doi:10.1016/j.cub.2006.09.033 · Cited by 125

The Pro-apoptotic Ras Effector Nore1 May Serve as a Ras-regulated Tumor Suppressor in the Lung

Vos, M. D., Martı́nez, A., Ellis, C. A., Vallecorsa, T., & Clark, G. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211019200 · Cited by 125

Ras signaling from plasma membrane and endomembrane microdomains

Plowman, S. J., & Hancock, J. F. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2005.06.004 · Cited by 124

Targeting Mutant KRAS for Anticancer Therapeutics: A Review of Novel Small Molecule Modulators

Wang, Y., Kaiser, C. E., Frett, B., & Li, H. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm3017706 · Cited by 123

Structural differences between a ras oncogene protein and the normal protein

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ASD v3.0: unraveling allosteric regulation with structural mechanisms and biological networks

Shen, Q., Wang, G., Li, S., Liu, X., Lu, S., Chen, Z., Song, K., Yan, J., Geng, L., Huang, Z., et al. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkv902 · Cited by 122

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

Regulation of RAS oncogenicity by acetylation

Yang, M. H., Nickerson, S., Kim, E. T., Liot, C., Laurent, G., Spang, R., Philips, M. R., Shan, Y., Shaw, D. E., Bar‐Sagi, D., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1201487109 · Cited by 119

On the mechanism of guanosine triphosphate hydrolysis in ras p21 proteins

Langen, R., Schweins, T., & Warshel, A. (1992) · Biochemistry · doi:10.1021/bi00152a002 · Cited by 118

NMR Characterization of Full-length Farnesylated and Non-farnesylated H-Ras and its Implications for Raf Activation

Thapar, R., Williams, J. G., & Campbell, S. L. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.08.106 · Cited by 118

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

Buhrman, G., Foight, G., & Mattos, C. (2007) · Structure · doi:10.1016/j.str.2007.10.011 · Cited by 118

Structural Basis for Inhibition of the Insulin Receptor by the Adaptor Protein Grb14

Depetris, R. S., Hu, J., Gimpelevich, I., Holt, L. J., Daly, R. J., & Hubbard, S. R. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.09.001 · Cited by 117

Ligand-induced conformational changes in ras p21: a normal mode and energy minimization analysis

Ma, J., & Karplus, M. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1313 · Cited by 117

The basis for K-Ras4B binding specificity to protein farnesyl-transferase revealed by 2 Å resolution ternary complex structures

Long, S. B., Casey, P. J., & Beese, L. S. (2000) · Structure · doi:10.1016/s0969-2126(00)00096-4 · Cited by 114

Mechanisms of Membrane Binding of Small GTPase K-Ras4B Farnesylated Hypervariable Region

Jang, H., Abraham, S. J., Chavan, T., Hitchinson, B., Khavrutskii, L., Tarasova, N. I., Nussinov, R., & Gaponenko, V. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.620724 · Cited by 112

The Design of Covalent Allosteric Drugs

Nussinov, R., & Tsai, C.-J. (2015) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010814-124401 · Cited by 112

Membrane-Mediated Induction and Sorting of K-Ras Microdomain Signaling Platforms

Weise, K., Kapoor, S., Denter, C., Nikolaus, J., Opitz, N., Koch, S., Triola, G., Herrmann, A., Waldmann, H., & Winter, R. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2010.12.689 · Cited by 112

Electrostatically optimized Ras-binding Ral guanine dissociation stimulator mutants increase the rate of association by stabilizing the encounter complex

Kiel, C., Selzer, T., Shaul, Y. D., Schreiber, G., & Herrmann, C. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401160101 · Cited by 111

Isoform-Specific Ras Functions in Development and Cancer

Quinlan, M. P., & Settleman, J. E. (2009) · Future Oncology · doi:10.2217/14796694.5.1.105 · Cited by 111

Direct Activation of Phospholipase C-ϵ by Rho

Wing, M. R., Snyder, J. T., Sondek, J., & Harden, T. K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306904200 · Cited by 111

Ras moves to stay in place

Schmick, M., Kraemer, A., & Bastiaens, P. I. H. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.02.004 · Cited by 110

Elucidation of Binding Determinants and Functional Consequences of Ras/Raf-Cysteine-rich Domain Interactions

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Hot-spot mutations in p110α of phosphatidylinositol 3-kinase (PI3K): Differential interactions with the regulatory subunit p85 and with RAS

Zhao, L., & Vogt, P. K. (2010) · Cell Cycle · doi:10.4161/cc.9.3.10599 · Cited by 108

Activation of Phospholipase C-ε by Heterotrimeric G Protein βγ-Subunits

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ASBench: benchmarking sets for allosteric discovery

Huang, W., Wang, G., Shen, Q., Liu, X., Lu, S., Geng, L., Huang, Z., & Zhang, J. (2015) · Bioinformatics · doi:10.1093/bioinformatics/btv169 · Cited by 107

Stabilizing a Weak Binding State for Effectors in the Human Ras Protein by Cyclen Complexes

Rosnizeck, I. C., Gräf, T., Spoerner, M., Traenkle, J., Filchtinski, D., Herrmann, C., Gremer, L., Vetter, I. R., Wittinghofer, A., König, B., et al. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.200907002 · Cited by 107

Compartmentalized signaling of Ras in fission yeast.

Onken, B., Wiener, H. H., Philips, M., & Chang, E. (2006) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0603318103 · Cited by 106

Solution Structure of the State 1 Conformer of GTP-bound H-Ras Protein and Distinct Dynamic Properties between the State 1 and State 2 Conformers

Araki, M., Shima, F., Yoshikawa, Y., Muraoka, S., Ijiri, Y., Nagahara, Y., Shirono, T., Kataoka, T., & Tamura, A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.227074 · Cited by 105

A second molecular biology revolution? The energy landscapes of biomolecular function

Nussinov, R., & Wolynes, P. G. (2014) · Physical Chemistry Chemical Physics · doi:10.1039/c4cp90027h · Cited by 104

Recent computational advances in the identification of allosteric sites in proteins

Lu, S., Huang, W., & Zhang, J. (2014) · Drug Discovery Today · doi:10.1016/j.drudis.2014.07.012 · Cited by 102

Inhibition of Insulin Receptor Catalytic Activity by the Molecular Adapter Grb14

Béréziat, V., Kasus‐Jacobi, A., Perdereau, D., Cariou, B., Girard, J. R., & Burnol, A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106574200 · Cited by 102

Crystal Structures of PI3Kα Complexed with PI103 and Its Derivatives: New Directions for Inhibitors Design

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Site-specific monoubiquitination activates Ras by impeding GTPase-activating protein function

Baker, R., Lewis, S. M., Sasaki, A. T., Wilkerson, E., Locasale, J. W., Cantley, L. C., Kuhlman, B. A., Dohlman, H. G., & Campbell, S. L. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2430 · Cited by 101

QM/MM modeling the Ras–GAP catalyzed hydrolysis of guanosine triphosphate

Grigorenko, B. L., Nemukhin, A. V., Topol, I. A., Cachau, R. E., & Burt, S. K. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20472 · Cited by 99

Novel type of Ras effector interaction established between tumour suppressor NORE1A and Ras switch II

Stieglitz, B., Bee, C., Schwarz, D. F., Yıldız, Ö., Moshnikova, A., Khokhlatchev, A. V., & Herrmann, C. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.125 · Cited by 98

Fundamental Link between Folding States and Functional States of Proteins

Kalbitzer, H. R., Spoerner, M., Ganser, P., Hozsa, C., & Kremer, W. (2009) · Journal of the American Chemical Society · doi:10.1021/ja904314q · Cited by 97

Why does the Ras switch “break” by oncogenic mutations?

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Regulation of Sos Activity by Intramolecular Interactions

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Free energy landscape of activation in a signalling protein at atomic resolution

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Membrane binding of lipidated Ras peptides and proteins — The structural point of view

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Interaction of Ras with phosphoinositide 3-kinase γ

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Dynamic cyclen–metal complexes for molecular sensing and chirality signaling

Shinoda, S. (2012) · Chemical Society Reviews · doi:10.1039/c2cs35295h · Cited by 92

A New View of Ras Isoforms in Cancers

Nussinov, R., Tsai, C., Chakrabarti, M., & Jang, H. (2015) · Cancer Research · doi:10.1158/0008-5472.can-15-1536 · Cited by 92

Three-dimensional structures and properties of a transforming and a nontransforming glycine-12 mutant of p21H-ras

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Cholesterol homeostasis: a key to prevent or slow down neurodegeneration

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The Distinct Conformational Dynamics of K-Ras and H-Ras A59G

Lukman, S., Grant, B. J., Gorfe, A. A., Grant, G. H., & McCammon, J. A. (2010) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000922 · Cited by 90

Ras‐effector interactions, the problem of specificity

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Ras and GTPase-activating protein (GAP) drive GTP into a precatalytic state as revealed by combining FTIR and biomolecular simulations

Rudack, T., Xia, F., Schlitter, J., Kötting, C., & Gerwert, K. B. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1204333109 · Cited by 90

Structures of Ras superfamily effector complexes: What have we learnt in two decades?

Mott, H. R., & Owen, D. (2015) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2014.999191 · Cited by 89

Conformational States of Ras Complexed with the GTP Analogue GppNHp or GppCH2p: Implications for the Interaction with Effector Proteins

Spoerner, M., Nuehs, A., Ganser, P., Herrmann, C., Wittinghofer, A., & Kalbitzer, H. R. (2005) · Biochemistry · doi:10.1021/bi0488000 · Cited by 89

Allosteric Modulation of Ras-GTP Is Linked to Signal Transduction through RAF Kinase

Buhrman, G., Kumar, V. S. S., Cirit, M., Haugh, J. M., & Mattos, C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.193854 · Cited by 88

RAS interaction with PI3K p110α is required for tumor-induced angiogenesis

Murillo, M. M., Zelenay, S., Nye, E. L., Castellano, E., Lassailly, F., Stamp, G., & Downward, J. (2014) · Journal of Clinical Investigation · doi:10.1172/jci74134 · Cited by 88

The Structural Basis of ATP as an Allosteric Modulator

Lu, S., Huang, W., Wang, Q., Shen, Q., Li, S., Nussinov, R., & Zhang, J. (2014) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003831 · Cited by 88

Direct Targeting of Rab‐GTPase–Effector Interactions

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Integrated RAS signaling defined by parallel NMR detection of effectors and regulators

Smith, M. J., & Ikura, M. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1435 · Cited by 87

Functional Consequences of Monoglucosylation of Ha-Ras at Effector Domain Amino Acid Threonine 35

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RalGDS family members couple Ras to Ral signalling and that's not all

Ferro, E., & Trabalzini, L. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.05.010 · Cited by 87

Multiple Regulatory Domains on the Byr2 Protein Kinase

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Nore1 and RASSF1 Regulation of Cell Proliferation and of the MST1/2 Kinases

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Structural Determinants of Ras-Raf Interaction Analyzed in Live Cells

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GTP Binding and Oncogenic Mutations May Attenuate Hypervariable Region (HVR)-Catalytic Domain Interactions in Small GTPase K-Ras4B, Exposing the Effector Binding Site

Lu, S., Banerjee, A., Jang, H., Zhang, J., Gaponenko, V., & Nussinov, R. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.664755 · Cited by 86

Posttranslational processing of the ras superfamily of small GTP-binding proteins

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Crystal structures of the state 1 conformations of the GTP‐bound H‐Ras protein and its oncogenic G12V and Q61L mutants

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The arginine finger strikes again

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Targeting RAS and PI3K in lung cancer

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SnapShot: Ras Signaling

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Interactions between Ras proteins and their effectors

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Direct Modulation of Small GTPase Activity and Function

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High-affinity interaction of the K-Ras4B hypervariable region with the RAS active site

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Identification of Residues of the H-Ras Protein Critical for Functional Interaction with Guanine Nucleotide Exchange Factors

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The Key Role of Calmodulin in KRAS-Driven Adenocarcinomas

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Two Ras Pathways in Fission Yeast Are Differentially Regulated by Two Ras Guanine Nucleotide Exchange Factors

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Structure of the G60A Mutant of Ras

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Inhibitors of Ras–SOS Interactions

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K-Ras Regulates the Steady-state Expression of Matrix Metalloproteinase 2 in Fibroblasts

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

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RalGDS Functions in Ras- and cAMP-mediated Growth Stimulation

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Two conformational states of Ras GTPase exhibit differential GTP-binding kinetics

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The Role of Magnesium for Geometry and Charge in GTP Hydrolysis, Revealed by Quantum Mechanics/Molecular Mechanics Simulations

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US National Cancer Institute's new Ras project targets an old foe

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Segregation of Negatively Charged Phospholipids by the Polycationic and Farnesylated Membrane Anchor of Kras

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“Pathway drug cocktail”: targeting Ras signaling based on structural pathways

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The role of the metal ion in the p21ras catalysed GTP-hydrolysis: Mn2+ versus Mg2+

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

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NORE1A is a Ras senescence effector that controls the apoptotic/senescent balance of p53 via HIPK2

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Characterization of a novel oncogenic K-ras mutation in colon cancer

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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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The Differential Palmitoylation States of N‐Ras and H‐Ras Determine Their Distinct Golgi Subcompartment Localizations

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The arginine finger of RasGAP helps Gln-61 align the nucleophilic water in GAP-stimulated hydrolysis of GTP

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Structure of a Transient Intermediate for GTP Hydrolysis by Ras

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Mutation analysis in Costello syndrome: functional and structural characterization of theHRASp.Lys117Arg mutation

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Involvement of the Switch 2 Domain of Ras in Its Interaction with Guanine Nucleotide Exchange Factors

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Tumor suppressor role of phospholipase Cε in Ras-triggered cancers

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The structural basis for cancer treatment decisions

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Structure of the Dominant Negative S17N Mutant of Ras,

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Lessons from computer simulations of Ras proteins in solution and in membrane

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The spatial structure of cell signaling systems

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Mathematical Modeling of K-Ras Nanocluster Formation on the Plasma Membrane

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The Activation of RalGDS Can Be Achieved Independently of Its Ras Binding Domain

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Specific cancer-associated mutations in the switch III region of Ras increase tumorigenicity by nanocluster augmentation

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Aggregation of Lipid-Anchored Full-Length H-Ras in Lipid Bilayers: Simulations with the MARTINI Force Field

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Therapeutic modulation of k-ras signaling in colorectal cancer

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A Systems Perspective of Ras Signaling in Cancer

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A Comparative CEST NMR Study of Slow Conformational Dynamics of Small GTPases Complexed with GTP and GTP Analogues

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Sequence Analysis Identifies a Ras-Associating (RA)-like Domain in the N-Termini of Band 4.1/JEF Domains and in the Grb7/10/14 Adapter Family

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Identification of residues of the H-ras protein critical for functional interaction with guanine nucleotide exchange factors.

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Oligomerization and nanocluster organization render specificity

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Carboxyl Methylation of Ras Regulates Membrane Targeting and Effector Engagement*

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Dual Activation of Phospholipase C-ϵ by Rho and Ras GTPases

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Apelin activates the expression of inflammatory cytokines in microglial BV2 cells via PI-3K/Akt and MEK/Erk pathways

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DRoP: A Water Analysis Program Identifies Ras-GTP-Specific Pathway of Communication between Membrane-Interacting Regions and the Active Site

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Backbone conformational flexibility of the lipid modified membrane anchor of the human N-Ras protein investigated by solid-state NMR and molecular dynamics simulation

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Monitoring Ras Interactions with the Nucleotide Exchange Factor Son of Sevenless (Sos) Using Site-specific NMR Reporter Signals and Intrinsic Fluorescence

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Regulatory links between PLC enzymes and Ras superfamily GTPases: Signalling via PLCɛ

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A method for the second-site screening of K-Ras in the presence of a covalently attached first-site ligand

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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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The disordered hypervariable region and the folded catalytic domain of oncogenic K-Ras4B partner in phospholipid binding

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Principles of K-Ras effector organization and the role of oncogenic K-Ras in cancer initiation through G1 cell cycle deregulation

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Design, Synthesis and Biological Evaluation of Sugar‐Derived Ras Inhibitors

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Functional Intracellular Antibody Fragments Do Not Require Invariant Intra-domain Disulfide Bonds

Tanaka, T. U., & Rabbitts, T. H. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.11.085 · Cited by 39

Bisphenol A Binds to Ras Proteins and Competes with Guanine Nucleotide Exchange: Implications for GTPase-Selective Antagonists

Schöpel, M., Jockers, K. F. G., Düppe, P. M., Autzen, J., Potheraveedu, V. N., Ince, S., Yip, K. T., Heumann, R., Herrmann, C., Scherkenbeck, J., et al. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm401291q · Cited by 39

Nucleotide Binding Switches the Information Flow in Ras GTPases

Raimondi, F., Portella, G., Orozco, M., & Fanelli, F. (2011) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1001098 · Cited by 38

p120 Ras GTPase-activating Protein Interacts with Ras-GTP through Specific Conserved Residues

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Dynamic multiprotein assemblies shape the spatial structure of cell signaling

Nussinov, R., & Jang, H. (2014) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2014.07.002 · Cited by 38

Glutathiolated Ras: Characterization and implications for Ras activation

Hobbs, G. A., Bonini, M. G., Gunawardena, H. P., Chen, X., & Campbell, S. L. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.10.531 · Cited by 37

Tumor biomarkers for diagnosis, prognosis and targeted therapy

Zhou, Y., Tao, L., Qiu, J., Xu, J., Yang, X., Zhang, Y., Tian, X., Guan, X., Cen, X., & Zhao, Y. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01823-2 · Cited by 836

Anticancer drug resistance: An update and perspective

Nussinov, R., Tsai, C., & Jang, H. (2021) · Drug Resistance Updates · doi:10.1016/j.drup.2021.100796 · Cited by 410

Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials

Xie, X., Yu, T., Li, X., Zhang, N., Foster, L. J., Peng, C., Huang, W., & He, G. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01589-z · Cited by 396

A model for RAS mutation patterns in cancers: finding the sweet spot

Li, S., Balmain, A., & Counter, C. M. (2018) · Nature Reviews Cancer · doi:10.1038/s41568-018-0076-6 · Cited by 384

Targeted protein degradation: advances in drug discovery and clinical practice

Zhong, G., Chang, X., Xie, W., & Zhou, X. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02004-x · Cited by 326

Ras Signaling: Allostery, Conformation, and Function

Nussinov, R., & Jang, H. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2017.11.2216

The Allosteric Switch and Conformational States in Ras GTPase Affected by Small Molecules

Johnson, C. W., & Mattos, C. (2013) · The Enzymes · doi:10.1016/b978-0-12-416749-0.00003-8 · Cited by 35

Relation between the Conformational Heterogeneity and Reaction Cycle of Ras: Molecular Simulation of Ras

Kobayashi, C., & Saito, S. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.09.063 · Cited by 33

Divergent Mechanisms Activating RAS and Small GTPases Through Post-translational Modification

Osaka, N., Hirota, Y., Ito, D., Ikeda, Y., Kamata, R., Fujii, Y., Chirasani, V. R., Campbell, S. L., Takeuchi, K., Senda, T., et al. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.707439 · Cited by 35

Allosteric Modulation of Ras-GTP Is Linked to Signal Transduction through RAF Kinase

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