The DOI matches its Crossref record; 82 of the 85 references it cites were found in a registry or an index.
KRAS Alleles: The Devil Is in the Detail
Open accessAbstract
KRAS is the most frequently mutated oncogene in cancer and KRAS mutation is commonly associated with poor prognosis and resistance to therapy. Since the KRAS oncoprotein is, as yet, not directly druggable, efforts to target KRAS mutant cancers focus on identifying vulnerabilities in downstream signaling pathways or in stress response pathways that are permissive for strong oncogenic signaling. One aspect of KRAS biology that is not well appreciated is the potential biological differences between the many distinct KRAS activating mutations. This review draws upon insights from both clinical and experimental studies to explore similarities and differences among KRAS alleles. Historical and emerging evidence supports the notion that the specific biology related to each allele might be exploitable for allele-specific therapy.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“G12D and G12V mutations are the most common in PDAC, followed by G12R.”
From KRAS: Biology, Inhibition, and Mechanisms of Inhibitor Resistance (2024) · cites this paper as [32]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“KRAS G12R, G13D, Q61H, Q61L, and A146T mutations have increased intrinsic exchange relative to wildtype, but G12C and G12V do not display large changes [4,29,30,31,32].”
From KRAS: Biology, Inhibition, and Mechanisms of Inhibitor Resistance (2024) · cites this paper as [32]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“G12C and G12V mutations are predominant in lung adenocarcinomas with smoking-associated mutational signatures [30,32].”
From KRAS: Biology, Inhibition, and Mechanisms of Inhibitor Resistance (2024) · cites this paper as [32]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Specific KRAS mutations show characteristic patterns of tissue preference (Figure 1b,c).”
From KRAS: Biology, Inhibition, and Mechanisms of Inhibitor Resistance (2024) · cites this paper as [32]
The cited source says what the claim attributes to it.
In the citing paper
“KRAS A146 mutations are primarily found in colorectal cancer and are rarely reported in other types.”
From KRAS: Biology, Inhibition, and Mechanisms of Inhibitor Resistance (2024) · cites this paper as [32]
In the citing paper
“Although epidemiological studies connect specific alleles to clinical outcomes, the mechanisms underlying the distinct clinical characteristics of mutant KRAS alleles are unclear.”
From The origins and genetic interactions of KRAS mutations are allele- and tissue-specific (2021) · cites this paper as [3]
In the citing paper
“associations have been uncovered between the specific KRAS mutation status and therapeutic responses and clinical outcomes of cancer patients3,6”
From The origins and genetic interactions of KRAS mutations are allele- and tissue-specific (2021) · cites this paper as [3]
In the citing paper
“indicating possible differences in signaling behavior of the mutant proteins that exploit the environment of the specific cellular context3,4”
From The origins and genetic interactions of KRAS mutations are allele- and tissue-specific (2021) · cites this paper as [3]
In the citing paper
“the activating alleles found in KRAS vary substantially across cancers”
From The origins and genetic interactions of KRAS mutations are allele- and tissue-specific (2021) · cites this paper as [3]
In the citing paper
“KRAS in particular, is among the most frequently mutated oncogenes in cancer and is commonly associated with therapeutic resistance and poor prognosis1,5,6.”
From The metabolic landscape of RAS-driven cancers from biology to therapy (2021) · cites this paper as [6]
In the citing paper
“Notably, mutations in codons 117 (K117N/R) and 146 (A146T/V) are seen exclusively in colon cancers [51].”
From Drugging KRAS: Current perspectives and state-of-art review (2022) · cites this paper as [51]
In the citing paper
“G12D and G12V are the most common in PDAC, which also shows enrichment for the G12R mutation that is rarely found in CRC lung and lung cancer (16).”
From KRAS mutation in pancreatic cancer (2021) · cites this paper as [16]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Cerami, E., Gao, J., Dogrusoz, U., Gross, B. E., Sumer, S. O., Aksoy, B. A., Jacobsen, A., Byrne, C. J., Heuer, M. L., Larsson, E., et al. (2012) · Cancer Discovery · doi:10.1158/2159-8290.cd-12-0095 · Cited by 17,455
Signatures of mutational processes in human cancer
Initiative, A. P. C. G., Alexandrov, L. B., ICGC Breast Cancer Consortium, ICGC MMML-Seq Consortium, PedBrain, I., Nik-Zainal, S., Wedge, D. C., Aparicio, S. A. J. R., Behjati, S., Biankin, A. V., et al. (2013) · Nature · doi:10.1038/nature12477 · Cited by 9,660
K-ras Mutations and Benefit from Cetuximab in Advanced Colorectal Cancer
Karapetis, C. S., Khambata-Ford, S., Jonker, D. J., O'Callaghan, C. J., Tu, D., Tebbutt, N. C., Simes, R. J., Chalchal, H., Shapiro, J. D., Robitaille, S., et al. (2008) · New England Journal of Medicine · doi:10.1056/nejmoa0804385 · Cited by 3,622
Zehir, A., Benayed, R., Shah, R. H., Syed, A., Middha, S., Kim, H. R., Srinivasan, P., Gao, J., Chakravarty, D., Devlin, S. M., et al. (2017) · Nature Medicine · doi:10.1038/nm.4333 · Cited by 3,380 · cited 1×
“As the sequences of whole cancer genomes become available, we are getting an unparalleled look at frequency and variability of KRAS alleles across the spectrum of primary and metastatic cancers (Figure 1A,B) [3].”
BackgroundK-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
Panitumumab–FOLFOX4 Treatment and RAS Mutations in Colorectal Cancer
Douillard, J.-Y., Oliner, K. S., Siena, S., Tabernero, J., Burkes, R., Barugel, M., Humblet, Y., Bodoky, G., Cunningham, D., Jassem, J., et al. (2013) · New England Journal of Medicine · doi:10.1056/nejmoa1305275 · Cited by 2,263
RAS Proteins and Their Regulators in Human Disease
Simanshu, D. K., Nissley, D. V., & McCormick, F. (2017) · Cell · doi:10.1016/j.cell.2017.06.009 · Cited by 1,943
Cetuximab for the Treatment of Colorectal Cancer
Jonker, D. J., O'Callaghan, C. J., Karapetis, C. S., Zalcberg, J. R., Tu, D., Au, H.-J., Berry, S. R., Krahn, M., Price, T., Simes, R. J., et al. (2007) · New England Journal of Medicine · doi:10.1056/nejmoa071834 · Cited by 1,904
The Guanine Nucleotide-Binding Switch in Three Dimensions
Vetter, I. R., & Wittinghofer, A. (2001) · Science · doi:10.1126/science.1062023 · Cited by 1,875
Cetuximab in the treatment of colorectal cancer.
Goldberg, R. M., Venook, A. P., & Schilsky, R. L. (2004) · PubMed · Cited by 1,518
Flagged first, then by citations
3 of the 85 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 301–376 of 376
A ternary association of KRas, EphA2, and integrins controls PDAC cell behavior
Fatima, M., Haider, N., Cain, S. A., Acharya, B. R., Chastney, M. R., Zha, J., Jones, M., Warwood, S., Knight, D., O'Reilly, D. A., et al. (2026) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2026.113421 · Cited by 1
Targeting Oncogenic KRAS Using Peptide Nucleic Acid Oligomers Attached to Cell-Penetrating Peptides
Mondal, J., Lam, D., Alcindor, T. O., Gerritsen, M. E., Brotz, T. M., Kennedy, J., Rehlaender, B., Ross, A. J., Levy, D. E., Bonagura, C. A., et al. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27167158 · Cited by 1
Dempke, W. C. M., Sippel, C., Fenchel, K., Heinemann, V., Cutsem, E. V., & Arnold, D. (2026) · Future Oncology · doi:10.1080/14796694.2026.2725499 · Cited by 1
Soeroso, N. N., Ananda, F. R., Sitanggang, J. S., & Vinolina, N. S. (2022) · F1000Research · doi:10.12688/f1000research.113303.1 · Cited by 1
Jacobsen, I. C., Spanggaard, I., Højgaard, M., Belcaid, L., Qvortrup, C., Yde, C. W., Schmidt, A. Y., Nielsen, F. C., Willemoe, G. L., Dam, M. S., et al. (2022) · Acta Oncologica · doi:10.1080/0284186x.2022.2156809 · Cited by 1
Ma, J., Song, Y., Zhuang, T., Yang, H., Yang, X., Zheng, J., Luo, J., Xia, Y., Fei, X., Chan, D. W., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1158964 · Cited by 1
Genetic features of pathogenesis in pancreatic adenocarcinomas
Набока, М. В., Garaev, T., Lyapustina, O. S., & Михайлович, В. Д. (2023) · Экспериментальная и клиническая гастроэнтерология · doi:10.31146/1682-8658-ecg-211-3-74-79 · Cited by 1
Lysines K117 and K147 play conserved roles in Ras activation from Drosophila to mammals
Singh, J., Karunaraj, P., Luf, M., & Pfleger, C. M. (2023) · G3 Genes Genomes Genetics · doi:10.1093/g3journal/jkad201 · Cited by 1
The Core Autophagy Protein ATG5 Regulates KRAS Degradation via the Ubiquitin-Proteasome Pathway
Zhang, L., Shen, X., Li, S., Zheng, Z., Hou, X., Zhang, G., & Zhang, B. (2023) · Biology Bulletin · doi:10.1134/s1062359023605888 · Cited by 1
A Facile Method to Append a Bio-ID Tag to Endogenous Mutant Kras Alleles
Budagyan, K., Cannon, A. C., & Chernoff, J. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3822-4_25 · Cited by 1
Motif-guided identification of KRAS-interacting proteins
Wu, S., Gao, X., Wu, D., Liu, L., Yao, H., Meng, X., Zhang, X., & Bai, F. (2024) · BMC Biology · doi:10.1186/s12915-024-02067-w · Cited by 1
Defining the First Part of the Oncogenic KRAS Journey
Osborne, J. K., & Minna, J. D. (2020) · Cell stem cell · doi:10.1016/j.stem.2020.09.009 · Cited by 1
Seo, Y., Chung, E. K., & Jung, B. H. (2023) · Biomedical Chromatography · doi:10.1002/bmc.5642 · Cited by 1
Zheng, Z., Chen, Z., Lin, Y., & Wei, J. (2023) · AIP Advances · doi:10.1063/5.0162189 · Cited by 1
Allosteric regulation of switch-II controls K-Ras oncogenicityPreprint
Yang, M. H., Tran, T. H., Hunt, B., Agnor, R., Johnson, C. W., Waybright, T. J., Nowak, J. A., Stephen, A. G., Simanshu, D. K., & Haigis, K. M. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.09.20.508702 · Cited by 1
Self-citationShifting KRAS hotspot mutations inhibition paradigm in colorectal cancerPreprint
Brás, A. R., Lopes, A., Mendes, N. M., Costa, P. J., Ferreira, A. I., Granja, S., da Silva, A. P. M., Tortosa, F., Baltazar, F., Gärtner, F., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.09.552513 · Cited by 1
Quantifying ‘just-right’ APC inactivation for colorectal cancer initiationPreprint
Guasch, M. B., Feeley, N. A., Soriano, I., Thorn, S., Tomlinson, I. P. M., Nicholson, M. D., & Tibor Antal, A. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.07.10.602868 · Cited by 2
A Drosophila model for Costello Syndrome caused by Ras mutation K117RPreprint
Karunaraj, P., Cao, E., Singh, H., Luf, M., Baker, S. J., Reddy, E. P., & Pfleger, C. M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.03.635762 · Cited by 1
Blocking KRAS Signaling for the Treatment of Lung Cancer: Mission Possible?
Horio, Y. (2018) · Haigan · doi:10.2482/haigan.58.953
Targeting Cancer from a Structural Biology Perspective
Reid, D. F., & Mattos, C. (2019) · Springer eBooks · doi:10.1007/978-981-32-9816-3_12
Damit, D., Patnaik, R. S., Chaw, L., Lu, S. K., Upali, T. P., Lu, Z. H., Kok, K. Y. Y., & Lim, Y. C. (2020) · Preprints.org · doi:10.20944/preprints202007.0277.v1
KRAS: The Art of Understanding a Complex Gene
Velasco, W. V., Ramos-Castaneda, M. A., Clowers, M. J., Deng, S., & Moghaddam, S. J. (2020) · Elsevier eBooks · doi:10.1016/b978-0-08-102723-3.00003-2
Alisertib exerts KRAS allele specific anticancer effects in colorectal cancerPreprint
Ren, B., Gao, Z., Zheng, K., Yang, Y., Su, P., Luo, Q., Feng, J. C., Luo, Z., Geng, Y., Ju, Y., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.10.14.340125
An Expanded Tool Kit for Modeling the Oncogenic Functions of KRAS
Kostyrko, K., & Sweet-Cordero, A. (2020) · Cancer Discovery · doi:10.1158/2159-8290.cd-20-1221
Helix-mimetics as Protein–Protein Interaction Inhibitors
Naiya, G., Chakraborty, M., Ghosh, P., & Roy, S. (2020) · Royal Society of Chemistry eBooks · doi:10.1039/9781788016544-00147
Ras and Ras Signaling as a Therapeutic Target in Cancer
Sliker, B. H., & Campbell, P. M. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820472-6.00006-2
Brain I3 Binding Protein regulates K-Ras4B membrane localization and signalingPreprint
McCabe, I. P., Zhang, H., Cooper, J. A., Turner, D. L., & Vojtek, A. B. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.09.21.461216
Ardalan, B., Azqueta, J. I., England, J., Sleeman, D., & Hartmann, R. F. (2022) · Journal of Cancer Treatment and Diagnosis · doi:10.29245/2578-2967/2022/2.1199
Gene Alterations, Mediators, and Artificial Intelligence in Colorectal Liver Metastases
Wagner, D., & Margonis, G. A. (2022) · Cells · doi:10.3390/cells11142205
Anoosheh, J. P., Barzegar, A., Hejazi, M. S., & Aghdam, E. M. (2022) · Life Sciences · doi:10.1016/j.lfs.2022.121053
Cancer Immunodiagnosis in Upper Gastrointestinal Cancers
Orhan, A. (2022) · Springer eBooks · doi:10.1007/978-3-030-80962-1_147-1
Data from Efficient Correction of Oncogenic KRAS and TP53 Mutations through CRISPR Base Editing
Sayed, S., Sidorova, O. A., Hennig, A., Augsburg, M., Vesga, C. P. C., Abohawya, M., Schmitt, L. T., Sürün, D., Stange, D. E., Mircetic, J., et al. (2023) · doi:10.1158/0008-5472.c.6514029.v1
Soeroso, N. N., Ananda, F. R., Sitanggang, J. S., & Vinolina, N. S. (2023) · F1000Research · doi:10.12688/f1000research.113303.2
曹, 修. (2023) · Hans Journal of Biomedicine · doi:10.12677/hjbm.2023.133039
Najumudeen, A. K., Fey, S. K., Millett, L. M., Ford, C. A., Gilroy, K. L., Gündüz, N., Ridgway, R. A., Anderson, E., Strathdee, D., Clark, W. A., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.29.555396
Lecian, O. M. (2023) · IgMin Research · doi:10.61927/igmin133
Cancer of Unknown Primary Presenting with Chylothorax
Tanaka, E., Oda, N., Ogawa, T., Takata, I., Terao, M., & Ueki, T. (2024) · Internal Medicine · doi:10.2169/internalmedicine.3988-24
Zielgerichtete Therapie des nichtkleinzelligen Lungenkarzinoms
Glanemann, F., & Wiesweg, M. (2024) · Die Onkologie · doi:10.1007/s00761-024-01582-3
Conclusions: the future of RAS drug discovery
Gill, A. L., & Shokat, K. M. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-21861-3.00009-7
Der, C. J., & McCormick, F. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-21861-3.00003-6
KRAS-driven cancer models for in vivo pharmacology and drug discovery
Chugh, S., Dow, L. E., Singh, M., & Aguirre, A. J. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-21861-3.00004-8
KRAS G12 mutant alleles differentially control glutamine metabolism via FOXO1Preprint
Ber, S., Yang, M. H., Sciacovelli, M., Samarajiwa, S., Patel, K., Nikitopoulou, E., Howitt, A., Cook, S. J., Venkitaraman, A. R., Frezza, C., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.19.618135
Chu, T., Zhang, R., Liu, X., Li, L., Li, Y., Niu, Z., Quan, H., Zhao, Y., & Li, Y. (2024) · Clinical and Experimental Medicine · doi:10.1007/s10238-024-01509-7
Nicholson, M. D., & Tomlinson, I. P. M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.01.29.635499
Tachibana, M., Ito, Y., Fujikawa, R., Tsukamoto, K., Uehara, M., Kobayashi, J., & Hayashi, T. (2025) · Diagnostics · doi:10.3390/diagnostics15070894
Mondal, J., Lam, D., Gerritsen, M. E., Brotz, T. M., Kennedy, J. G., Rehlaender, B., Ross, A. J., Levy, D. E., Bonagura, C. A., Lanzilotta, W. N., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.28.645837
Islam, M. S., Ranjit, E., Aktar, S., Moetamedirad, N., Lu, C., Shiddiky, M. J. A., Gopalan, V., & Lam, A. K.-Y. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.06.01.657284
Cancer Immunodiagnosis in Upper Gastrointestinal Cancers
Orhan, A. (2025) · Springer eBooks · doi:10.1007/978-3-032-00763-6_147
Tomaschko, M., Ng, K., Moore, C., Pillsbury, C. E., Rana, S., Campbell, J., Mukherjee, S., Mikolajczak, A., Anastasiou, P., de Castro, A., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.27.684825
Pan, S.-T., Zhou, J., Yang, F., Zhou, S.-F., & Ren, T. (2020) · Figshare · doi:10.6084/m9.figshare.12629179
Pan, S.-T., Zhou, J., Yang, F., Zhou, S.-F., & Ren, T. (2020) · Figshare · doi:10.6084/m9.figshare.12629182
SNPD-siKRAS: siRNA specifically inhibits KRAS with a single-nucleotide mutationPreprint
Kobayashi, Y., Asano, Y., Sato, A., Taniguchi, H., & Ui‐Tei, K. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.09.18.677211
Colorectal Micropapillary Adenocarcinoma: Molecular Mechanisms and Clinical Implications
Chen, B., Zhang, R., Ding, Y., Zhang, K., Song, X., & Chen, J. (2026) · Journal of Gastrointestinal Cancer · doi:10.1007/s12029-025-01372-z
Profiling KRAS mutations in whole blood by error-corrected maximum depth sequencing
Ramaker, R. C., Zhang, Y., Strickler, J. H., Allen, P., Abbruzzese, J. L., & Counter, C. M. (2026) · npj Precision Oncology · doi:10.1038/s41698-026-01399-w
Bertrand‐Chapel, A. (2021) · theses.fr (ABES) · doi:10.70675/6f1078b7z94d3z4096z85a9z40b435cd6a59
MAPK pathway modulation and its implications in KRAS mutant lung adenocarcinoma
Román, S. D. H. (2023) · theses.fr (ABES) · doi:10.70675/8eaccae1ze96bz4279zb69fzaafa5e50c341
Targeting pancreatic cancer with combined inhibition of EGFR and RAF
Brandstetter, J., Goldstein, L., Schreiber, T., Palme, R., Lindner, T., Joksch, M., Krause, B., Vollmar, B., & Kumstel, S. (2026) · PLoS ONE · doi:10.1371/journal.pone.0347843
Association between 8-OHdG Levels and Eosinophil Counts in Chronic Rhinosinusitis with Nasal Polyps
Vieira, T. D. S., Guimarães, L. M., de Siqueira, E. C., Amaral, R. M. B., Anselmo‐Lima, W. T., Tamashiro, E., Diniz, M. G., Valera, F. C. P., Gomez, R. S., & Gomes, C. C. (2026) · International Archives of Otorhinolaryngology · doi:10.1055/s-0046-1819639
La malattia di Gorham-Stout: una rara forma di osteolisi progressiva
Rossi, M., Battafarano, G., & Fattore, A. D. (2026) · L Endocrinologo · doi:10.1007/s40619-026-01797-z
Fong, J. Y., Low, Y. S., Ng, J. J. C., Yam, H. C., Ng, A. W. R., Mai, C., Teo, M. Y. M., & In, L. L. A. (2026) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2026.108493
Tomaschko, M., Ng, K., Moore, C. L., Pillsbury, C. E., Rana, S., Campbell, J., Mukherjee, S., Mikolajczak, A., Anastasiou, P., de Castro, A., et al. (2026) · Cancer Research · doi:10.1158/0008-5472.can-25-5693
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
Osama, H., & Saleh, E. (2026) · Molecular Biology Reports · doi:10.1007/s11033-026-12445-y
Clinically relevant pathologic classification of Congenital Cystic Lung Malformations
Nelson, N. D., Berger, N. F., Peranteau, W. H., & Pogoriler, J. E. (2026) · Seminars in Pediatric Surgery · doi:10.1016/j.sempedsurg.2026.151696
Martin, T. D., Choi, M. Y., McBride, J. C., & Elledge, S. J. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2614664123
ARNTL2 promotes metastatic phenotypes through SERPINE1 transcription in KRAS G12D pancreatic cancer
Shi, X., Yin, X., Gao, S., Wu, X., Wang, H., Wang, B., Xu, X., Zheng, K., Wei, J., Li, G., et al. (2026) · iScience · doi:10.1016/j.isci.2026.117479
The Role of KRAS in Non-Small Cell Lung Cancer: From Molecular Background to Precision Medicine
Gaździcka, J., & Gołąbek, K. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27188194
Nicholson, M. D., & Tomlinson, I. P. M. (2026) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1014858
Amissah, O., Chen, W., Baiden, B. E., Basnet, R., Li, Z., & Kim, G. (2026) · Research Square · doi:10.21203/rs.3.rs-11414448/v1
BindingDB Entry 50013003: Drugging the undruggable: a computational chemist's view of KRAS
BindingDB (2022) · UC San Diego · doi:10.7270/q2db85kh
BindingDB (2025) · UC San Diego · doi:10.7270/q2w66rfz
Uncovering KRAS -mutant allele-specific biology and vulnerabilities in non-small cell lung cancer
d’Arienzo, P. D., McDaid, W. J., Tinsley, K. L., Chen, T., Gasson, E. J., Lindsay, C. R., & Malliri, A. (2026) · Biochemical Journal · doi:10.1042/bcj20250138
Metadata
- Authors
- Haigis, K. M.
- Affiliations
- Beth Israel Deaconess Medical Center (US)
- Corresponding author
- Haigis, Kevin M.
- ORCID
- Haigis, Kevin M.
- Venue
- Trends in Cancer
- Publisher
- Elsevier BV
- Published
- 2017-10
- Volume
- 3
- Issue
- 10
- Pages
- 686-697
- ISSN
- 2405-8025 (ISSN-L)
- 2405-8033
- PMC
- PMC5824632
- OpenAlex
- W2754809261
- Cited by
- 373
- References
- 85
- Citations by year
- 2026: 28 · 2025: 45 · 2024: 41 · 2023: 42 · 2022: 60 · 2021: 54 · 2020: 52 · 2019: 39 · 2018: 11 · 2017: 1
- FWCI
- 2.64
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Trends in cancer (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- NIH/NCI (CA178017, CA199252, CA195744)
- 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 › Melanoma and MAPK Pathways
- Keywords
- KRAS, KRAS mutation, oncogenic signaling, downstream signaling pathways, stress response pathways, cancer therapy resistance
- MeSH terms
- Alleles, Animals, Cell Transformation, Neoplastic, Genotype, Humans, Mutation, Neoplasms, Prognosis, Structure-Activity Relationship, Proto-Oncogene Proteins p21(ras), Genetic Predisposition to Disease, GTP Phosphohydrolases, Genetic Association Studies, Molecular Targeted Therapy
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
