Ras protein abundance correlates with Ras isoform mutation patterns in cancer
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Abstract
Activating mutations of Ras genes are often observed in cancer. The protein products of the three Ras genes are almost identical. However, for reasons that remain unclear, KRAS is far more frequently mutated than the other Ras isoforms in cancer and RASopathies. We have quantified HRAS, NRAS, KRAS4A and KRAS4B protein abundance across a large panel of cell lines and healthy tissues. We observe consistent patterns of KRAS > NRAS»HRAS protein expression in cells that correlate with the rank order of Ras mutation frequencies in cancer. Our data provide support for the model of a sweet-spot of Ras dosage mediating isoform-specific contributions to cancer and development. We suggest that in most cases, being the most abundant Ras isoform correlates with occupying the sweet-spot and that HRAS and NRAS expression is usually insufficient to promote oncogenesis when mutated. However, our results challenge the notion that rare codons mechanistically underpin the predominance of KRAS mutant cancers. Finally, direct measurement of mutant versus wildtype KRAS protein abundance revealed a frequent imbalance that may suggest additional non-gene duplication mechanisms for optimizing oncogenic Ras dosage.
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Cites
Global quantification of mammalian gene expression control
Schwanhäusser, B., Busse, D., Li, N., Dittmar, G., Schuchhardt, J., Wolf, J., Chen, W., & Selbach, M. (2011) · Nature · doi:10.1038/nature10098 · Cited by 6,566 · cited 3× · see citing works
“It also means that Ras is a relatively abundant node within the wider Ras signaling network [21].”
Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a
Serrano, M., Lin, A. W., McCurrach, M. E., Beach, D., & Lowe, S. W. (1997) · Cell · doi:10.1016/s0092-8674(00)81902-9 · Cited by 5,178 · see citing works
ras oncogenes in human cancer: a review.
Bos, J. L. (1989) · PubMed · Cited by 5,061 · see citing works
On the Dependency of Cellular Protein Levels on mRNA Abundance
Liu, Y., Beyer, A., & Aebersold, R. (2016) · Cell · doi:10.1016/j.cell.2016.03.014 · Cited by 3,221 · see citing works
Kulak, N. A., Pichler, G., Paron, I., Nagaraj, N., & Mann, M. (2014) · Nature Methods · doi:10.1038/nmeth.2834 · Cited by 1,719 · see citing works
mRNAs, proteins and the emerging principles of gene expression control
Buccitelli, C., & Selbach, M. (2020) · Nature Reviews Genetics · doi:10.1038/s41576-020-0258-4 · Cited by 1,243 · cited 1× · see citing works
“In addition to the role of rare codons, differences in mRNA processing, transport and degradation, differences in access to and processing by translation machinery and differences in protein stability can all result in a disconnect between relative mRNA versus protein abundance [22, 23].”
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-citationRAS 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
Senescence of human fibroblasts induced by oncogenic Raf
Zhu, J., Woods, D., McMahon, M., & Bishop, J. M. (1998) · Genes & Development · doi:10.1101/gad.12.19.2997 · Cited by 826 · see citing works
A “Proteomic Ruler” for Protein Copy Number and Concentration Estimation without Spike-in Standards
Wiśniewski, J. R., Hein, M. Y., Cox, J., & Mann, M. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.037309 · Cited by 690 · see citing works
Woods, D. B., Parry, D., Cherwinski, H. M., Bosch, E., Lees, E. M., & McMahon, M. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.9.5598 · Cited by 639 · see citing works
Yu, C., Dang, Y., Zhou, Z., Wu, C., Zhao, F., Sachs, M. S., & Liu, Y. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.07.018 · Cited by 605 · see citing works
CAIcal: A combined set of tools to assess codon usage adaptation
Puigbò, P., Bravo, I., & García-Vallvé, S. (2008) · Biology Direct · doi:10.1186/1745-6150-3-38 · Cited by 569 · see citing works
K-ras is an essential gene in the mouse with partial functional overlap with N-rasPreprint
Johnson, L., Greenbaum, D. C., Cichowski, K. M., Mercer, K. L., Murphy, E. A., Schmitt, E. S., Bronson, R. T., Umanoff, H., Edelmann, W., Kucherlapati, R., et al. (1997) · Genes & Development · doi:10.1101/gad.11.19.2468 · Cited by 540 · see citing works
Dose-dependent oncogene-induced senescence in vivo and its evasion during mammary tumorigenesis
Sarkisian, C. J., Keister, B. A., Stairs, D. B., Boxer, R. B., Moody, S. E., & Chodosh, L. A. (2007) · Nature Cell Biology · doi:10.1038/ncb1567 · Cited by 490 · 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
Evolutionary routes and KRAS dosage define pancreatic cancer phenotypes
Mueller, S., Engleitner, T., Maresch, R., Zukowska, M., Lange, S., Kaltenbacher, T., Konukiewitz, B., Öllinger, R., Zwiebel, M., Strong, A., et al. (2018) · Nature · doi:10.1038/nature25459 · Cited by 420 · 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
Translation is a non-uniform process
Varenne, S., Buc, J., Lloubès, R., & Lazdunski, C. J. (1984) · Journal of Molecular Biology · doi:10.1016/0022-2836(84)90027-5 · Cited by 384 · 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
Isotope dilution strategies for absolute quantitative proteomics
Brun, V., Masselon, C., Garin, J., & Dupuis, A. (2009) · Journal of Proteomics · doi:10.1016/j.jprot.2009.03.007 · Cited by 314 · 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
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
KRAS Allelic Imbalance Enhances Fitness and Modulates MAP Kinase Dependence in Cancer
Burgess, M. R., Hwang, E., Mroue, R., Bielski, C. M., Wandler, A. M., Huang, B. J., Firestone, A. J., Young, A., Lacap, J. A., Crocker, L., et al. (2017) · Cell · doi:10.1016/j.cell.2017.01.020 · Cited by 183 · see citing works
Sunaga, N., Shames, D. S., Girard, L., Peyton, M., Larsen, J. E., Imai, H., Soh, J., Sato, M., Yanagitani, N., Kaira, K., et al. (2011) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-10-0750 · Cited by 175 · see citing works
Mutant proteins as cancer-specific biomarkers
Wang, Q., Chaerkady, R., Wu, J., Hwang, H. J., Papadopoulos, N., Kopelovich, L., Maitra, A., Matthaei, H., Eshleman, J. R., Hruban, R. H., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1019203108 · Cited by 168 · see citing works
Rare Codons Regulate KRas Oncogenesis
Lampson, B. L., Pershing, N. L., Prinz, J. A., Lacsina, J. R., Marzluff, W. F., Nicchitta, C. V., MacAlpine, D. M., & Counter, C. M. (2012) · Current Biology · doi:10.1016/j.cub.2012.11.031 · Cited by 150 · see citing works
Dupuis, A., Hennekinne, J., Garin, J., & Brun, V. (2008) · PROTEOMICS · doi:10.1002/pmic.200800326 · Cited by 130 · 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
Ntai, I., Fornelli, L., DeHart, C. J., Hutton, J. E., Doubleday, P. F., LeDuc, R. D., van Nispen, A. J., Fellers, R. T., Whiteley, G., Boja, E. S., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1716122115 · Cited by 108 · see citing works
Plowman, S. J., Williamson, D. J., O’Sullivan, M. J., Doig, J., Ritchie, A., Harrison, D. J., Melton, D. W., Arends, M. J., Hooper, M., & Patek, C. E. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.24.9245-9250.2003 · Cited by 104 · see citing works
Ras isoform abundance and signalling in human cancer cell lines
Omerović, J., Hammond, D. E., Clague, M. J., & Prior, I. A. (2007) · Oncogene · doi:10.1038/sj.onc.1210925 · Cited by 101 · see citing works
Self-citationRare codons capacitate Kras-driven de novo tumorigenesis
Pershing, N. L. K., Lampson, B. L., Belsky, J. A., Kaltenbrun, E., MacAlpine, D. M., & Counter, C. M. (2015) · Journal of Clinical Investigation · doi:10.1172/jci77627 · Cited by 77 · see citing works
A rare codon-based translational program of cell proliferation
Guimaraes, J. C., Mittal, N., Gnann, A., Jedlinski, D., Riba, A., Buczak, K., Schmidt, A., & Zavolan, M. (2020) · Genome biology · doi:10.1186/s13059-020-1943-5 · Cited by 72 · see citing works
Xu, J., Haigis, K. M., Firestone, A. J., McNerney, M. E., Li, Q., Davis, E., Chen, S.-C., Nakitandwe, J., Downing, J. R., Jacks, T., et al. (2013) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0096 · Cited by 68 · see citing works
Quantification of spatiotemporal patterns of Ras isoform expression during development
Newlaczyl, A. U., Coulson, J. M., & Prior, I. A. (2017) · Scientific Reports · doi:10.1038/srep41297 · Cited by 58 · see citing works
Self-citationAbsolute Quantification of Endogenous Ras Isoform Abundance
Mageean, C. J., Griffiths, J. R., Smith, D. L., Clague, M. J., & Prior, I. A. (2015) · PLoS ONE · doi:10.1371/journal.pone.0142674 · Cited by 36 · see citing works
Self-citationMutation bias within oncogene families is related to proliferation-specific codon usage
Benisty, H., Weber, M. L., Hernandez‐Alias, X., Schaefer, M. H., & Serrano, L. G. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2016119117 · Cited by 29 · see citing works
Stephens, R. M., Yi, M., Kessing, B. D., Nissley, D. V., & McCormick, F. P. (2017) · Cancer Informatics · doi:10.1177/1176935117711944 · Cited by 26 · see citing works
Oncogene Overdose: Too Much of a Bad Thing for Oncogene-Addicted Cancer Cells
Amin, A. D., Rajan, S. S., Groysman, M. J., Pongtornpipat, P., & schatz, J. H. (2015) · Biomarkers in Cancer · doi:10.4137/bic.s29326 · Cited by 25 · see citing works
Fuentes‐Mateos, R., Jimeno, D., Gómez, C., Calzada, N., Fernández‐Medarde, A., & Santos, E. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-2075-2 · Cited by 20 · see citing works
Signaling levels mold the RAS mutation tropism of urethane
Li, S., & Counter, C. M. (2021) · eLife · doi:10.7554/elife.67172 · Cited by 13 · see citing works
Exploiting codon usage identifies intensity-specific modifiers of Ras/MAPK signaling in vivo
Sawyer, J. K., Kabiri, Z., Montague, R. A., Allen, S. R., Stewart, R. K., Paramore, S. V., Cohen, E., Zaribafzadeh, H., Counter, C. M., & Fox, D. T. (2020) · PLoS Genetics · doi:10.1371/journal.pgen.1009228 · Cited by 10 · see citing works
Absolute Quantitation of GTPase Protein Abundance
Hood, F. E., Sahraoui, Y. M. E., Jenkins, R. E., & Prior, I. A. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1190-6_4 · Cited by 3 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Protein conformational ensembles in function: roles and mechanisms
Nussinov, R., Liu, Y., Zhang, W., & Jang, H. (2023) · RSC Chemical Biology · doi:10.1039/d3cb00114h · Cited by 111 · see citing works
MYC and KRAS cooperation: from historical challenges to therapeutic opportunities in cancer
Casacuberta‐Serra, S., González-Larreategui, Í., Capitán-Leo, D., & Soucek, L. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01907-z · Cited by 80 · see citing works
Walker, G., Brown, C., Ge, X., Kumar, S., Muzumdar, M. D., Gupta, K., & Bhattacharyya, M. (2023) · Nature Nanotechnology · doi:10.1038/s41565-023-01547-4 · Cited by 46 · see citing works
Gastric intestinal metaplasia: progress and remaining challenges
Tong, Q.-Y., Pang, M.-J., Hu, X.-H., Huang, X., Sun, J., Wang, X., Burclaff, J., Mills, J. C., Wang, Z.-N., & Miao, Z. (2024) · Journal of Gastroenterology · doi:10.1007/s00535-023-02073-9 · Cited by 45 · see citing works
Whitley, M. J., Tran, T. H., Rigby, M., Yi, M., Dharmaiah, S., Waybright, T. J., Ramakrishnan, N., Perkins, S. C., Taylor, T. E., Messing, S. A. J., et al. (2024) · Science Advances · doi:10.1126/sciadv.adj4137 · Cited by 39 · see citing works
Zhang, J., Lim, S. M., Yu, M. R., Chen, C., Wang, J., Wang, W., Rui, H., Lu, J., Lü, S., Mok, T. S. K., et al. (2024) · Cancer Discovery · doi:10.1158/2159-8290.cd-24-0006 · Cited by 39 · see citing works
Emerging landscape of KRAS inhibitors in cancer treatment
Riedl, J. M., Matsubara, H., McNeil, R., Patel, P. S., de la Cruz, F. F., Gulhan, D., & Corcoran, R. B. (2026) · Cancer Cell · doi:10.1016/j.ccell.2026.01.001 · Cited by 40 · see citing works
Nussinov, R. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169044 · Cited by 33 · see citing works
Recapitulating the potential contribution of protein S-palmitoylation in cancer
Chaturvedi, S., & Sonawane, A. (2024) · Cancer and Metastasis Reviews · doi:10.1007/s10555-024-10217-3 · Cited by 17 · see citing works
Cheng, C., Hou, K., Hsu, C., & Chiang, L. (2023) · Advanced Science · doi:10.1002/advs.202304926 · Cited by 14 · see citing works
Nolan, A. A., Raso, C., Kölch, W., von Kriegsheim, A., Wynne, K. J., & Matallanas, D. (2023) · Cancers · doi:10.3390/cancers15164141 · Cited by 12 · see citing works
Rossi, J. A. K., Nuevo‐Tapioles, C., O’Keefe, R. A., Hunkeler, M., Schmoker, A. M., Fissore-O'Leary, M., Su, W., Ahearn, I. M., Branco, C. M., Cheong, H., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.115087 · Cited by 9 · see citing works
Kim, H., Gasmi-Seabrook, G. M. C., Uchida, A., Gebregiworgis, T., Marshall, C. B., & Ikura, M. (2025) · Journal of Molecular Biology · doi:10.1016/j.jmb.2025.169162 · Cited by 10 · see citing works
Differential functions of the KRAS splice variants
Rossi, J. A. K., Nuevo‐Tapioles, C., & Philips, M. R. (2023) · Biochemical Society Transactions · doi:10.1042/bst20221347 · Cited by 8 · see citing works
Chippalkatti, R., Parisi, B., Kouzi, F., Laurini, C., Fredj, N. B., & Abankwa, D. (2024) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2024.151425 · Cited by 8 · see citing works
Zhou, M. R., Duan, X., Jin, T., Feng, X., Liu, Y., Wang, S., Feng, J., Zhang, M., Chai, T., Mao, B., et al. (2024) · Molecular Diversity · doi:10.1007/s11030-024-10863-3 · Cited by 8 · see citing works
The ubiquitin code of RAS proteins: Decoding its role in cancer progression
Shi, Y., Shen, Y., Zhang, X., Zhu, N. W., Ding, Y., Yuan, Y., & Wang, J. (2025) · iScience · doi:10.1016/j.isci.2025.113029 · Cited by 7 · see citing works
Experimental variables determine the outcome of RAS-RAS interactions
Zhou, Z., Nguyen, T.-L., Li, X.-X., Poujol, C., Berlinska, E., Michelina, S. V., Kapp, J. N., Plückthun, A., Winslow, M. M., Ambrogio, C., et al. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107859 · Cited by 7 · see citing works
Tan, Y. S., Chakrabarti, M., Stein, R. M., Prentis, L. E., Rizzo, R. C., Kurtzman, T., Fischer, M. M., & Balius, T. E. (2025) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.4c01623 · Cited by 6 · see citing works
Wild-type RAS signaling is an essential therapeutic target in RAS -mutated cancers
Sealover, N. E., Finniff, B. A., Hughes, J. M., Sheffels, E., Lee, H., LaMorte, J. P., Gambhir, V., Beckley, Z., Linke, A. J., Wilkerson, M. D., et al. (2025) · Science Signaling · doi:10.1126/scisignal.adx5186 · Cited by 6 · see citing works
The impact of RAS on cell differentiation in health and disease
Duval, C. J., Bottone, S., Schaffner‐Reckinger, E., & Abankwa, D. (2025) · Biochemical Journal · doi:10.1042/bcj20253364 · Cited by 6 · see citing works
Signaling to make human ribosomes: Connections between the cytoplasm and the nucleolus
Lawrence, I. R., Sutton, E. C., Bhaskar, S., & Baserga, S. J. (2026) · Molecular Cell · doi:10.1016/j.molcel.2026.01.007 · Cited by 6 · see citing works
MTMR regulates KRAS function by controlling plasma membrane levels of phospholipids
Lange, T. E., Naji, A. K., van der Hoeven, R., Liang, H., Zhou, Y., Hammond, G. R. V., Hancock, J. F., & Cho, K. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202403126 · Cited by 5 · see citing works
Revisiting RAS family GTPase signaling: effector selectivity and oncogenic bypass
Simanshu, D. K., & McCormick, F. P. (2026) · Biochemical Journal · doi:10.1042/bcj20250142 · Cited by 4 · see citing works
Ras/Raf dimerization model for activation of Raf kinase
de Barros, M., Labrie, G., & Mattos, C. (2025) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2025.103150 · Cited by 4 · see citing works
RAS GTPases and Interleaflet Coupling in the Plasma MembranePreprint
Liu, J., Arora, N., & Zhou, Y. (2023) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a041414 · Cited by 5 · see citing works
Nadee, P., Prompat, N., Yamabhai, M., Sangkhathat, S., Benjakul, S., Tipmanee, V., & Saetang, J. (2024) · Advanced Theory and Simulations · doi:10.1002/adts.202400489 · Cited by 3 · see citing works
LncRNA SLNCR phenocopies the E2F1 DNA binding site to promote melanoma progression
Shah, K. K., Anastasakou, E., Sejour, L., Wang, Y., Wert-Lamas, L., Rauchet, C., Studer, S., Goller, S. G., Distel, R. J., Marasco, W. A., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115608 · Cited by 3 · see citing works
Functional distinction in oncogenic Ras variant activity in Caenorhabditis elegans
Lyu, H., & Chamberlin, H. (2024) · Disease Models & Mechanisms · doi:10.1242/dmm.050577 · Cited by 3 · see citing works
KRAS inhibitors in drug resistance and potential for combination therapy
Rathod, L. S., Sakle, N. S., & Mokale, S. N. (2024) · Tumori Journal · doi:10.1177/03008916241289206 · Cited by 2 · see citing works
Rac1 selectively binds a specific lamellipodin isoform via a noncanonical helical interface
Gao, T., Zhang, P., Kurimchak, A. M., Duncan, J. S., & Wu, J. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.111023 · Cited by 2 · see citing works
Targeting a Glutamic Acid in PDEδ with Fluoromethyl-Aryl Electrophiles Impairs K-Ras Signaling
Zhang, R., Huetzen, M. A., Binici, A., Martín‐Gago, P., Gasper, R., Rudashevskaya, E. L., Liu, J., Nagaraju, C., Reckzeh, E. S., Stuedle, A. S. T., et al. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c02082 · Cited by 2 · see citing works
Hu, L., Ahmari, N., Schaeper, A., Pundavela, J., Kim, M., Dombi, E., Wu, J., Brunmair, J., Petronczki, Ö. Y., & Ratner, N. (2026) · Science Advances · doi:10.1126/sciadv.aeg3475 · Cited by 2 · see citing works
Computational screening of phytochemicals targeting mutant KRAS in colorectal cancer
Arooj, M., Mateen, R. M., Javed, M., Ali, M., Fareed, M. I., Parveen, R., Bahadur, A., Iqbal, S., Mahmood, S., Knani, S., et al. (2025) · Scientific Reports · doi:10.1038/s41598-025-14229-z · Cited by 2 · see citing works
Baseline expression of c-Myc defines the tissue specificity of oncogenic K-RasPreprint
Popow, O., Yu, Q., Yapp, C., Hull, S., Paulo, J. A., Hanna, B., Xu, S., Kuang, Y., Sigel, C., Paweletz, C. P., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.21.665965 · Cited by 2 · see citing works
Almowallad, S. J., Alanazi, S. S., Obidan, A., Alsulami, S. O., Younis, F. A., & Alwabsi, H. A. (2025) · Proceedings of the Indian National Science Academy · doi:10.1007/s43538-025-00541-9 · Cited by 1 · see citing works
Intrinsic resistance to RAS inhibitors is driven by dysregulation of KRAS degradation
Ivanišević, T., Ma, Y., Boxel, E. V., Magits, W., Lechat, B., Koçberber, Z., Willnow, P., Fendt, S., Velde, G. V., Sewduth, R. N., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-67109-5 · Cited by 2 · see citing works
Deshpande, A. A., Lockhart, J. H., Napoli, M., & Flores, E. R. (2026) · Molecular and Cellular Biology · doi:10.1080/10985549.2026.2662223 · Cited by 1 · see citing works
Yousefipour, K., Rohani, S. S. R., Hosseini, S. M. M., Kafilzadeh, K., Alavi, N. S., & Firouzabadi, N. (2026) · Cancer Cell International · doi:10.1186/s12935-026-04351-x · Cited by 1 · see citing works
Magnesium as a conformational gatekeeper of KRAS : Structural dynamics and therapeutic implications
Srinivasu, B. Y., Damerla, T. S., Stec, A., Zhou, Z., Engen, J. R., Westover, K. D., & Wales, T. E. (2026) · Protein Science · doi:10.1002/pro.70681 · Cited by 1 · see citing works
ADCs for colorectal carcinoma: decoding clinical evidence for molecular design innovation
Wu, X., Du, F., Liu, Z., Zhang, B. H., Tong, J., Liu, Y., & Xia, T. (2026) · SLAS DISCOVERY · doi:10.1016/j.slasd.2026.100320 · Cited by 1 · see citing works
RAS, BRAF, and MMR system mutations in metastatic colorectal cancers: an observational study
Khoshnoudi, H., Joybari, A. Y., Sanatdoost, P. N., Toutounchi, A. H., Adinevand, E., & Nematihonar, B. (2024) · International Journal of Surgery Oncology · doi:10.1097/ij9.0000000000000133 · Cited by 1 · see citing works
Editorial: Identifying the isoform-specific roles of RAS paralogs in health and disease
Nakhaei‐Rad, S., & Fejtová, A. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1199356
Arkani, M., Mahallati, A. H., & Entezari, M. (2023) · Qur̓ān/pizhūhī-i khāvar/shināsān · doi:10.61186/iau.33.3.230
Kaczmarczyk, J. A., Whiteley, G., & Blonder, J. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3922-1_17
Mediating kinase activity in Ras-mutant cancer: potential for an individualised approach?
Healy, F. M., Turner, A. L., Marensi, V., & MacEwan, D. J. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1441938
An updated patent review of antitumor macrocyclic kinase inhibitors (2019 present)
He, X., Chen, L., Wu, S., Chen, Z., Zhu, W., & Qiao, D. (2025) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2025.2484368
Di‐Luoffo, M., Arcucci, S., Therville, N., Marty, T., D’Angelo, R., Chaouki, M., Thibault, B., Swider, P., Assémat, P., Delarue, M., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.23.681444
Kuchenov, D., Ziebell, F., Salopiata, F., Thomas, A., Citir, M., Klingmüller, U., Huber, W., & Schultz, C. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.21.683831
Jeldes, E., Varas‐Godoy, M., González-Chacón, P., Campos, A. V., Martin, A. J., Villamán, C., Roco-Videla, Á., Olavarría, J. V., & Villota, C. (2026) · Medicina · doi:10.3390/medicina62010110
Innovative targeted therapies for mosaic RAS-related vascular malformations
Morin, G. (2024) · theses.fr (ABES) · doi:10.70675/88882e5fz1bf9z4dbezae13zba4200ee9598
MAPK pathway modulation and its implications in KRAS mutant lung adenocarcinoma
Román, S. D. H. (2023) · theses.fr (ABES) · doi:10.70675/8eaccae1ze96bz4279zb69fzaafa5e50c341
Virtual Screening for Lead Molecules in Aegle Marmelos (L.) Correa. on Mutated Ras Proteins
Chandran, N. N. B., & Thomas, R. P. (2026) · Biosciences Biotechnology Research Asia · doi:10.13005/bbra/3498
Dorbin, D., Herrera, J., Davidson, R., Chandrashekar, N., Scheuber, G., Jayakrishnan, P., Rajesh, C., Johnson, G., Yuan, J., Sochor, M., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.07.05.735339
Yang, X., Tao, X., Qi, W., Luo, R., Lan, T., Xie, K., Cai, Y., Gao, F., Lv, Y., Liu, C., et al. (2026) · Journal of Pharmaceutical Analysis · doi:10.1016/j.jpha.2026.101718
Current Molecular-Targeted Therapies in Melanoma and Their Mechanism of Resistance
Bahari, R., Nguyen, M., Sohail, N., Lopez, S., Vasanthi, S. S., Amin, J., Ramaswami, D., Kapetaneas, G., Karne, R., Altayeh, U., et al. (2026) · Cancers · doi:10.3390/cancers18142310
- Authors
- Hood, F. E., Sahraoui, Y. M., Jenkins, R. E., & Prior, I. A.
- Affiliations
- University of Liverpool (GB)
- Corresponding author
- Prior, Ian A.
- Venue
- Oncogene
- Published
- 2023-03-02
- Volume
- 42
- Issue
- 15
- Pages
- 1224-1232
- ISSN
- 0950-9232 (ISSN-L)
- 1476-5594
- PMC
- PMC10079525
- OpenAlex
- W4322775106
- Cited by
- 56
- References
- 44
- Citations by year
- 2026: 14 · 2025: 16 · 2024: 17 · 2023: 9
- FWCI
- 4.99
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Oncogene (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- North West Cancer Research Fund (CR1166)
- Wellcome Trust (WT203983)
- 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 › Cancer Research › Cancer Genomics and Diagnostics
- Keywords
- Ras isoforms, KRAS, NRAS, HRAS, K-Ras4B, RASopathies, cancer cell lines, codon preference, carcinogenesis
- MeSH terms
- Humans, Mutation, Neoplasms, Signal Transduction, Proto-Oncogene Proteins p21(ras), ras Proteins, Protein Isoforms
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