Drugging Ras GTPase: a comprehensive mechanistic and signaling structural view
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In this review we overview current advances in Ras structural knowledge and the signaling pathways that can be co-targeted along with Ras to mitigate drug resistance.
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Designing PPI inhibitors to block the interaction of RAS and RAS effect factors represents a promising paradigm for modulating RAS function and provides new impetus for the discovery of related drugs.
“Designing PPI inhibitors to block the interaction of RAS and RAS effect factors represents a promising paradigm for modulating RAS function and provides new impetus for the discovery of related drugs.86,326–329”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [326]
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Hallmarks of Cancer: The Next Generation
Hanahan, D., & Weinberg, R. A. (2011) · Cell · doi:10.1016/j.cell.2011.02.013 · Cited by 66,590 · see citing works
Vogelstein, B., Papadopoulos, N., Velculescu, V. E., Zhou, S., Diaz, L. A., & Kinzler, K. W. (2013) · Science · doi:10.1126/science.1235122 · Cited by 7,863 · see citing works
Multidrug resistance in cancer: role of ATP–dependent transporters
Gottesman, M. M., Fojo, T., & Bates, S. E. (2002) · Nature Reviews Cancer · doi:10.1038/nrc706 · Cited by 5,536 · see citing works
Cancer drug resistance: an evolving paradigm
Holohan, C., Van Schaeybroeck, S., Longley, D. B., & Johnston, P. G. (2013) · Nature Reviews Cancer · doi:10.1038/nrc3599 · Cited by 4,681 · see citing works
<i>EGFR</i> Mutation and Resistance of Non–Small-Cell Lung Cancer to Gefitinib
Kobayashi, S., Boggon, T. J., Dayaram, T., Jänne, P. A., Kocher, O., Meyerson, M., Johnson, B. E., Eck, M. J., Tenen, D. G., & Halmos, B. (2005) · New England Journal of Medicine · doi:10.1056/nejmoa044238 · Cited by 3,964 · see citing works
Barbacid, M. (1987) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.56.070187.004023 · Cited by 3,885 · see citing works
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 RAS signalling pathways in cancer therapy
Downward, J. (2003) · Nature reviews. Cancer · doi:10.1038/nrc969 · Cited by 3,262 · see citing works
ABT-199, a potent and selective BCL-2 inhibitor, achieves antitumor activity while sparing platelets
Souers, A. J., Leverson, J. D., Boghaert, E. R., Ackler, S. L., Catron, N. D., Chen, J., Dayton, B. D., Ding, H., Enschede, S. H., Fairbrother, W. J., et al. (2013) · Nature Medicine · doi:10.1038/nm.3048 · Cited by 3,058 · 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
COSMIC: mining complete cancer genomes in the Catalogue of Somatic Mutations in Cancer
Forbes, S. A., Bindal, N., Bamford, S., Cole, C., Kok, C. Y., Beare, D., Jia, M., Shepherd, R., Leung, K., Menzies, A., et al. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkq929 · Cited by 2,278 · see citing works
A Comprehensive Survey of Ras Mutations in Cancer
Prior, I. A., Lewis, P. D., & Mattos, C. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-2612 · Cited by 2,063 · see citing works
Drugging the undruggable RAS: Mission Possible?
Cox, A. D., Fesik, S. W., Kimmelman, A. C., Luo, J., & Der, C. J. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4389 · Cited by 1,997 · 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
RAS oncogenes: the first 30 years
Malumbres, M., & Barbacid, M. (2003) · Nature Reviews Cancer · doi:10.1038/nrc1097 · Cited by 1,902 · see citing works
RAS oncogenes: weaving a tumorigenic web
Pylayeva-Gupta, Y., Grabocka, E., & Bar-Sagi, D. (2011) · Nature Reviews Cancer · doi:10.1038/nrc3106 · Cited by 1,789 · see citing works
Overriding Imatinib Resistance with a Novel ABL Kinase Inhibitor
Shah, N. P., Tran, C., Lee, F. Y., Chen, P., Norris, D. J., & Sawyers, C. L. (2004) · Science · doi:10.1126/science.1099480 · Cited by 1,785 · see citing works
Molecular mechanisms of drug resistance
Longley, D., & Johnston, P. (2005) · The Journal of Pathology · doi:10.1002/path.1706 · Cited by 1,686 · see citing works
Mammalian ABC Transporters in Health and Disease
Borst, P., & Elferink, R. P. J. O. (2002) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.71.102301.093055 · Cited by 1,566 · see citing works
The Ras-RasGAP Complex: Structural Basis for GTPase Activation and Its Loss in Oncogenic Ras Mutants
Scheffzek, K., Ahmadian, M. R., Kabsch, W., Wiesmüller, L., Lautwein, A., Schmitz, F., & Wittinghofer, A. (1997) · Science · doi:10.1126/science.277.5324.333 · Cited by 1,543 · see citing works
Ras oncogenes: split personalities
Karnoub, A. E., & Weinberg, R. A. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2438 · Cited by 1,467 · see citing works
Meaningful relationships: the regulation of the Ras/Raf/MEK/ERK pathway by protein interactions
Kölch, W. (2000) · Biochemical Journal · doi:10.1042/bj3510289 · Cited by 1,443 · see citing works
MMP-9 Supplied by Bone Marrow–Derived Cells Contributes to Skin Carcinogenesis
Coussens, L. M., Tinkle, C. L., Hanahan, D., & Werb, Z. (2000) · Cell · doi:10.1016/s0092-8674(00)00139-2 · Cited by 1,306 · 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
Targeting RAS–ERK signalling in cancer: promises and challenges
Samatar, A. A., & Poulikakos, P. I. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4281 · Cited by 1,163 · see citing works
Directed Self-Assembly of Monodisperse Phospholipid Bilayer Nanodiscs with Controlled Size
Denisov, I. G., Grinkova, Y. V., Lazarides, A. A., & Sligar, S. G. (2004) · Journal of the American Chemical Society · doi:10.1021/ja0393574 · Cited by 1,066 · see citing works
Small-Molecule Inhibitors of Protein-Protein Interactions: Progressing toward the Reality
Arkin, M. R., Tang, Y., & Wells, J. A. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.09.001 · Cited by 1,065 · see citing works
RAS isoforms and mutations in cancer at a glance
Hobbs, G. A., Der, C. J., & Rossman, K. L. (2016) · Journal of Cell Science · doi:10.1242/jcs.182873 · Cited by 973 · see citing works
Ras in Cancer and Developmental Diseases
Fernández‐Medarde, A., & Santos, E. (2011) · Genes & Cancer · doi:10.1177/1947601911411084 · Cited by 959 · see citing works
Intratumor Heterogeneity: Evolution through Space and Time
Swanton, C. (2012) · Cancer Research · doi:10.1158/0008-5472.can-12-2217 · Cited by 931 · see citing works
K- and N-Ras Are Geranylgeranylated in Cells Treated with Farnesyl Protein Transferase Inhibitors
Whyte, D. B., Kirschmeier, P., Hockenberry, T. N., Nunez-Oliva, I., James, L., Catino, J. J., Bishop, W. R., & Pai, J.-K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.22.14459 · Cited by 884 · see citing works
Blocking Oncogenic Ras Signaling for Cancer Therapy
Adjei, A. A. (2001) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/93.14.1062 · Cited by 831 · see citing works
Targeting RAF kinases for cancer therapy: BRAF-mutated melanoma and beyond
Holderfield, M. T., Deuker, M. M., McCormick, F. P., & McMahon, M. (2014) · Nature reviews. Cancer · doi:10.1038/nrc3760 · Cited by 828 · see citing works
Human RAS Superfamily Proteins and Related GTPases
Colicelli, J. (2004) · Science s STKE · doi:10.1126/stke.2502004re13 · Cited by 828 · see citing works
Self-Assembly of Discoidal Phospholipid Bilayer Nanoparticles with Membrane Scaffold Proteins
Bayburt, T. H., Grinkova, Y. V., & Sligar, S. G. (2002) · Nano Letters · doi:10.1021/nl025623k · Cited by 814 · see citing works
The structural basis of the activation of Ras by Sos
Boriack-Sjodin, P. A., Margarit, S. M., Bar-Sagi, D., & Kuriyan, J. (1998) · Nature · doi:10.1038/28548 · Cited by 799 · see citing works
Stephen, A. G., Esposito, D., Bagni, R. K., & McCormick, F. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.02.017 · Cited by 795 · see citing works
Understanding Ras: ‘it ain’t over ’til it’s over’
Shields, J. M., Pruitt, K., McFall, A. J., Maddox, A. S., & Der, C. J. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01740-2 · Cited by 780 · see citing works
Protein–protein interactions define specificity in signal transductionPreprint
Pawson, T. J., & Nash, P. (2000) · Genes & Development · doi:10.1101/gad.14.9.1027 · Cited by 775 · 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
Self-citationSelective inhibition of oncogenic KRAS output with small molecules targeting the inactive state
Patricelli, M. P., Janes, M. R., Li, L.-S., Hansen, R., Peters, U., Kessler, L. V., Chen, Y., Kucharski, J. M., Feng, J., Ely, T., et al. (2016) · Cancer Discovery · doi:10.1158/2159-8290.cd-15-1105 · Cited by 759 · see citing works
Luca, A. D., Maiello, M. R., D’Alessio, A., Pergameno, M., & Normanno, N. (2012) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2011.639361 · Cited by 737 · see citing works
Drugging the p53 pathway: understanding the route to clinical efficacy
Khoo, K. H., Verma, C. S., & Lane, D. P. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4236 · Cited by 723 · see citing works
Ras history: The saga continues
Cox, A. D., & Der, C. J. (2010) · Small GTPases · doi:10.4161/sgtp.1.1.12178 · Cited by 706 · 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
Self-citationAllele-specific inhibitors inactivate mutant KRAS G12C by a trapping mechanism
Lito, P., Solomon, M., Li, L.-S., Hansen, R., & Rosen, N. (2016) · Science · doi:10.1126/science.aad6204 · Cited by 691 · see citing works
KRAS: feeding pancreatic cancer proliferation
Bryant, K. L., Mancias, J. D., Kimmelman, A. C., & Der, C. J. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.12.004 · Cited by 675 · see citing works
Accessing protein conformational ensembles using room-temperature X-ray crystallography
Fraser, J. S., Bedem, H. V. D., Samelson, A. J., Lang, P. T., Holton, J. M., Echols, N., & Alber, T. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1111325108 · Cited by 619 · see citing works
The effects of deregulated DNA damage signalling on cancer chemotherapy response and resistance
Bouwman, P., & Jonkers, J. (2012) · Nature Reviews Cancer · doi:10.1038/nrc3342 · Cited by 615 · 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
Small molecule inhibition of the KRAS–PDEδ interaction impairs oncogenic KRAS signalling
Zimmermann, G., Papke, B., Ismail, S., Vartak, N., Chandra, A., Hoffmann, M., Hahn, S. A., Triola, G., Wittinghofer, A., Bastiaens, P. I. H., et al. (2013) · Nature · doi:10.1038/nature12205 · Cited by 596 · see citing works
Binding of Ras to Phosphoinositide 3-Kinase p110α Is Required for Ras- Driven Tumorigenesis in Mice
Gupta, S., Ramjaun, A. R., Haiko, P., Wang, Y., Warne, P. H., Nicke, B., Nye, E. L., Stamp, G., Alitalo, K. K., & Downward, J. (2007) · Cell · doi:10.1016/j.cell.2007.03.051 · Cited by 589 · see citing works
Genome-wide analysis of ETS-family DNA-binding in vitro and in vivo
Wei, G., Badis, G., Berger, M. F., Kivioja, T., Palin, K., Enge, M., Bonke, M., Jolma, A., Varjosalo, M., Gehrke, A. R., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.106 · Cited by 568 · see citing works
Regulating the regulator: post-translational modification of RAS
Ahearn, I. M., Haigis, K. M., Bar‐Sagi, D., & Philips, M. R. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3255 · Cited by 557 · see citing works
Bell, D. W., Gore, I., Okimoto, R. A., Godin-Heymann, N., Sordella, R., Mulloy, R., Sharma, S. V., Brannigan, B. W., Mohapatra, G., Settleman, J., et al. (2005) · Nature Genetics · doi:10.1038/ng1671 · Cited by 529 · see citing works
Circumventing cancer drug resistance in the era of personalized medicine
Garraway, L. A., & Jänne, P. A. (2012) · Cancer Discovery · doi:10.1158/2159-8290.cd-12-0012 · Cited by 503 · see citing works
Modulators of Protein–Protein Interactions
Milroy, L.-G., Grossmann, T. N., Hennig, S., Brunsveld, L., & Ottmann, C. (2014) · Chemical Reviews · doi:10.1021/cr400698c · Cited by 497 · see citing works
Discovery of Small Molecules that Bind to K‐Ras and Inhibit Sos‐Mediated Activation
Sun, Q., Burke, J. P., Phan, J., Burns, M. C., Olejniczak, E. T., Waterson, A. G., Lee, T., Rossanese, O. W., & Fesik, S. W. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201201358 · Cited by 490 · see citing works
Margarit, S. M., Sondermann, H., Hall, B. E., Nagar, B., Hoelz, A., Pirruccello, M., Bar‐Sagi, D., & Kuriyan, J. (2003) · Cell · doi:10.1016/s0092-8674(03)00149-1 · Cited by 486 · see citing works
Marshall, C. J. (1996) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(96)80066-4 · Cited by 463 · see citing works
Ras oncogenes and their downstream targets
Rajalingam, K., Schreck, R., Rapp, U. R., & Albert, Š. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2007.01.012 · Cited by 458 · see citing works
Colon Cancer Stem Cells: Promise of Targeted Therapy
Todaro, M., Francipane, M. G., Medema, J. P., & Stassi, G. (2010) · Gastroenterology · doi:10.1053/j.gastro.2009.12.063 · Cited by 444 · see citing works
Tenbaum, S. P., Ordóñez‐Morán, P., Puig, I., Chicote, I., Arqués, O., Landolfi, S., Fernández, Y., Herance, J. R., Gispert, J. D., Mendizabal, L., et al. (2012) · Nature Medicine · doi:10.1038/nm.2772 · Cited by 386 · see citing works
The Ras protein superfamily: Evolutionary tree and role of conserved amino acids
Rojas, A. M., Fuentes, G., Rausell, A., & Valencia, A. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201103008 · Cited by 378 · see citing works
Confirmation of the arginine-finger hypothesis for the GAP-stimulated GTP-hydrolysis reaction of Ras
Ahmadian, M. R., Stege, P., Scheffzek, K., & Wittinghofer, A. (1997) · Nature Structural Biology · doi:10.1038/nsb0997-686 · Cited by 375 · see citing works
eIF4F is a nexus of resistance to anti-BRAF and anti-MEK cancer therapies
Boussemart, L., Malka-Mahieu, H., Girault, I., Allard, D., Hemmingsson, O., Tomasic, G., Thomas, M., Basmadjian, C., Ribeiro, N., Thuaud, F., et al. (2014) · Nature · doi:10.1038/nature13572 · Cited by 373 · see citing works
Strategies for reversing drug resistance
Fojo, T., & Bates, S. E. (2003) · Oncogene · doi:10.1038/sj.onc.1206951 · Cited by 358 · 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
Self-citationTargeting RAS Membrane Association: Back to the Future for Anti-RAS Drug Discovery?
Cox, A. D., Der, C. J., & Philips, M. R. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-3214 · Cited by 351 · see citing works
Dynamic properties of the Ras switch I region and its importance for binding to effectors
Spoerner, M., Herrmann, C., Vetter, I. R., Kalbitzer, H. R., & Wittinghofer, A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.081441398 · Cited by 324 · see citing works
Therapeutic Strategies for Targeting Ras Proteins
Gysin, S., Salt, M. B., Young, A. E., & McCormick, F. (2011) · Genes & Cancer · doi:10.1177/1947601911412376 · Cited by 321 · see citing works
McCormick, F. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-2662 · Cited by 320 · see citing works
Therapeutic Targeting of Oncogenic K‐Ras by a Covalent Catalytic Site Inhibitor
Lim, S. M., Westover, K. D., Ficarro, S. B., Harrison, R. A., Choi, H. G., Pacold, M. E., Carrasco, M., Hunter, J., Kim, N. D., Xie, T., et al. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201307387 · Cited by 300 · see citing works
Mutant KRAS is a druggable target for pancreatic cancer
Zorde Khvalevsky, E., Gabai, R., Rachmut, I. H., Horwitz, E., Brunschwig, Z., Orbach, A., Shemi, A., Golan, T., Domb, A. J., Yavin, E., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1314307110 · Cited by 295 · see citing works
A Small Molecule RAS-Mimetic Disrupts RAS Association with Effector Proteins to Block Signaling
Divakar, S. K. A., Carpio, R. V., Dutta, K., Baker, S. J., Cosenza, S. C., Basu, I., Gupta, Y. K., Reddy, M. V. R., Ueno, L. A., Hart, J. R., et al. (2016) · Cell · doi:10.1016/j.cell.2016.03.045 · Cited by 278 · 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
Functional Specificity of Ras Isoforms: So Similar but So Different
Castellano, E., & Santos, E. (2011) · Genes & Cancer · doi:10.1177/1947601911408081 · Cited by 273 · see citing works
Schweins, T., Geyer, M., Scheffzek, K., Warshel, A., Kalbitzer, H. R., & Wittinghofer, A. (1995) · Nature Structural Biology · doi:10.1038/nsb0195-36 · Cited by 272 · see citing works
Inhibition of protein–protein interactions using designed molecules
Wilson, A. J. (2009) · Chemical Society Reviews · doi:10.1039/b807197g · Cited by 262 · see citing works
NMR-based functional profiling of RASopathies and oncogenic RAS mutations
Smith, M. J., Neel, B. G., & Ikura, M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218173110 · 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
Allosteric modulation of Ras positions Q61 for a direct role in catalysis
Buhrman, G., Holzapfel, G. A., Fetics, S., & Mattos, C. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912226107 · Cited by 246 · see citing works
Small RNA combination therapy for lung cancer
Xue, W., Dahlman, J. E., Tammela, T., Khan, O. F., Sood, S., Dave, A., Cai, W., Chirino, L. M., Yang, G. R., Bronson, R. T., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1412686111 · Cited by 243 · see citing works
Hunter, J. C., Gurbani, D., Ficarro, S. B., Carrasco, M. A., Lim, S. M., Choi, H. G., Xie, T., Marto, J. A., Chen, Z., Gray, N. S., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1404639111 · Cited by 242 · see citing works
K-Ras4A splice variant is widely expressed in cancer and uses a hybrid membrane-targeting motif
Tsai, F. D., Lopes, M. S., Zhou, M., Court, H., Ponce, O., Fiordalisi, J. J., Gierut, J. J., Cox, A. D., Haigis, K. M., & Philips, M. R. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1412811112 · Cited by 226 · 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
Self-citationMazhab-Jafari, M. T., Marshall, C. B., Smith, M. J., Gasmi-Seabrook, G. M. C., Stathopulos, P. B., Inagaki, F., Kay, L. E., Neel, B. G., & Ikura, M. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1419895112 · Cited by 220 · 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
Self-citationMapping 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
Small-molecule modulation of Ras signaling
Spiegel, J., Cromm, P. M., Zimmermann, G., Grossmann, T. N., & Waldmann, H. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1560 · Cited by 215 · see citing works
Ilić, N., Utermark, T., Widlund, H. R., & Roberts, T. M. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1108237108 · Cited by 213 · see citing works
Gorfe, A. A., Hanzal‐Bayer, M., Abankwa, D., Hancock, J. F., & McCammon, J. A. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm061053f · Cited by 209 · 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
Self-citationApproach for targeting Ras with small molecules that activate SOS-mediated nucleotide exchange
Burns, M. C., Sun, Q., Daniels, R. N., Camper, D., Kennedy, J. P., Phan, J., Olejniczak, E. T., Lee, T., Waterson, A. G., Rossanese, O. W., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1315798111 · Cited by 199 · see citing works
A novel switch region regulates H‐ras membrane orientation and signal output
Abankwa, D., Hanzal‐Bayer, M., Ariotti, N., Plowman, S. J., Gorfe, A. A., Parton, R. G., McCammon, J. A., & Hancock, J. F. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.10 · Cited by 199 · see citing works
K-Ras promotes tumorigenicity through suppression of non-canonical Wnt signaling
Wang, M.-T., Holderfield, M., Galeas, J., Delrosario, R., To, M. D., Balmain, A., & McCormick, F. (2015) · Cell · doi:10.1016/j.cell.2015.10.041 · Cited by 196 · see citing works
Role of Oncogenic K-Ras in Cancer Stem Cell Activation by Aberrant Wnt/β-Catenin Signaling
Moon, B.-S., Jeong, W.-J., Park, J., Kim, T. I., Min, D. S., & Choi, K. (2014) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djt373 · Cited by 185 · see citing works
Requirement for Interaction of PI3-Kinase p110α with RAS in Lung Tumor Maintenance
Castellano, E., Sheridan, C., Thin, M. Z., Nye, E. L., Spencer‐Dene, B., Diefenbacher, M. E., Moore, C., Kumar, M. S., Murillo, M. M., Gronroos, E. C., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.09.012 · Cited by 184 · see citing works
Grant, B. J., Gorfe, A. A., & McCammon, J. A. (2009) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000325 · Cited by 182 · see citing works
Arqués, O., Chicote, I., Puig, I., Tenbaum, S. P., Argilés, G., Dienstmann, R., Fernández, N., Caratù, G., Matito, J., Silberschmidt, D., et al. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-3081 · Cited by 179 · see citing works
Ras–effector interactions: after one decade
Herrmann, C. (2003) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(02)00007-6 · Cited by 179 · 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
Koide, H., Satoh, T., Nakafuku, M., & Kaziro, Y. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.18.8683 · 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
Self-citationScheffzek, K., Lautwein, A., Kabsch, W., Ahmadian, M. R., & Wittinghofer, A. (1996) · Nature · doi:10.1038/384591a0 · Cited by 173 · see citing works
Organization, dynamics, and segregation of Ras nanoclusters in membrane domains
Janosi, L., Li, Z., Hancock, J. F., & Gorfe, A. A. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1200773109 · Cited by 170 · see citing works
State-of-the-art strategies for targeting protein–protein interactions by small-molecule inhibitors
Sheng, C., Dong, G., Miao, Z., Zhang, W., & Wang, W. (2015) · Chemical Society Reviews · doi:10.1039/c5cs00252d · Cited by 165 · see citing works
A chemical-genetic screen reveals a mechanism of resistance to PI3K inhibitors in cancer
Muellner, M. K., Uras, I. Z., Gapp, B. V., Kerzendorfer, C., Šmída, M., Lechtermann, H., Craig-Mueller, N., Colinge, J., Duernberger, G., & Nijman, S. M. B. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.695 · Cited by 165 · 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
Direct inhibition of oncogenic KRAS by hydrocarbon-stapled SOS1 helices
Leshchiner, E. S., Parkhitko, A. A., Bird, G. H., Luccarelli, J., Bellairs, J. A., Escudero, S., Opoku-Nsiah, K., Godes, M., Perrimon, N., & Walensky, L. D. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1413185112 · Cited by 159 · see citing works
Analysis of Binding Site Hot Spots on the Surface of Ras GTPase
Buhrman, G., O′Connor, C., Zerbe, B. S., Kearney, B. M., Napoleon, R. L., Kovrigina, E. A., Vajda, S., Kozakov, D., Kovrigin, E. L., & Mattos, C. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.09.011 · Cited by 158 · 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
H-Ras forms dimers on membrane surfaces via a protein–protein interface
Lin, W., Iversen, L., Tu, H., Rhodes, C., Christensen, S. M., Iwig, J. S., Hansen, S. D., Huang, W. Y. C., & Groves, J. T. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321155111 · Cited by 156 · see citing works
Ras activation by SOS: Allosteric regulation by altered fluctuation dynamics
Iversen, L., Tu, H.-L., Lin, W.-C., Christensen, S. M., Abel, S. M., Iwig, J., Wu, H.-J., Gureasko, J., Rhodes, C., Petit, R. S., et al. (2014) · Science · doi:10.1126/science.1250373 · Cited by 154 · see citing works
Principles of Allosteric Interactions in Cell Signaling
Nussinov, R., Tsai, C.-J., & Liu, J. (2014) · Journal of the American Chemical Society · doi:10.1021/ja510028c · Cited by 154 · see citing works
Self-citationFormation of the Ras Dimer Is Essential for Raf-1 Activation
Inouye, K., Mizutani, S., Koide, H., & Kaziro, Y. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.6.3737 · Cited by 154 · see citing works
Tanaka, T. U., Williams, R. L., & Rabbitts, T. H. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601744 · Cited by 151 · see citing works
Inhibition of Ras Signaling by Blocking Ras–Effector Interactions with Cyclic Peptides
Upadhyaya, P., Qian, Z., Selner, N. G., Clippinger, S. R., Wu, Z., Briesewitz, R., & Pei, D. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201502763 · Cited by 149 · see citing works
Spoerner, M., Hozsa, C., Poetzl, J. A., Reiss, K., Ganser, P., Geyer, M., & Kalbitzer, H. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.145235 · Cited by 148 · see citing works
N-Ras Forms Dimers at POPC Membranes
Güldenhaupt, J., Rudack, T., Bachler, P. S., Mann, D., Triola, G., Waldmann, H., Kötting, C., & Gerwert, K. B. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.08.043 · Cited by 148 · see citing works
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 · 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
Self-citationAndrographolide 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 · see citing works
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 · 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
Self-citationPrakash, P., Zhou, Y., Hong, L., Hancock, J. F., & Gorfe, A. A. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2016.01.019 · Cited by 135 · see citing works
Erratum: Drugging the p53 pathway: understanding the route to clinical efficacy
Khoo, K. H., Verma, C. S., & Lane, D. P. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4288 · Cited by 135 · see citing works
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 · see citing works
Ras nanoclusters: Molecular structure and assembly
Abankwa, D., Gorfe, A. A., & Hancock, J. F. (2007) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2007.08.003 · Cited by 130 · see citing works
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 126 · see citing works
Lee, J. H., Zhang, Q., Jo, S., Chai, S. C., Oh, M., Im, W., Lu, H., & Lim, H. (2010) · Journal of the American Chemical Society · doi:10.1021/ja108230s · Cited by 126 · see citing works
Ledford, H. K. (2015) · Nature · doi:10.1038/520278a · Cited by 126 · see citing works
Nguyen, L. T., Tretiakova, M., Silvis, M. R., Lucas, J. M., Klezovitch, O., Coleman, I. M., Bolouri, H., Kutyavin, V. I., Morrissey, C. M., True, L. D., et al. (2015) · Cancer Cell · doi:10.1016/j.ccell.2015.05.005 · Cited by 123 · see citing works
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 · see citing works
Self-citationTargeting 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 121 · see citing works
Antibody-Mediated Delivery of Anti– KRAS -siRNA In Vivo Overcomes Therapy Resistance in Colon Cancer
Bäumer, S., Bäumer, N., Appel, N., Terheyden, L., Fremerey, J., Schelhaas, S., Wardelmann, E., Buchholz, F., Berdel, W. E., & Müller‐Tidow, C. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-2017 · Cited by 119 · see citing works
Thapar, R., Williams, J. G., & Campbell, S. L. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.08.106 · Cited by 119 · see citing works
Trinh, T. B., Upadhyaya, P., Qian, Z., & Pei, D. (2015) · ACS Combinatorial Science · doi:10.1021/acscombsci.5b00164 · Cited by 119 · see citing works
Buhrman, G., Wink, G., & Mattos, C. (2007) · Structure · doi:10.1016/j.str.2007.10.011 · Cited by 116 · see citing works
Taylor, S., Hickman, J. A., & Dive, C. (2000) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/92.1.18 · Cited by 116 · see citing works
Development of siRNA Payloads to Target <i>KRAS</i> -Mutant Cancer
Yuan, T. L., Fellmann, C., Lee, C.-S., Ritchie, C. D., Thapar, V., Lee, L. C., Hsu, D. J., Grace, D., Carver, J. O., Zuber, J., et al. (2014) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0900 · Cited by 113 · see citing works
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 · see citing works
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 110 · see citing works
Self-citationSchmick, M., Kraemer, A., & Bastiaens, P. I. H. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2015.02.004 · Cited by 108 · see citing works
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 · see citing works
Self-citationStabilizing 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 · see citing works
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 · see citing works
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 · see citing works
Self-citationKeskin, Ö., Ma, B., Rogale, K., Gunasekaran, K., & Nussinov, R. (2005) · Physical Biology · doi:10.1088/1478-3975/2/2/s03 · Cited by 99 · see citing works
Self-citationStieglitz, 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 · see citing works
Reddy, M. V. R., Venkatapuram, P., Mallireddigari, M. R., Pallela, V. R., Cosenza, S. C., Robell, K. A., Akula, B., Hoffman, B. S., & Reddy, E. P. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm200570p · Cited by 97 · see citing works
Therapeutic Silencing of KRAS Using Systemically Delivered siRNAs
Pecot, C. V., Wu, S. Y., Bellister, S. A., Filant, J., Rupaimoole, R., Hisamatsu, T., Bhattacharya, R., Maharaj, A., Azam, S. H., Rodriguez‐Aguayo, C., et al. (2014) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-14-0074 · Cited by 96 · see citing works
Regulation of Sos Activity by Intramolecular Interactions
Corbalán‐García, S., Margarit, S. M., Galron, D., Yang, S., & Bar‐Sagi, D. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.2.880 · Cited by 96 · see citing works
A Chemical Perspective on Allostery
Ribeiro, A. A. S. T., & Ortiz, V. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00543 · Cited by 94 · see citing works
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 · see citing works
Self-citationMembrane-associated Ras dimers are isoform-specific: K-Ras dimers differ from H-Ras dimers
Jang, H., Muratcioğlu, S., Gürsoy, A., Keskin, Ö., & Nussinov, R. (2016) · Biochemical Journal · doi:10.1042/bcj20160031 · Cited by 91 · see citing works
Self-citationThe 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 · see citing works
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 · see citing works
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 · see citing works
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 86 · see citing works
Self-citationLu, 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 · see citing works
Self-citationDirect Targeting of Rab‐GTPase–Effector Interactions
Spiegel, J., Cromm, P. M., Itzen, A., Goody, R. S., Grossmann, T. N., & Waldmann, H. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201308568 · Cited by 86 · see citing works
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 85 · see citing works
Waldmann, H., Karaguni, I., Carpintero, M., Gourzoulidou, E., Herrmann, C., Brockmann, C., Oschkinat, H., & Müller, O. (2004) · Angewandte Chemie International Edition · doi:10.1002/anie.200353089 · Cited by 83 · see citing works
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 81 · see citing works
Targeting RAS and PI3K in lung cancer
Downward, J. (2008) · Nature Medicine · doi:10.1038/nm1208-1315 · Cited by 80 · see citing works
Interactions between Ras proteins and their effectors
McCormick, F. P., & Wittinghofer, A. (1996) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(96)80123-6 · Cited by 80 · see citing works
Adaptation to mTOR kinase inhibitors by amplification of eIF4E to maintain cap-dependent translation
Cope, C. L., Gilley, R., Balmanno, K., Sale, M. J., Howarth, K., Hampson, M., Smith, P. D., Guichard, S. M., & Cook, S. J. (2013) · Journal of Cell Science · doi:10.1242/jcs.137588 · Cited by 79 · see citing works
High-affinity interaction of the K-Ras4B hypervariable region with the RAS active site
Chavan, T. S., Jang, H., Khavrutskii, L., Abraham, S. J., Banerjee, A., Freed, B. C., Johannessen, L., Tarasov, S. G., Gaponenko, V., Nussinov, R., et al. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.09.034 · Cited by 79 · see citing works
Self-citationSmall molecule modulators of protein-protein interactions: selected case studies
Aeluri, M., Chamakuri, S., Dasari, B., Guduru, S. K. R., Jimmidi, R., Jogula, S., & Arya, P. (2014) · Chemical Reviews · doi:10.1021/cr4004049 · Cited by 79 · see citing works
Direct Modulation of Small GTPase Activity and Function
Cromm, P. M., Spiegel, J., Grossmann, T. N., & Waldmann, H. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201504357 · Cited by 78 · 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
Self-citationDirect Attack on RAS: Intramolecular Communication and Mutation-Specific Effects
Marcus, K., & Mattos, C. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-2148 · Cited by 75 · see citing works
The higher level of complexity of K‐Ras4B activation at the membrane
Jang, H., Banerjee, A., Chavan, T., Lu, S., Zhang, J., Gaponenko, V., & Nussinov, R. (2015) · The FASEB Journal · doi:10.1096/fj.15-279091 · Cited by 75 · see citing works
Self-citationGlobal Conformational Dynamics in Ras
O’Connor, C., & Kovrigin, E. L. (2008) · Biochemistry · doi:10.1021/bi801076c · Cited by 74 · see citing works
Crystal Structure of M-Ras Reveals a GTP-bound “Off” State Conformation of Ras Family Small GTPases
Ye, M., Shima, F., Muraoka, S., Liao, J., Okamoto, H., Yamamoto, M., Tamura, A., Yagi, N., Ueki, T., & Kataoka, T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505503200 · Cited by 73 · see citing works
Identifying DNA Methylation Biomarkers of Cancer Drug Response
Maier, S., Dahlstroem, C., Haefliger, C., Plum, A., & Piepenbrock, C. (2005) · American Journal of PharmacoGenomics · doi:10.2165/00129785-200505040-00003 · Cited by 72 · see citing works
Inhibitors of Ras–SOS Interactions
Lu, S., Jang, H., Zhang, J., & Nussinov, R. (2016) · ChemMedChem · doi:10.1002/cmdc.201500481 · Cited by 72 · see citing works
Self-citationLópez-Alcalá, C., Alvarez-Moya, B., Villalonga, P., Calvo, M., Bachs, O., & Agell, N. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706238200 · Cited by 71 · see citing works
Mechanisms of Ras membrane organization and signaling: Ras on a rocker
Abankwa, D., Gorfe, A. A., & Hancock, J. F. (2008) · Cell Cycle · doi:10.4161/cc.7.17.6596 · Cited by 70 · see citing works
Oncogenic KRAS signaling and YAP1/β-catenin: Similar cell cycle control in tumor initiation
Nussinov, R., Tsai, C., Jang, H., Korcsmáros, T., & Csermely, P. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.04.001 · Cited by 70 · see citing works
Self-citationInhibition of Ras–effector interactions by cyclic peptides
Wú, X., Upadhyaya, P., Villalona-Calero, M. A., Briesewitz, R., & Pei, D. (2012) · MedChemComm · doi:10.1039/c2md20329d · Cited by 69 · see citing works
Akasaka, K., Tamada, M., Wang, F., Kariya, K.-I., Shima, F., Kikuchi, A., Yamamoto, M., Shirouzu, M., Yokoyama, S., & Kataoka, T. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.10.5353 · Cited by 69 · 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
Self-citationMetal–Bis(2‐picolyl)amine Complexes as State 1(T) Inhibitors of Activated Ras Protein
Rosnizeck, I. C., Spoerner, M., Harsch, T., Kreitner, S., Filchtinski, D., Herrmann, C., Engel, D., König, B., & Kalbitzer, H. R. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201204148 · Cited by 65 · see citing works
“Pathway drug cocktail”: targeting Ras signaling based on structural pathways
Nussinov, R., Tsai, C.-J., & Mattos, C. (2013) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2013.07.009 · Cited by 62 · see citing works
Self-citationThe Hypervariable Region of K-Ras4B Is Responsible for Its Specific Interactions with Calmodulin
Abraham, S. J., Nolet, R., Calvert, R. J., Anderson, L. M., & Gaponenko, V. (2009) · Biochemistry · doi:10.1021/bi900769j · Cited by 61 · see citing works
Li, Z., Janosi, L., & Gorfe, A. A. (2012) · Journal of the American Chemical Society · doi:10.1021/ja307716z · Cited by 61 · see citing works
H-ras Protein in a Bilayer: Interaction and Structure Perturbation
Gorfe, A. A., Babakhani, A., & McCammon, J. A. (2007) · Journal of the American Chemical Society · doi:10.1021/ja073949v · Cited by 61 · see citing works
The Ras–Membrane Interface: Isoform-Specific Differences in the Catalytic Domain
Parker, J. A., & Mattos, C. (2015) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-14-0535 · Cited by 61 · see citing works
Scheffzek, K., Grünewald, P., Wohlgemuth, S., Kabsch, W., Tu, H., Wigler, M., Wittinghofer, A., & Herrmann, C. (2001) · Structure · doi:10.1016/s0969-2126(01)00674-8 · Cited by 60 · see citing works
Spoerner, M., Nuehs, A., Herrmann, C., Steiner, G., & Kalbitzer, H. R. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.05681.x · Cited by 56 · see citing works
Gorfe, A. A. (2009) · Current Medicinal Chemistry · doi:10.2174/092986710789957832 · Cited by 55 · see citing works
Clausen, R., Ma, B., Nussinov, R., & Shehu, A. (2015) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1004470 · Cited by 54 · see citing works
Self-citationArozarena, I., Calvo, F., & Crespo, P. (2011) · Genes & Cancer · doi:10.1177/1947601911409213 · Cited by 52 · see citing works
Chakrabarti, M., Jang, H., & Nussinov, R. (2016) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5b11110 · Cited by 52 · see citing works
Self-citationThe Role of Conserved Waters in Conformational Transitions of Q61H K-ras
Prakash, P., Sayyed–Ahmad, A., & Gorfe, A. A. (2012) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1002394 · Cited by 51 · see citing works
Sayyed–Ahmad, A., Cho, K., Hancock, J. F., & Gorfe, A. A. (2016) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.6b02403 · Cited by 50 · see citing works
Lessons from computer simulations of Ras proteins in solution and in membrane
Prakash, P., & Gorfe, A. A. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.07.024 · Cited by 49 · see citing works
The spatial structure of cell signaling systems
Nussinov, R. (2013) · Physical Biology · doi:10.1088/1478-3975/10/4/045004 · Cited by 49 · see citing works
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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 · see citing works
RAS: Striking at the Core of the Oncogenic Circuitry
Gimple, R. C., & Wang, X. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00965 · Cited by 174 · see citing works
Allosteric Modulator Discovery: From Serendipity to Structure-Based Design
Lu, S., He, X., Ni, D., & Zhang, J. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01749 · Cited by 176 · see citing works
Self-citationLu, S., Shen, Q., & Zhang, J. (2019) · Accounts of Chemical Research · doi:10.1021/acs.accounts.8b00570 · Cited by 166 · see citing works
Self-citationSmall Molecule Allosteric Modulators of G-Protein-Coupled Receptors: Drug–Target Interactions
Lu, S., & Zhang, J. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01844 · Cited by 144 · see citing works
Self-citationChen, J., Zhang, S., Wang, W., Pang, L., Zhang, Q., & Liu, X. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.0c01470 · Cited by 140 · see citing works
Nussinov, R., Jang, H., Tsai, C., & Cheng, F. (2019) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1006658 · Cited by 129 · see citing works
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Liu, J., Wang, Y., & Lin, L. (2018) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2018.09.007 · Cited by 123 · see citing works
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Nussinov, R., Tsai, C., & Jang, H. (2017) · Cancer Research · doi:10.1158/0008-5472.can-17-2727 · Cited by 122 · see citing works
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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
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Guarnera, E., & Berezovsky, I. N. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2020.01.010 · Cited by 117 · see citing works
Ni, D., Lu, S., & Zhang, J. (2019) · Medicinal Research Reviews · doi:10.1002/med.21585 · Cited by 116 · see citing works
Self-citationTherapeutic targeting of RAS: New hope for drugging the “undruggable”
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Self-citationChen, J., Wang, J., Yang, W., Zhao, L., & Hu, G. (2024) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.4c01174 · Cited by 82 · see citing works
Lanfredini, S., Thapa, A., & O’Neill, E. E. (2019) · Biochemical Society Transactions · doi:10.1042/bst20170521 · Cited by 78 · see citing works
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Song, Z., Wang, F., Cui, S., & Qu, X. (2018) · Cancer Investigation · doi:10.1080/07357907.2017.1422512 · Cited by 71 · see citing works
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Self-citationWang, Y., Ji, D., Lei, C., Chen, Y., Qiu, Y., Li, X., Li, M., Ni, D., Pu, J., Zhang, J., et al. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.01.044 · Cited by 64 · see citing works
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Parker, J. A., & Mattos, C. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a031427 · Cited by 60 · see citing works
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Ottaiano, A., Normanno, N., Facchini, S., Cassata, A., Nappi, A. G., Romano, C., Silvestro, L., Stefano, A. D., Rachiglio, A. M., Roma, C., et al. (2020) · Cancers · doi:10.3390/cancers12071919 · Cited by 53 · see citing works
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Lu, S., & Zhang, J. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2016.11.013 · Cited by 53 · see citing works
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Self-citationChen, J., Wang, L., Wang, W., Sun, H., Pang, L., & Bao, H. (2021) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2021.104639 · Cited by 49 · see citing works
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Hossain, M. A. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.176727 · Cited by 47 · see citing works
Vatansever, S., Gumus, Z. H., & Erman, B. (2016) · Scientific Reports · doi:10.1038/srep37012 · Cited by 45 · see citing works
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Cabral, L. G. D. S., Martins, I. M., Paulo, E. P. D. A., Pomini, K. T., Poyet, J., & Maria, D. (2025) · Biomolecules · doi:10.3390/biom15050621 · Cited by 45 · see citing works
Jang, H., Banerjee, A., Chavan, T., Gaponenko, V., & Nussinov, R. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.785063 · Cited by 43 · see citing works
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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
Self-citationYao, Y., Wang, Y., Chen, L., Tian, Z., Yang, G., Wang, R., Wang, C., Wu, Q., Wu, Y., Gao, J., et al. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-00908-0 · Cited by 41 · see citing works
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Ghufran, M., Rehman, A. U., Shah, M., Ayaz, M., Ng, H. L., & Wadood, A. (2019) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2019.1704880 · Cited by 42 · see citing works
Nussinov, R., Tsai, C., & Jang, H. (2018) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2018.01.002 · Cited by 41 · see citing works
Self-citationTian, X., Cai, J., Ma, S., Fang, Y., Huang, H., Lin, T., Rao, H., Li, M., Xia, Z., Kang, T., et al. (2020) · 癌症:英文版 · doi:10.1002/cac2.12039 · Cited by 40 · see citing works
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Xie, C., Li, Y., Li, L.-L., Fan, X.-X., Wang, Y.-W., Wei, C.-L., Liu, L., Leung, E. L.-H., & Yao, X.-J. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00823 · Cited by 40 · see citing works
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Kamgar-Dayhoff, P., & Brelidze, T. I. (2021) · Oncotarget · doi:10.18632/oncotarget.28010 · Cited by 39 · see citing works
Chen, J., Zeng, Q., Wang, W., Hu, Q., & Bao, H. (2022) · RSC Advances · doi:10.1039/d1ra07936k · Cited by 39 · see citing works
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Li, X., Dai, J., Ni, D., He, X., Zhang, H., Zhang, J., Fu, Q., Liu, Y., & Lu, S. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.12.020 · Cited by 38 · see citing works
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Zou, T., Mao, X., Yin, J., Li, X., Chen, J., Zhu, T., Li, Q., Zhou, H., & Liu, Z. (2016) · Clinical Genetics · doi:10.1111/cge.12908 · Cited by 38 · see citing works
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Harrison, R. A., Lu, J., Carrasco, M. A., Hunter, J., Manandhar, A., Gondi, S. R., Westover, K. D., & Engen, J. R. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.10.017 · Cited by 37 · see citing works
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Qiu, Y., Wang, Y., Chai, Z., Ni, D., Li, X., Pu, J., Chen, J., Zhang, J., Lu, S., Lv, C., et al. (2021) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.02.014 · Cited by 37 · see citing works
Self-citationSpratford, C. M., Goins, L. M., Chi, F., Girard, J. R., Macias, S. N., Ho, V. W., & Banerjee, U. K. (2021) · Development · doi:10.1242/dev.200216 · Cited by 34 · see citing works
Zhang, H., Ni, D., Fan, J., Li, M.-Y., Zhang, J., Chen, H., Nussinov, R., & Lu, S. (2022) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.2c00591 · Cited by 36 · see citing works
Self-citationLi, W., Wang, Y., Tan, S., Rao, Q., Zhu, T., Huang, G. C., Li, Z. Y., & Liu, G. (2018) · Medical Science Monitor · doi:10.12659/msm.911640 · Cited by 35 · see citing works
Xu, X., Chen, Y., Fu, Q., Ni, D., Zhang, J., Li, X., & Lu, S. (2019) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2018.1553167 · Cited by 35 · see citing works
Self-citationChen, J., Wang, J., Yang, W., Zhao, L., Zhao, J., & Hu, G. (2024) · Molecules · doi:10.3390/molecules29102317 · Cited by 34 · see citing works
Castro, M. A., Rodenak‐Kladniew, B., Massone, A. R., Polo, M. P., de Bravo, M. M. G., & Crespo, R. (2018) · Food & Function · doi:10.1039/c7fo01912b · Cited by 34 · see citing works
Chen, K., Shang, Z., Dai, A.-L., & Dai, P.-L. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.117816 · Cited by 33 · see citing works
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Maloney, R., Zhang, M., Liu, Y., Jang, H., & Nussinov, R. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04296-0 · Cited by 33 · see citing works
Self-citationNussinov, R. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169044 · Cited by 33 · see citing works
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Liao, T.-J., Tsai, C., Jang, H., Fushman, D., & Nussinov, R. (2016) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.09.001 · Cited by 31 · see citing works
Self-citationNi, D., Song, K., Zhang, J., & Lu, S. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18112249 · Cited by 30 · see citing works
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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
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Muratcioğlu, S., Jang, H., Gürsoy, A., Keskin, Ö., & Nussinov, R. (2017) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.7b03035 · Cited by 30 · see citing works
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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
Self-citationNi, D., Liu, D., Zhang, J., & Lu, S. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19010151 · Cited by 26 · see citing works
Self-citationJilly, R., Khan, N. Z., Aronsson, H., & Schneider, D. (2018) · Frontiers in Plant Science · doi:10.3389/fpls.2018.00206 · Cited by 26 · see citing works
Gong, R., Chen, M., Huang, C., Wong, H. L. X., Kwan, H. Y., & Bian, Z. (2022) · Cell Communication and Signaling · doi:10.1186/s12964-022-00834-2 · Cited by 26 · see citing works
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Nussinov, R., Tsai, C., & Jang, H. (2018) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2018.02.009 · Cited by 25 · see citing works
Self-citationLi, H., Qi, W.-L., Wang, Y., & Meng, L. (2021) · Genes & Diseases · doi:10.1016/j.gendis.2021.08.011 · Cited by 25 · see citing works
Pan-RAS inhibitors: Hitting multiple RAS isozymes with one stone
Coley, A. B., Ward, A., Keeton, A. B., Chen, X., Maxuitenko, Y. Y., Prakash, A., Li, F., Foote, J. B., Buchsbaum, D. J., & Piazza, G. A. (2022) · Advances in cancer research · doi:10.1016/bs.acr.2021.07.009 · Cited by 25 · see citing works
Gogate, A., Belcourt, J., Shah, M., Wang, A., Frankel, A., Kolmel, H., Chalon, M., Stephen, P., Kolli, A., Tawfik, S. M., et al. (2023) · Pharmacological Reviews · doi:10.1124/pharmrev.123.000815 · Cited by 25 · see citing works
Efficient iron utilization compensates for loss of extracellular matrix of ovarian cancer spheroids
Wang, Q., Gu, T., Ma, L., Bu, S., Zhou, W., Mao, G., Wang, L., Guo, Y., & Lai, D. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.01.001 · Cited by 23 · see citing works
Chen, Y., Chen, J., Lin, Y., Xu, L., Liu, J., Xu, Y., Yang, H., Liang, H., & Tang, H. (2016) · Toxicology Letters · doi:10.1016/j.toxlet.2016.08.006 · Cited by 23 · see citing works
Wang, L., Zheng, G., Liu, X., Ni, D., He, X., Cheng, J., & Lu, S. (2018) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2018.1496139 · Cited by 23 · see citing works
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Li, Y., Yin, Y., He, Y., He, K., & Li, J. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.11.015 · Cited by 21 · see citing works
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Berta, D., Gehrke, S., Nyíri, K., Vértessy, B. G., & Rosta, E. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c04330 · Cited by 21 · see citing works
Recent advances in the biology and therapy of medullary thyroid carcinoma
Nelkin, B. D. (2017) · F1000Research · doi:10.12688/f1000research.12645.1 · Cited by 21 · see citing works
Qi, F., Qin, W., Zhang, Y., Luo, Y., Niu, B., An, Q., Yang, B., Shi, K., Yu, Z., Chen, J., et al. (2021) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-021-02085-4 · Cited by 20 · see citing works
Xiong, Y., Zeng, J., Xia, F., Cui, Q., Deng, X., & Xu, X. (2022) · Journal of Computational Chemistry · doi:10.1002/jcc.26846 · Cited by 20 · see citing works
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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
Self-citationPDRG1 promotes the proliferation and migration of GBM cells by the MEK/ERK/CD44 pathway
Sun, J., Xu, Y., Liu, J., Cui, H., Cao, H., & Ren, J. (2021) · Cancer Science · doi:10.1111/cas.15214 · Cited by 19 · see citing works
Bao, H., Wang, W., Sun, H. B., & Chen, J. Z. (2023) · SAR and QSAR in environmental research · doi:10.1080/1062936x.2023.2165542 · Cited by 19 · see citing works
Endogenous IQGAP1 and IQGAP3 do not functionally interact with Ras
Morgan, C. J., Hedman, A. C., Li, Z., & Sacks, D. B. (2019) · Scientific Reports · doi:10.1038/s41598-019-46677-9 · Cited by 19 · see citing works
Development of a Nucleotide Exchange Inhibitor That Impairs Ras Oncogenic Signaling
Marín‐Ramos, N. I., Piñar, C., Vázquez‐Villa, H., Martín‐Fontecha, M., González, Á., Canales, Á., Algar, S., Mayo, P. P., Jiménez‐Barbero, J., Gajate, C., et al. (2016) · Chemistry - A European Journal · doi:10.1002/chem.201604905 · Cited by 19 · see citing works
Qi, W.-L., Li, H.-Y., Wang, Y., Xu, L., Deng, J.-T., Zhang, X., Wang, Y.-X., & Meng, L.-H. (2023) · Acta Pharmacologica Sinica · doi:10.1038/s41401-022-01015-0 · Cited by 19 · see citing works
Xie, F., Zhao, Y. F., Wang, S., Ma, J., Wang, X., & Qian, L. (2018) · Journal of Cellular Biochemistry · doi:10.1002/jcb.27614 · Cited by 18 · see citing works
The Hypervariable Region of K-Ras4B Governs Molecular Recognition and Function
Abdelkarim, H., Banerjee, A., Grudzien, P. K., Leschinsky, N., Abushaer, M., & Gaponenko, V. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20225718 · Cited by 18 · see citing works
Tebar, F., Chavero, A., Agell, N., Lu, A., Rentero, C., Enrich, C., & Grewal, T. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21103680 · Cited by 18 · see citing works
A feedforward circuit shaped by ECT2 and USP7 contributes to breast carcinogenesis
Zhang, Q., Cao, C., Gong, W., Bao, K., Wang, Q., Wang, Y., Bi, L., Ma, S., Zhao, J., Liu, L., et al. (2020) · Theranostics · doi:10.7150/thno.46878 · Cited by 18 · see citing works
Yu, Z., Su, H., Chen, J., & Hu, G. (2022) · Molecules · doi:10.3390/molecules27175596 · Cited by 16 · see citing works
Mou, L., Cui, T., Liu, W., Zhang, H., Cai, Z., Lu, S., & Gao, G. (2016) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12895 · Cited by 16 · see citing works
Self-citationZhang, H., He, X., Ni, D., Mou, L., Chen, X., & Lu, S. (2019) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2019.1567390 · Cited by 16 · see citing works
Self-citation
- Authors
- Lu, S., Jang, H., Gu, S., Zhang, J., & Nussinov, R.
- Affiliations
- Shanghai Jiao Tong University (CN)
- Frederick National Laboratory for Cancer Research (US)
- Tel Aviv University (IL)
- Corresponding author
- Zhang, Jian
- Nussinov, Ruth
- Venue
- Chemical Society Reviews
- Publisher
- Royal Society of Chemistry (RSC)
- Published
- 2016
- Volume
- 45
- Issue
- 18
- Pages
- 4929-4952
- ISSN
- 0306-0012 (ISSN-L)
- 1460-4744
- PMC
- PMC5021603
- OpenAlex
- W2464027273
- Cited by
- 188
- References
- 243
- Citations by year
- 2026: 13 · 2025: 14 · 2024: 14 · 2023: 18 · 2022: 22 · 2021: 26 · 2020: 12 · 2019: 24 · 2018: 18 · 2017: 17 · 2016: 10
- FWCI
- 2.08
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Chemical Society Reviews (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (HHSN261200800001C)
- National Cancer Institute (Z01BC010440, HHSN261200800001E))
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- Ras GTPase, RAS inhibitors, RAS mutations, drug resistance, allosteric site, YAP, c-Myc, MAPK/ERK pathway, PI3K/AKT/mTOR pathway, cell cycle regulation, RAS-driven cancers
- MeSH terms
- Allosteric Regulation, Antineoplastic Agents, Humans, Mutation, Neoplasms, ras Proteins, Drug Resistance, Neoplasm, Phosphatidylinositol 3-Kinases, Catalytic Domain, RNA, Small Interfering, Molecular Targeted Therapy
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