A Comprehensive Survey of Ras Mutations in Cancer
Open accessAbstract
All mammalian cells express 3 closely related Ras proteins, termed H-Ras, K-Ras, and N-Ras, that promote oncogenesis when they are mutationally activated at codon 12, 13, or 61. Although there is a high degree of similarity among the isoforms, K-Ras mutations are far more frequently observed in cancer, and each isoform displays preferential coupling to particular cancer types. We examined the mutational spectra of Ras isoforms curated from large-scale tumor profiling and found that each isoform exhibits surprisingly distinctive codon mutation and amino-acid substitution biases. These findings were unexpected given that these mutations occur in regions that share 100% amino-acid sequence identity among the 3 isoforms. Of importance, many of these mutational biases were not due to differences in exposure to mutagens, because the patterns were still evident when compared within specific cancer types. We discuss potential genetic and epigenetic mechanisms, as well as isoform-specific differences in protein structure and signaling, that may promote these distinct mutation patterns and differential coupling to specific cancers. Cancer Res; 72(10); 2457–67. ©2012 AACR.
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Approximately 90% of PDAC cases harbor a KRAS mutation.
“Approximately 90% of PDAC cases harbor a Kirsten rat sarcoma (KRAS) mutation (Prior et al., 2012).”
From The antitumoral effect of statins in pancreatic ductal adenocarcinoma: a scoping review (2026) · cites this paper as Prior et al., 2012
In “Ras mutation frequencies > Large-scale tumour profiling” (page unavailable), the paper says early, small-sample analyses reported KRAS mutations in 90% of pancreatic tumours. It then explicitly states that its larger-scale pancreas mutation rate is 60%, rather than the generally quoted 90%, contrary to the unqualified claim. (LLM, conf=0.87)
Checked by a reasoning model — may be wrong.
Experimental — accuracy not yet measuredKRAS G12C mutation is present in approximately 3% of colorectal cancer cases.
“This specific mutation, present in ~3% of CRC cases, 2 is associated with significantly reduced progression-free survival (PFS) and overall survival (OS) compared to KRAS wildtype tumors.[3][4][5]”
KRAS mutations, especially KRASG12C and KRASG12V, are strongly associated with smoking.
“Unlike other clinically actionable genomic alterations found in NSCLCs (such as EGFR and ALK aberrations), KRAS mutations, particularly KRASG12C and KRASG12V, are strongly associated with smoking29–31.”
From The current state of the art and future trends in RAS-targeted cancer therapies (2022) · cites this paper as [29]
RAS mutations and the deregulated signaling they cause account for one third of all human cancers.
“However, RAS mutations and the resulting deregulated signaling events are responsible for one third of all human cancers4 (Figure 1).”
From The metabolic landscape of RAS-driven cancers from biology to therapy (2021) · cites this paper as [4]
KRAS is mutated in many cancers, predominantly adenocarcinomas, while NRAS mutations are prominent in melanoma and myeloid cancer.
“Overall, KRAS is mutated in many cancers (predominantly adenocarcinomas), whereas NRAS mutations are prominent in melanoma and myeloid cancer4,15,16 (Fig. 1).”
From The metabolic landscape of RAS-driven cancers from biology to therapy (2021) · cites this paper as [4]
The basis of specific G12X mutation frequencies has remained unclear, except for the G12C transversion mutation associated with smoking in lung cancer.
“The basis of the specific G12X mutation frequencies has remained unclear, except for the G12C transversion mutation (c.34G>T) associated with smoking in lung cancer [6,7].”
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Cites
ras oncogenes in human cancer: a review.
Bos, J. L. (1989) · PubMed · Cited by 5,061 · 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
The Guanine Nucleotide-Binding Switch in Three Dimensions
Vetter, I. R., & Wittinghofer, A. (2001) · Science · doi:10.1126/science.1062023 · Cited by 1,875 · see citing works
Denissenko, M. F., Pao, A., Tang, M.-S., & Pfeifer, G. P. (1996) · Science · doi:10.1126/science.274.5286.430 · Cited by 1,650 · see citing works
Tobacco carcinogens, their biomarkers and tobacco-induced cancer
Hecht, S. S. (2003) · Nature reviews. Cancer · doi:10.1038/nrc1190 · Cited by 1,551 · 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
Zarbl, H., Sukumar, S. V., Arthur, A. V., Martı́n-Zanca, D., & Barbacid, M. (1985) · Nature · doi:10.1038/315382a0 · Cited by 806 · see citing works
The RASopathies: developmental syndromes of Ras/MAPK pathway dysregulation
Tidyman, W. E., & Rauen, K. A. (2009) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2009.04.001 · Cited by 780 · see citing works
Endomembrane Trafficking of Ras
Choy, E., Chiu, V. K., Silletti, J., Feoktistov, M., Morimoto, T., Michaelson, D., Ivanov, I. E., & Philips, M. R. (1999) · Cell · doi:10.1016/s0092-8674(00)80607-8 · Cited by 754 · see citing works
De Roock, W., Jonker, D. J., Di Nicolantonio, F., Sartore-Bianchi, A., Tu, D., Siena, S., Lamba, S., Arena, S., Frattini, M., Piessevaux, H., et al. (2010) · JAMA · doi:10.1001/jama.2010.1535 · Cited by 748 · see citing works
Direct visualization of Ras proteins in spatially distinct cell surface microdomains
Prior, I. A., Muncke, C., Parton, R. G., & Hancock, J. F. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200209091 · Cited by 735 · see citing works
Self-citationRas 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
Cloning of bovine GAP and its interaction with oncogenic ras p21
Vogel, U. S., Dixon, R. A. F., Schaber, M. D., Diehl, R. E., Marshall, M. S., Scolnick, E. M., Sigal, I. S., & Gibbs, W. W. (1988) · Nature · doi:10.1038/335090a0 · Cited by 649 · see citing works
Haigis, K. M., Kendall, K. R., Wang, Y., Cheung, A., Haigis, M. C., Glickman, J. N., Niwa-Kawakita, M., Sweet-Cordero, A., Sebolt-Leopold, J., Shannon, K. M., et al. (2008) · Nature Genetics · doi:10.1038/ng.115 · Cited by 610 · see citing works
Biological properties of human c-Ha-ras1 genes mutated at codon 12
Seeburg, P. H., Colby, W. W., Capon, D. J., Goeddel, D. V., & Levinson, A. D. (1984) · Nature · doi:10.1038/312071a0 · Cited by 567 · see citing works
Biological and biochemical properties of human rasH genes mutated at codon 61
Der, C. J., Finkel, T., & Cooper, G. M. (1986) · Cell · doi:10.1016/0092-8674(86)90495-2 · Cited by 547 · see citing works
Thyroid Cancer Epidemiology and Prognostic Variables
Sipos, J. A., & Mazzaferri, E. L. (2010) · Clinical Oncology · doi:10.1016/j.clon.2010.05.004 · Cited by 514 · see citing works
Ras Isoforms Vary in Their Ability to Activate Raf-1 and Phosphoinositide 3-Kinase
Yan, J., Roy, S., Apolloni, A., Lane, A., & Hancock, J. F. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.37.24052 · Cited by 477 · see citing works
Bivona, T. G., Quatela, S. E., Bodemann, B. O., Ahearn, I. M., Soskis, M. J., Mor, A., Miura, J., Wiener, H. H., Wright, L. P., Saba, S. G., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.012 · Cited by 467 · see citing works
The Palmitoylation Machinery Is a Spatially Organizing System for Peripheral Membrane Proteins
Rocks, O., Gerauer, M., Vartak, N., Koch, S., Huang, Z., Pechlivanis, M., Kuhlmann, J., Brunsveld, L., Chandra, A., Ellinger, B., et al. (2010) · Cell · doi:10.1016/j.cell.2010.04.007 · Cited by 454 · see citing works
H-ras but Not K-ras Traffics to the Plasma Membrane through the Exocytic Pathway
Apolloni, A., Prior, I. A., Lindsay, M. R., Parton, R. G., & Hancock, J. F. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.7.2475-2487.2000 · Cited by 416 · see citing works
Self-citationCOMPARTMENTALIZED RAS/MAPK SIGNALING
Mor, A., & Philips, M. R. (2006) · Annual Review of Immunology · doi:10.1146/annurev.immunol.24.021605.090723 · Cited by 400 · see citing works
K-Ras is essential for the development of the mouse embryo
Koera, K., Nakamura, K. D., Nakao, K., Miyoshi, J., Toyoshima, K., Hatta, T., Otani, H., Aiba, A., & Katsuki, M. (1997) · Oncogene · doi:10.1038/sj.onc.1201284 · Cited by 355 · see citing works
Esteban, L. M., Vicario‐Abejón, C., Fernández‐Salguero, P. M., Fernández‐Medarde, A., Swaminathan, N., Yienger, K., Lopez, E., Malumbres, M., McKay, R. D. G., Ward, J. M., et al. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.5.1444-1452.2001 · Cited by 298 · see citing works
Voice, J. K., Klemke, R. L., Le, A., & Jackson, J. H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.24.17164 · Cited by 288 · see citing works
Le Calvez, F., Mukeria, A., Hunt, J. D., Kelm, O., Hung, R. J., Tanière, P., Brennan, P., Boffetta, P., Zaridze, D. G., & Hainaut, P. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-0551 · Cited by 273 · 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
Self-citationPurification of ras GTPase activating protein from bovine brain.
Gibbs, W. W., Schaber, M. D., Allard, W. J., Sigal, I. S., & Scolnick, E. M. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.14.5026 · Cited by 245 · see citing works
ras oncogenes: their role in neoplasia
Barbacid, M. (1990) · European Journal of Clinical Investigation · doi:10.1111/j.1365-2362.1990.tb01848.x · Cited by 242 · see citing works
The murine N-ras gene is not essential for growth and development.
Umanoff, H., Edelmann, W., Pellicer, À., & Kucherlapati, R. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.5.1709 · Cited by 234 · see citing works
Differential modification of Ras proteins by ubiquitination.
Jura, N., Scotto–Lavino, E., Sobczyk, A., & Bar-Sagi, D. (2006) · Molecules and Cells · doi:10.1016/j.molcel.2006.02.011 · Cited by 219 · see citing works
Mapping the Nucleotide and Isoform-Dependent Structural and Dynamical Features of Ras Proteins
Gorfe, A. A., Grant, B. J., & McCammon, J. A. (2008) · Structure · doi:10.1016/j.str.2008.03.009 · Cited by 216 · see citing works
Frequency and Spectrum of Mutations at Codons 12 and 13 of the C-K-ras Gene in Human Tumors
Capellá, G., Cronauer-Mitra, S., Pienado, M. A., & Perucho, M. (1991) · Environmental Health Perspectives · doi:10.1289/ehp.9193125 · Cited by 214 · see citing works
Ras-catalyzed hydrolysis of GTP: a new perspective from model studies.
Maegley, K. A., Admiraal, S. J., & Herschlag, D. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.16.8160 · Cited by 211 · 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
O'Byrne, K. J., Gatzemeier, U., Bondarenko, I., Barrios, C. H., Eschbach, C., Martens, U. M., Hotko, Y., Kortsik, C., Paz-Ares, L. G., Pereira, J. R., et al. (2011) · The Lancet Oncology · doi:10.1016/s1470-2045(11)70189-9 · Cited by 205 · see citing works
Differential Activation of the Rac Pathway by Ha-Ras and K-Ras
Walsh, A. B., & Bar‐Sagi, D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010573200 · Cited by 173 · see citing works
Denissenko, M. F., Pao, A., Pfeifer, G. P., & Tang, M. (1998) · Oncogene · doi:10.1038/sj.onc.1201647 · Cited by 166 · see citing works
C-Ki-ras mutations in chronic ulcerative colitis and sporadic colon carcinoma
Burmer, G. C., Levine, D. S., Kulander, B. G., Haggitt, R. C., Rubin, C. E., & Rabinovitch, P. S. (1990) · Gastroenterology · doi:10.1016/0016-5085(90)91024-z · Cited by 147 · see citing works
H-Ras Signaling and K-Ras Signaling Are Differentially Dependent on Endocytosis
Roy, S., Wyse, B. D., & Hancock, J. F. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.14.5128-5140.2002 · Cited by 134 · see citing works
Factors that influence the mutagenic patterns of DNA adducts from chemical carcinogens
Seo, K.-Y., Jelinsky, S. A., & Loechler, E. L. (2000) · Mutation Research/Reviews in Mutation Research · doi:10.1016/s1383-5742(00)00047-8 · Cited by 126 · see citing works
Potenza, N., Vecchione, C., Notte, A., Rienzo, A. D., Rosica, A., Bauer, L., Affuso, A., Felice, M. D., Russo, T., Poulet, R., et al. (2005) · EMBO Reports · doi:10.1038/sj.embor.7400397 · Cited by 126 · see citing works
Ras acylation, compartmentalization and signaling nanoclusters (Review)
Henis, Y. I., Hancock, J. F., & Prior, I. A. (2009) · Molecular Membrane Biology · doi:10.1080/09687680802649582 · Cited by 124 · see citing works
Self-citationRas proteins: paradigms for compartmentalised and isoform-specific signalling
Omerović, J., Laude, A., & Prior, I. A. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7133-8 · Cited by 124 · see citing works
Self-citationSpatio-temporal segregation of Ras signals: one ship, three anchors, many harbors
Rocks, O., Lorentzen, A., & Bastiaens, P. I. H. (2006) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2006.06.007 · Cited by 123 · see citing works
Preferential DNA Damage and Poor Repair Determine ras Gene Mutational Hotspot in Human Cancer
Feng, Z. (2002) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/94.20.1527 · 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
Self-citationC-terminal Truncation of p21H Preserves Crucial Kinetic and Structural Properties
John, J., Schlichting, I., SCHILTZ, E., ROSCH, P. J., & Wittinghofer, A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)51599-4 · Cited by 111 · see citing works
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 · see citing works
Quinlan, M. P., Quatela, S. E., Philips, M. R., & Settleman, J. E. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01661-07 · Cited by 95 · see citing works
Franken, S. M., Scheidig, A. J., Krengel, U., Rensland, H., Lautwein, A., Geyer, M., Scheffzek, K., Goody, R. S., & Kalbitzer, H. R. (1993) · Biochemistry · doi:10.1021/bi00084a005 · Cited by 91 · 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
Self-citationPorta, M. S., Crous‐Bou, M., Wark, P. A., Vineis, P., Real, F. X., Malats, N., & Kampman, E. (2009) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2009.07.003 · Cited by 83 · see citing works
Ahmadian, M. R., Wiesmüller, L., Lautwein, A., Bischoff, F. R., & Wittinghofer, A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.27.16409 · Cited by 80 · 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
Törmänen, V., & Pfeifer, G. P. (1992) · PubMed · Cited by 70 · see citing works
Hu, W., Feng, Z., & Tang, M. (2003) · Biochemistry · doi:10.1021/bi034631s · Cited by 63 · see citing works
Fluoride complexes of oncogenic Ras mutants to study the Ras-RasGAP interaction
Gremer, L., Gilsbach, B. K., Ahmadian, M. R., & Wittinghofer, A. (2008) · Biological Chemistry · doi:10.1515/bc.2008.132 · Cited by 56 · see citing works
Studies on the structure and mechanism of H-ras p21
Goody, R. S., PAI, E. F., Schlichting, I., Rensland, H., Scheidig, A. J., Franken, S. M., & Wittinghofer, A. (1992) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.1992.0037 · Cited by 39 · see citing works
Keller, J. W., Franklin, J. L., Graves‐Deal, R., Friedman, D. B., Whitwell, C. W., & Coffey, R. J. (2006) · Journal of Cellular Physiology · doi:10.1002/jcp.20898 · Cited by 36 · see citing works
Hypermutable bases in the p53 cancer gene are at vulnerable positions in DNA secondary structures.
Wright, B. E., Reimers, J. M., Schmidt, K. H., & Reschke, D. K. (2002) · PubMed · Cited by 35 · see citing works
Mutations and Expression of the ras Family Genes in Leukemias
Gougopoulou, D. M., Kiaris, H., Ergazaki, M., Anagnostopoulos, N. I., Grigoraki, V., & Spandidos, D. A. (1996) · Stem Cells · doi:10.1002/stem.140725 · Cited by 31 · see citing works
In silico p53 mutation hotspots in lung cancer
Lewis, P. D. (2004) · Carcinogenesis · doi:10.1093/carcin/bgh068 · Cited by 30 · see citing works
Self-citationQuinlan, M. P., & Settleman, J. E. (2008) · Cell Cycle · doi:10.4161/cc.7.10.5927 · Cited by 28 · see citing works
Kreeger, P. K., Wang, Y., Haigis, K. M., & Lauffenburger, D. A. (2010) · Integrative Biology · doi:10.1039/b925935j · Cited by 16 · see citing works
Flagged first, then by citations
1 of the 67 references couldn’t be matched to a known paper.
Cited by
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Cystine transporter SLC7A11/xCT in cancer: ferroptosis, nutrient dependency, and cancer therapy
Koppula, P., Zhuang, L., & Gan, B. (2020) · Protein & Cell · doi:10.1007/s13238-020-00789-5 · Cited by 2,546 · see citing works
Targeting Ferroptosis as a Vulnerability in Cancer
Lei, G., Zhuang, L., & Gan, B. (2022) · Nature reviews. Cancer · doi:10.1038/s41568-022-00459-0 · Cited by 2,252 · 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
Pereira, B., Chin, S., Rueda, O. M., Vollan, H. K. M., Provenzano, E., Bardwell, H. A., Pugh, M., Jones, L. R., Russell, R., Sammut, S., et al. (2016) · Nature Communications · doi:10.1038/ncomms11479 · Cited by 1,712 · see citing works
The Frequency of Ras Mutations in Cancer
Prior, I. A., Hood, F. E., & Hartley, J. L. (2020) · Cancer Research · doi:10.1158/0008-5472.can-19-3682 · Cited by 1,130 · see citing works
Self-citationKRAS Mutation: From Undruggable to Druggable in Cancer
Huang, L., Guo, Z., Wang, F., & Fu, L. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00780-4 · Cited by 1,127 · 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
KRAS: The Critical Driver and Therapeutic Target for Pancreatic Cancer
Waters, A. M., & Der, C. J. (2018) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a031435 · Cited by 875 · 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
Biochemical and Structural Analysis of Common Cancer-Associated KRAS Mutations
Hunter, J. C., Manandhar, A., Carrasco, M. A., Gurbani, D., Gondi, S., & Westover, K. D. (2015) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-15-0203 · Cited by 786 · see citing works
Identification of MRTX1133, a Noncovalent, Potent, and Selective KRAS <sup>G12D</sup> Inhibitor
Wang, X., Allen, S., Blake, J. F., Bowcut, V., Briere, D. M., Calinisan, A., Dahlke, J. R., Fell, J. B., Fischer, J. P., Gunn, R. J., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01688 · Cited by 769 · see citing works
Lanman, B. A., Allen, J. R., Allen, J. G., Amegadzie, A. K., Ashton, K. S., Booker, S. K., Chen, J. J., Chen, N., Frohn, M. J., Goodman, G., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01180 · Cited by 765 · see citing works
Relationships among smoking, oxidative stress, inflammation, macromolecular damage, and cancer
Caliri, A. W., Tommasi, S., & Nia, A. B. (2021) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2021.108365 · Cited by 689 · see citing works
Direct small-molecule inhibitors of KRAS: from structural insights to mechanism-based design
Ostrem, J. M. L., & Shokat, K. M. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.139 · Cited by 641 · see citing works
Protein degraders enter the clinic — a new approach to cancer therapy
Chirnomas, D., Hornberger, K. R., & Crews, C. M. (2023) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-023-00736-3 · Cited by 658 · see citing works
The current state of the art and future trends in RAS-targeted cancer therapies
Punekar, S. R., Velcheti, V., Neel, B. G., & Wong, K.-K. (2022) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-022-00671-9 · Cited by 549 · see citing works
G-quadruplexes: a promising target for cancer therapy
Kosiol, N., Juranek, S., Brossart, P., Heine, A., & Paeschke, K. (2021) · Molecular Cancer · doi:10.1186/s12943-021-01328-4 · Cited by 540 · see citing works
Genetics and biology of pancreatic ductal adenocarcinoma
Ying, H., Dey, P., Yao, W., Kimmelman, A. C., Draetta, G. F., Maitra, A., & DePinho, R. A. (2016) · Genes & Development · doi:10.1101/gad.275776.115 · Cited by 527 · see citing works
Evaluation of the use of therapeutic peptides for cancer treatment
Marqus, S., Pirogova, E., & Piva, T. J. (2017) · Journal of Biomedical Science · doi:10.1186/s12929-017-0328-x · Cited by 514 · see citing works
The MAPK and AMPK signalings: interplay and implication in targeted cancer therapy
Yuan, J., Dong, X., Yap, J., & Hu, J. (2020) · Journal of Hematology & Oncology · doi:10.1186/s13045-020-00949-4 · Cited by 500 · see citing works
YAP/TAZ Signaling and Resistance to Cancer Therapy
Nguyen, C. D. K., & Yi, C. (2019) · Trends in Cancer · doi:10.1016/j.trecan.2019.02.010 · Cited by 437 · see citing works
Drugging an undruggable pocket on KRAS
Kessler, D., Gmachl, M., Mantoulidis, A., Martin, L. J., Zoephel, A., Mayer, M., Gollner, A., Covini, D., Fischer, S., Gerstberger, T., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1904529116 · Cited by 449 · see citing works
MYC Deregulation in Primary Human Cancers
Kalkat, M., Melo, J. D., Hickman, K. A., Lourenco, C., Redel, C., Resetca, D., Tamachi, A., Tu, W. B., & Penn, L. Z. (2017) · Genes · doi:10.3390/genes8060151 · Cited by 445 · see citing works
Targeted Degradation of Oncogenic KRAS <sup>G12C</sup> by VHL-Recruiting PROTACs
Bond, M. J., Chu, L., Nalawansha, D. A., Li, K., & Crews, C. M. (2020) · ACS Central Science · doi:10.1021/acscentsci.0c00411 · Cited by 450 · see citing works
Therapeutic developments in pancreatic cancer
Hu, Z., & O'Reilly, E. M. (2023) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-023-00840-w · Cited by 425 · see citing works
The clinical development of MEK inhibitors
Zhao, Y., & Adjei, A. A. (2014) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2014.83 · Cited by 403 · see citing works
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 · see citing works
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 395 · see citing works
Four Key Steps Control Glycolytic Flux in Mammalian Cells
Tanner, L. B., Goglia, A. G., Wei, M. H., Sehgal, T., Parsons, L. R., Park, J. O., White, E., Toettcher, J. E., & Rabinowitz, J. D. (2018) · Cell Systems · doi:10.1016/j.cels.2018.06.003 · Cited by 368 · see citing works
Wang, S., Zheng, Y., Yang, F., Zhu, L., Zhu, X.-Q., Wang, Z.-F., Wu, X.-L., Zhou, C.-H., Yan, J.-Y., Hu, B.-Y., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00659-4 · Cited by 369 · see citing works
Targeting the untargetable KRAS in cancer therapy
Liu, P., Wang, Y., & Li, X. (2019) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2019.03.002 · Cited by 366 · see citing works
Advancements in nanoparticle-based treatment approaches for skin cancer therapy
Zeng, L., Gowda, B. H. J., Ahmed, M. G., Abourehab, M. A. S., Chen, Z., Zhang, C., Li, J., & Kesharwani, P. (2023) · Molecular Cancer · doi:10.1186/s12943-022-01708-4 · Cited by 368 · 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
Targeting 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
The metabolic landscape of RAS-driven cancers from biology to therapy
Mukhopadhyay, S., Vander Heiden, M. G., & McCormick, F. (2021) · Nature Cancer · doi:10.1038/s43018-021-00184-x · Cited by 315 · see citing works
Ferroptosis in health and disease
Berndt, C., Alborzinia, H., Skafar, V., Ayton, S., Barayeu, U., Bartelt, A., Bayır, H., Bebber, C. M., Birsoy, K., Böttcher, J. P., et al. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103211 · Cited by 353 · see citing works
Targeting KRAS in non-small-cell lung cancer: recent progress and new approaches
Reck, M., Carbone, D. P., Garassino, M., & Barlesi, F. (2021) · Annals of Oncology · doi:10.1016/j.annonc.2021.06.001 · Cited by 326 · see citing works
Jänne, P. A., van den Heuvel, M. M., Barlesi, F., Cobo, M., Mazieres, J., Crinò, L., Orlov, S., Blackhall, F., Wolf, J., Garrido, P., et al. (2017) · JAMA · doi:10.1001/jama.2017.3438 · Cited by 335 · see citing works
Molecular epidemiology and diagnostics of KRAS mutations in human cancer
Timar, J., & Kashofer, K. (2020) · Cancer and Metastasis Reviews · doi:10.1007/s10555-020-09915-5 · Cited by 334 · see citing works
The mutational landscapes of genetic and chemical models of Kras-driven lung cancer
Westcott, P. M. K., Halliwill, K. D., To, M. D., Rashid, M., Rust, A. G., Keane, T., Delrosario, R., Jen, K., Gurley, K. E., Kemp, C. J., et al. (2014) · Nature · doi:10.1038/nature13898 · Cited by 333 · see citing works
McCormick, F. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-2662 · Cited by 320 · see citing works
The Hippo pathway in cancer: YAP/TAZ and TEAD as therapeutic targets in cancer
Cunningham, R., & Hansen, C. G. (2022) · Clinical Science · doi:10.1042/cs20201474 · Cited by 331 · see citing works
Biomolecular Condensates and Cancer
Boija, A., Klein, I. A., & Young, R. A. (2021) · Cancer Cell · doi:10.1016/j.ccell.2020.12.003 · Cited by 320 · see citing works
Colchicine-Binding Site Inhibitors from Chemistry to Clinic: A Review
McLoughlin, E. C., & O’Boyle, N. M. (2020) · Pharmaceuticals · doi:10.3390/ph13010008 · Cited by 327 · see citing works
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 · see citing works
Jackson, M., Marks, L., May, G., & Wilson, J. B. (2018) · Essays in Biochemistry · doi:10.1042/ebc20170053 · Cited by 251 · see citing works
Crystal structure of human KRAS G12C covalently bound to a phthalazine inhibitor
Mohr, C. (2019) · Worldwide Protein Data Bank · doi:10.2210/pdb6pgo/pdb · Cited by 313 · see citing works
Chemistries of bifunctional PROTAC degraders
Cao, C., He, M., Wang, L., He, Y., & Rao, Y. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00220e · Cited by 313 · see citing works
Lim, J. K. M., Delaidelli, A., Minaker, S. W., Zhang, H., Čolović, M., Yang, H., Negri, G. L., von Karstedt, S., Lockwood, W. W., Schaffer, P. C., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1821323116 · Cited by 311 · see citing works
KRAS oncogene in non-small cell lung cancer: clinical perspectives on the treatment of an old target
Román, M., Baraibar, I., López, I., Nadal, E., Rolfo, C., Vicent, S., & Gil-Bazo, I. (2018) · Molecular Cancer · doi:10.1186/s12943-018-0789-x · Cited by 301 · see citing works
Adagrasib in Advanced Solid Tumors Harboring a <i>KRAS</i> <sup> <i>G12C</i> </sup> Mutation
Bekaii-Saab, T. S., Yaeger, R., Spira, A. I., Pelster, M. S., Sabari, J. K., Hafez, N., Barve, M., Velastegui, K., Yan, X., Shetty, A., et al. (2023) · Journal of Clinical Oncology · doi:10.1200/jco.23.00434 · Cited by 313 · 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
Lipid-Sorting Specificity Encoded in K-Ras Membrane Anchor Regulates Signal Output
Zhou, Y., Prakash, P., Hong, L., Cho, K., Gorfe, A. A., & Hancock, J. F. (2016) · Cell · doi:10.1016/j.cell.2016.11.059 · Cited by 298 · see citing works
Ultraviolet Photodissociation Mass Spectrometry for Analysis of Biological Molecules
Brodbelt, J. S., Morrison, L. J., & Santos, I. C. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00440 · Cited by 291 · see citing works
Shepherd, F. A., Domerg, C., Hainaut, P. L., Janne, P. A., Pignon, J., Graziano, S. L., Douillard, J.-Y., Brambilla, E., Chevalier, T. L., Seymour, L., et al. (2013) · Journal of Clinical Oncology · doi:10.1200/jco.2012.48.1390 · Cited by 294 · see citing works
Copper bioavailability is a KRAS-specific vulnerability in colorectal cancer
Aubert, L., Nandagopal, N., Steinhart, Z., Lavoie, G., Nourreddine, S., Berman, J. M., Saba-El-Leil, M. K., Papadopoli, D. J., Lin, S., Hart, T., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17549-y · Cited by 288 · see citing works
Structure and mechanisms of ROS generation by NADPH oxidases
Magnani, F., & Mattevi, A. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.03.001 · Cited by 286 · see citing works
Rho GTPase signaling in cancer progression and dissemination
Crosas‐Molist, E., Samain, R., Kohlhammer, L., Orgaz, J. L., George, S. L., Maiques, Ó., Barcelo, J., & Sanz‐Moreno, V. (2021) · Physiological Reviews · doi:10.1152/physrev.00045.2020 · Cited by 277 · 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
Multivalent Small-Molecule Pan-RAS Inhibitors
Welsch, M., Kaplan, A. R., Chambers, J. M., Stokes, M. E., Bos, P. H., Zask, A., Zhang, Y., Sánchez-Martín, M., Badgley, M. A., Huang, C., et al. (2017) · Cell · doi:10.1016/j.cell.2017.02.006 · Cited by 273 · see citing works
Cancer immune evasion, immunoediting and intratumour heterogeneity
Roerden, M., & Spranger, S. (2025) · Nature reviews. Immunology · doi:10.1038/s41577-024-01111-8 · Cited by 285 · see citing works
Koga, T., Suda, K., Fujino, T., Ohara, S., Hamada, A., Nishino, M., Chiba, M., Shimoji, M., Takemoto, T., Arita, T., et al. (2021) · Journal of Thoracic Oncology · doi:10.1016/j.jtho.2021.04.015 · Cited by 265 · see citing works
Pant, S., Wainberg, Z. A., Weekes, C. D., Furqan, M., Kasi, P. M., Devoe, C. E., Leal, A. D., Chung, V., Basturk, O., VanWyk, H., et al. (2024) · Nature Medicine · doi:10.1038/s41591-023-02760-3 · Cited by 267 · see citing works
A Comparative Analysis of Individual RAS Mutations in Cancer Biology
Muñoz-Maldonado, C., Zimmer, Y., & Medová, M. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.01088 · Cited by 250 · 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
Yi, M., Nissley, D. V., McCormick, F. P., & Stephens, R. M. (2020) · Scientific Reports · doi:10.1038/s41598-020-66986-8 · Cited by 237 · see citing works
Metabolic networks in mutant KRAS-driven tumours: tissue specificities and the microenvironment
Kerk, S. A., Papagiannakopoulos, T. Y., Shah, Y. M., & Lyssiotis, C. A. (2021) · Nature reviews. Cancer · doi:10.1038/s41568-021-00375-9 · Cited by 238 · see citing works
Bond, M. J., & Crews, C. M. (2021) · RSC Chemical Biology · doi:10.1039/d1cb00011j · Cited by 227 · see citing works
Allosteric Effects of the Oncogenic RasQ61L Mutant on Raf-RBD
Fetics, S., Guterres, H., Kearney, B. M., Buhrman, G., Ma, B., Nussinov, R., & Mattos, C. (2015) · Structure · doi:10.1016/j.str.2014.12.017 · Cited by 231 · see citing works
Self-citationComprehensive assessment of cancer missense mutation clustering in protein structures
Kamburov, A., Lawrence, M. S., Polak, P. P., Leshchiner, I., Lage, K., Golub, T. R., Lander, E. S., & Getz, G. A. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1516373112 · Cited by 218 · 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
Ras nanoclusters: Versatile lipid-based signaling platforms
Zhou, Y., & Hancock, J. F. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.09.008 · Cited by 224 · 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
ERK5: Structure, regulation and function
Nithianandarajah-Jones, G. N., Wilm, B., Goldring, C. E., Müller, J., & Cross, M. J. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.07.007 · Cited by 221 · see citing works
Young, A., Lou, D., & McCormick, F. (2013) · Cancer Discovery · doi:10.1158/2159-8290.cd-12-0231 · Cited by 211 · see citing works
Aging and the rise of somatic cancer-associated mutations in normal tissues
Risques, R. A., & Kennedy, S. R. (2018) · PLoS Genetics · doi:10.1371/journal.pgen.1007108 · Cited by 212 · 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
Ras and Rap1: A tale of two GTPases
Shah, S. K., Brock, E. J., Ji, K., & Mattingly, R. R. (2018) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2018.03.005 · Cited by 210 · see citing works
Huang, J., Jiang, G., Song, Q., Gu, X. Q., Meng, H., Wang, X.-L., Song, H., Chen, L., Lin, Y., Jiang, D. M., et al. (2017) · Nature Communications · doi:10.1038/ncomms15144 · Cited by 211 · see citing works
Cancer, metastasis, and the epigenome
Kiri, S., & Ryba, T. (2024) · Molecular Cancer · doi:10.1186/s12943-024-02069-w · Cited by 214 · 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
KRAS inhibitors: resistance drivers and combinatorial strategies
Isermann, T., Sers, C., Der, C. J., & Papke, B. (2024) · Trends in cancer · doi:10.1016/j.trecan.2024.11.009 · Cited by 207 · 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
Drugging Ras GTPase: a comprehensive mechanistic and signaling structural view
Lu, S., Jang, H., Gu, S., Zhang, J., & Nussinov, R. (2016) · Chemical Society Reviews · doi:10.1039/c5cs00911a · Cited by 188 · see citing works
Correlation of mutation profile and response in patients with myelofibrosis treated with ruxolitinib
Patel, K. P., Newberry, K. J., Luthra, R., Jabbour, E. J., Pierce, S. A., Cortes, J. E., Singh, R. R., Mehrotra, M., Routbort, M. J., Luthra, M. G., et al. (2015) · Blood · doi:10.1182/blood-2015-03-633404 · Cited by 195 · see citing works
Approach 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
The path to the clinic: a comprehensive review on direct KRASG12C inhibitors
Kwan, A. K., Piazza, G. A., Keeton, A. B., & Leite, C. A. (2022) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-021-02225-w · Cited by 192 · see citing works
KRAS-related proteins in pancreatic cancer
Mann, K. M., Ying, H., Juan, J. M., Jenkins, N. A., & Copeland, N. G. (2016) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2016.09.003 · Cited by 186 · see citing works
KRAS G12C Game of Thrones, which direct KRAS inhibitor will claim the iron throne?
Nagasaka, M., Li, Y., Sukari, A., Ou, S.-H. I., Al-Hallak, M. N., & Azmi, A. S. (2020) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2020.101974 · Cited by 185 · 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
Wang, Z., Liu, F., Fan, N., Zhou, C., Li, D., MacVicar, T., Dong, Q., Bruns, C. J., & Zhao, Y. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.589508 · Cited by 184 · see citing works
RAS-mediated oncogenic signaling pathways in human malignancies
Khan, A. Q., Kuttikrishnan, S., Siveen, K. S., Prabhu, K. S., Shanmugakonar, M., Al‐Naemi, H. A., Haris, M., Dermime, S., & Shahab Uddin, M. S. (2018) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2018.03.001 · Cited by 179 · see citing works
The current understanding on the impact of KRAS on colorectal cancer
Meng, M., Zhong, K., Jiang, T., Liu, Z., Kwan, H. Y., & Su, T. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111717 · Cited by 171 · see citing works
E3 ligases and deubiquitinating enzymes regulating the MAPK signaling pathway in cancers
Park, H., & Baek, K. (2022) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2022.188736 · Cited by 180 · see citing works
KRAS Mutant Pancreatic Cancer: No Lone Path to an Effective Treatment
Zeitouni, D., Pylayeva‐Gupta, Y., Der, C. J., & Bryant, K. L. (2016) · Cancers · doi:10.3390/cancers8040045 · Cited by 179 · see citing works
Arginase 1 is a key driver of immune suppression in pancreatic cancer
Menjivar, R. E., Nwosu, Z. C., Du, W., Donahue, K. L., Hong, H. S., Espinoza, C. E., Brown, K. L., Velez-Delgado, A., Yan, W., Lima, F., et al. (2023) · eLife · doi:10.7554/elife.80721 · Cited by 180 · see citing works
Structural basis of recognition of farnesylated and methylated KRAS4b by PDEδ
Dharmaiah, S., Bindu, L. K., Tran, T. H., Gillette, W., Frank, P. H., Ghirlando, R., Nissley, D. V., Esposito, D., McCormick, F. P., Stephen, A. G., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1615316113 · Cited by 176 · see citing works
Biomarkers That Currently Affect Clinical Practice in Lung Cancer: EGFR, ALK, MET, ROS-1, and KRAS
Korpanty, G. J., Graham, D. M., Vincent, M. D., & Leighl, N. B. (2014) · Frontiers in Oncology · doi:10.3389/fonc.2014.00204 · Cited by 174 · see citing works
Fluorine-containing drugs approved by the FDA in 2021
He, J., Li, Z., Dhawan, G., Zhang, W., Sorochinsky, A. E., Butler, G., Soloshonok, V. A., & Han, J. (2022) · Chinese Chemical Letters · doi:10.1016/j.cclet.2022.06.001 · Cited by 173 · see citing works
Overcoming Challenges for CD3-Bispecific Antibody Therapy in Solid Tumors
Middelburg, J., Kemper, K., Engelberts, P. J., Labrijn, A. F., Schuurman, J., & van Hall, T. (2021) · Cancers · doi:10.3390/cancers13020287 · Cited by 174 · see citing works
- Authors
- Prior, I. A., Lewis, P. D., & Mattos, C.
- Affiliations
- Northeastern University (US)
- Corresponding author
- Prior, Ian A.
- Venue
- Cancer Research
- Published
- 2012-05-14
- Volume
- 72
- Issue
- 10
- Pages
- 2457-2467
- ISSN
- 0008-5472 (ISSN-L)
- 1538-7445
- PMC
- PMC3354961
- OpenAlex
- W2135184154
- Cited by
- 2,063
- References
- 67
- Citations by year
- 2026: 114 · 2025: 154 · 2024: 169 · 2023: 203 · 2022: 189 · 2021: 223 · 2020: 203 · 2019: 164 · 2018: 162 · 2017: 144 · 2016: 110 · 2015: 111 · 2014: 52 · 2013: 47 · 2012: 13
- FWCI
- 23.60
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Cancer Research (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Wellcome Trust (067398)
- Cancer Research UK (A6672)
- Biotechnology and Biological Sciences Research Council (BB/G018162/1)
- National Cancer Institute (R56CA096867)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer Genomics and Diagnostics
- 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
- Keywords
- RAS mutations, KRAS, H-Ras, NRAS, Ras isoforms, codon 12 mutation, mutational spectra, carcinogenesis, epigenetic mechanisms, Ras signaling
- MeSH terms
- Cell Transformation, Neoplastic, Codon, Humans, Models, Molecular, Molecular Conformation, Neoplasms, Genes, ras, Signal Transduction, Point Mutation, ras Proteins, Protein Isoforms, Catalytic Domain, Databases, Genetic, Epigenesis, Genetic
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