The DOI matches its Crossref record; 157 of the 162 references it cites were found in a registry or an index.
RAS Proteins and Their Regulators in Human Disease
Open accessAbstract
RAS proteins are binary switches, cycling between ON and OFF states during signal transduction. These switches are normally tightly controlled, but in RAS-related diseases, such as cancer, RASopathies, and many psychiatric disorders, mutations in the RAS genes or their regulators render RAS proteins persistently active. The structural basis of the switch and many of the pathways that RAS controls are well known, but the precise mechanisms by which RAS proteins function are less clear. All RAS biology occurs in membranes: a precise understanding of RAS' interaction with membranes is essential to understand RAS action and to intervene in RAS-driven diseases.
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
“In particular, farnesylation at the position 185 cysteine residue results in KRAS anchoring at the plasma membrane, initiating the activation of KRAS and its downstream signaling42.”
From Mechanisms of KRAS inhibitor resistance in KRAS-mutant colorectal cancer harboring Her2 amplification and aberrant KRAS localization (2025) · cites this paper as [42]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“Post-translational modification of KRAS plays an important role in KRAS–MAPK pathway activation.”
From Mechanisms of KRAS inhibitor resistance in KRAS-mutant colorectal cancer harboring Her2 amplification and aberrant KRAS localization (2025) · cites this paper as [42]
The cited source says what the claim attributes to it.
In the citing paper
“KRAS is one of the most frequently mutated oncogenes in cancer, yet efforts to directly target KRAS have been mostly unsuccessful because initial analyses of KRAS proteins indicated that they lack a clear pocket to which small molecules can bind with high affinity [1, 2].”
From Anti-tumor efficacy of a potent and selective non-covalent KRASG12D inhibitor (2022) · cites this paper as [2]
The cited source says what the claim attributes to it.
In the citing paper
“Although KRAS mutations are often collectively classified as a single oncogenic entity, distinct KRAS alleles exhibit substantial biochemical and functional heterogeneity [1,4,12].”
From Precision Targeting of KRAS-Mutant Cancers: Beyond G12C Toward G12D and Pan-RAS Therapeutic Strategies (2026) · cites this paper as [4]
In the citing paper
“Mutational activation of KRAS promotes the initiation and progression of cancers, especially in the colorectum, pancreas, lung, and blood plasma, with varying prevalence of specific activating missense mutations.”
From The origins and genetic interactions of KRAS mutations are allele- and tissue-specific (2021) · cites this paper as [1]
In the citing paper
“However, it is frequently mutated in only a handful of cancers, with the highest frequencies in colorectal adenocarcinoma (COAD), lung adenocarcinoma (LUAD), multiple myeloma (MM), and pancreatic adenocarcinoma (PAAD).”
From The origins and genetic interactions of KRAS mutations are allele- and tissue-specific (2021) · cites this paper as [1]
In the citing paper
“KRAS is one of the most commonly mutated genes in cancer1,2”
From The origins and genetic interactions of KRAS mutations are allele- and tissue-specific (2021) · cites this paper as [1]
In the citing paper
“When mutated at one of its four hotspot codons—12, 13, 61, or 146—activated KRAS protein hyperactivates many downstream effector pathways, such as the MAPK and PI3K-AKT signaling pathways1”
From The origins and genetic interactions of KRAS mutations are allele- and tissue-specific (2021) · cites this paper as [1]
In the citing paper
“As protein tyrosine phosphorylation plays an essential role in multiple intracellular processes, SHP2 is involved in the regulation of multiple signaling pathways, including those involved in cancer cells, such as RAS-MAPK, PI3K-AKT and JAK-STAT pathways.”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [261]
In the citing paper
“RAS acts as a molecular switch, transmitting signals of cell growth and differentiation by binding to GTP or GDP and switching between active and inactive states.261”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [261]
In the citing paper
“abnormalities in components of the RAS pathway, including activating RAS mutations, are common across a diverse range of malignancies”
From The current state of the art and future trends in RAS-targeted cancer therapies (2022) · cites this paper as [4]
In the citing paper
“The RAS family GTPases, KRAS, NRAS and HRAS, cycle between GTP-loaded ‘on’ and GDP-loaded ‘off’ states4,6, involving the action of RAS-guanine nucleotide exchange factors (RAS-GEFs) and RAS-GTPase-activating proteins (RAS-GAPs), respectively.”
From The current state of the art and future trends in RAS-targeted cancer therapies (2022) · cites this paper as [4]
In the citing paper
“Almost all cancer-associated RAS mutations (~95%) affect codon 12, 13 or 61, and lead to a markedly increased basal RAS-GTP:RAS-GDP ratio and constitutive activation of RAS effectors4,6.”
From The current state of the art and future trends in RAS-targeted cancer therapies (2022) · cites this paper as [4]
In the citing paper
“When mutated, oncogenic RAS remains preferentially in the active GTP-bound state, whereas GTP hydrolysis by its GTPase function and enzymes such as GTPase-activating proteins, is compromised1,2.”
From The metabolic landscape of RAS-driven cancers from biology to therapy (2021) · cites this paper as [1]
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 [1]
In the citing paper
“These mutations dramatically shift the equilibrium of Ras protein to exist mostly in the GTP-bound state and effectively uncouple Ras proteins from upstream receptor inputs and drive constitutive signaling to downstream Ras effector pathways (13).”
From KRAS mutation in pancreatic cancer (2021) · cites this paper as [13]
In the citing paper
“On the one hand, the affinity of KRAS and GTP is at the pM level, while the concentration of GTP in cells is up to 0.5 μM.”
From Targeting KRAS mutant cancers: from druggable therapy to drug resistance (2022) · cites this paper as [18]
In the citing paper
“It is difficult to achieve effective competition like protein kinase inhibitors [18, 19].”
From Targeting KRAS mutant cancers: from druggable therapy to drug resistance (2022) · cites this paper as [18]
In the citing paper
“Oncogenic KRAS can activate various downstream effector pathways, and the best characterized are phosphatidylinositol 3-kinase (PI3K) and mitogen-activated protein kinases (MAPK) (23–25).”
From New Horizons in KRAS-Mutant Lung Cancer: Dawn After Darkness (2019) · cites this paper as [24]
In the citing paper
“we recognize that these elements have a substantial influence on KRAS dynamics [53,54] and signaling [55].”
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
K-Ras(G12C) inhibitors allosterically control GTP affinity and effector interactions
Ostrem, J. M., Peters, U., Sos, M. L., Wells, J. A., & Shokat, K. M. (2013) · Nature · doi:10.1038/nature12796 · Cited by 2,557
GEFs and GAPs: Critical Elements in the Control of Small G Proteins
Bos, J. L., Rehmann, H., & Wittinghofer, A. (2007) · Cell · doi:10.1016/j.cell.2007.05.018 · Cited by 1,903
The Guanine Nucleotide-Binding Switch in Three Dimensions
Vetter, I. R., & Wittinghofer, A. (2001) · Science · doi:10.1126/science.1062023 · Cited by 1,875
All ras proteins are polyisoprenylated but only some are palmitoylated
Hancock, J. F., Magee, A. I., Childs, J. E., & Marshall, C. J. (1989) · Cell · doi:10.1016/0092-8674(89)90054-8 · Cited by 1,775
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
Regulation of Small GTPases by GEFs, GAPs, and GDIs
Cherfils, J., & Zeghouf, M. (2013) · Physiological Reviews · doi:10.1152/physrev.00003.2012 · Cited by 1,245
A Cytoplasmic Protein Stimulates Normal N- ras p21 GTPase, But Does Not Affect Oncogenic Mutants
Trahey, M., & McCormick, F. (1987) · Science · doi:10.1126/science.2821624 · Cited by 1,211
Self-citationDistinct patterns of somatic genome alterations in lung adenocarcinomas and squamous cell carcinomas
Cancer Genome Atlas Research Network, Campbell, J. D., Alexandrov, A., Kim, J., Wala, J., Berger, A. H., Pedamallu, C. S., Shukla, S. A., Guo, G., Brooks, A. N., et al. (2016) · Nature Genetics · doi:10.1038/ng.3564 · Cited by 1,200
Milburn, M. V., Tong, L., deVos, A. M., Brünger, A. T., Yamaizumi, Z., Nishimura, S., & Kim, S. (1990) · Science · doi:10.1126/science.2406906 · Cited by 1,062
Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane
Leevers, S. J., Paterson, H. F., & Marshall, C. J. (1994) · Nature · doi:10.1038/369411a0 · Cited by 1,011
Cited by
Sorted by citations
Items 901–1,000 of 1,005
Kang, J.-S., Nam, L. B., Yoo, O.-K., Lee, K., Suh, Y., Kim, D., Kim, W. K., Lim, C., Lee, H., & Keum, Y. (2022) · Antioxidants · doi:10.3390/antiox11010114 · Cited by 11
Blockade of PD-L1/PD-1 signaling promotes osteo-/odontogenic differentiation through Ras activation
Jeon, S. M., Lim, J. S., Park, S. H., Kim, H. J., Kim, H., & Lee, J. (2022) · International Journal of Oral Science · doi:10.1038/s41368-022-00168-2 · Cited by 11
Structural keys unlock RAS–MAPK cellular signalling pathway
Lavoie, H., & Therrien, M. (2022) · Nature · doi:10.1038/d41586-022-02189-7 · Cited by 11
Zhang, Y., Zhang, B., Li, Y., Dai, Y., Li, J., Li, D., Xia, Z., Zhang, J., Liu, P., Chen, M., et al. (2022) · Frontiers of Medicine · doi:10.1007/s11684-021-0911-0 · Cited by 11
Immune dysregulation associated with co-occurring germline CBL and SH2B3 variants
Baccelli, F., Leardini, D., Muratore, E., Messelodi, D., Bertuccio, S. N., Chiriaco, M., Cancrini, C., Conti, F., Castagnetti, F., Pedace, L., et al. (2022) · Human Genomics · doi:10.1186/s40246-022-00414-y · Cited by 11
Marini, E., Marino, M., Gionfriddo, G., Maione, F., Pandini, M., Oddo, D., Giorgis, M., Rolando, B., Blua, F., Gastaldi, S., et al. (2022) · Molecules · doi:10.3390/molecules27238513 · Cited by 11
Kim, B., Lee, S., & Moon, K. C. (2023) · Human Pathology · doi:10.1016/j.humpath.2023.09.011 · Cited by 11
Source, co-occurrence, and prognostic value of PTEN mutations or loss in colorectal cancer
Serebriiskii, I. G., Pavlov, V. A., Andrianov, G. V., Litwin, S., Basickes, S., Newberg, J. Y., Frampton, G. M., Meyer, J. E., & Golemis, E. A. (2023) · npj Genomic Medicine · doi:10.1038/s41525-023-00384-7 · Cited by 11
Synthesis of Ras proteins and their application in biofunctional studies
Hu, J., Zhu, P., Li, Y., & Chen, Y. (2018) · Chinese Chemical Letters · doi:10.1016/j.cclet.2018.05.035 · Cited by 11
Wilkins, J. A., Kaasik, K., Chalkley, R. J., & Burlingame, A. L. (2020) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra120.001944 · Cited by 11
MICA ∗012:01 Allele Facilitates the Metastasis of KRAS-Mutant Colorectal Cancer
Ding, W., Ma, Y., Zhu, W., Pu, W., Zhang, J., Qian, F., Zhou, Y., Deng, Y., Guo, S., Wang, J., et al. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2020.00511 · Cited by 11
Patel, H. V., Johnson, M., Brea, R. J., Rudd, A. K., & Devaraj, N. K. (2020) · ACS Chemical Biology · doi:10.1021/acschembio.0c00222 · Cited by 11
RasV12 Expression in Microglia Initiates Retinal Inflammation and Induces Photoreceptor Degeneration
Moriuchi, Y., Iwagawa, T., Tsuhako, A., Koso, H., Fujita, Y., & Watanabe, S. (2020) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.61.13.34 · Cited by 11
Phakomatoses and Endocrine Gland Tumors: Noteworthy and (Not so) Rare Associations
Chevalier, B., Dupuis, H., Jannin, A., Lemaître, M., Cao, C. D., Cardot-Bauters, C., Espiard, S., & Vantyghem, M. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2021.678869 · Cited by 11
Novel insights into the pathogenesis and treatment of NRAS mutant melanoma
Zhao, J. W., Galvez, C., Beckermann, K. E., Johnson, D. B., & Sosman, J. A. (2021) · Expert Review of Precision Medicine and Drug Development · doi:10.1080/23808993.2021.1938545 · Cited by 11
Dong, Z., Liu, M., Zou, X., Wenqing, S., Liu, X., Zeng, J., & Yang, Z. (2021) · Veterinary Sciences · doi:10.3390/vetsci9010011 · Cited by 11
Machado, C. B., da Cunha, L. S., Maués, J. H. D. S., Pessoa, F. M. C. D. P., de Oliveira, M. B., Ribeiro, R. M., Lopes, G. S., de Moraes, M. O., de Moraes, M. E. A., Khayat, A. S., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23105486 · Cited by 13
Issahaku, A. R., Salifu, E. Y., & Soliman, M. E. S. (2022) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2022.2074141 · Cited by 13
Targeting KRAS-mutant stomach/colorectal tumors by disrupting the ERK2-p53 complex
Wang, X., Xie, Q. M., Ji, Y., Yang, J., Shen, J., Peng, F., Zhang, Y., Jiang, F., Kong, X., Ma, W., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2022.111972 · Cited by 11
Friend or Foe: Regulation, Downstream Effectors of RRAD in Cancer
Sun, Z., Li, Y., Tan, X., Liu, W., He, X., Pan, D., Li, E., Xu, L., & Long, L. (2023) · Biomolecules · doi:10.3390/biom13030477 · Cited by 13
Park, B., Kim, H., & Jeon, T. J. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.03.223 · Cited by 11
Role of KRAS in regulating normal human airway basal cell differentiation
Ogawa, F., Walters, M. S., Shafquat, A., O’Beirne, S. L., Kaner, R. J., Mezey, J. G., Zhang, H., Leopold, P. L., & Crystal, R. G. (2019) · Respiratory Research · doi:10.1186/s12931-019-1129-4 · Cited by 14
Tripathi, S., Dsouza, N. R., Urrutia, R. A., & Zimmermann, M. T. (2020) · Bioinformatics · doi:10.1093/bioinformatics/btaa972 · Cited by 11
Kwon, J. J., Dilly, J., Liu, S., Kim, E., Bian, Y., Dharmaiah, S., Tran, T. H., Kapner, K. S., Ly, S. H., Yang, X., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.22.618529 · Cited by 13
Self-citationClinicopathological analysis and genomic profiling of a rare histiocyte-rich rhabdomyoblastic tumor
Xia, Y., Ye, L., Gong, P., Jiang, H., & Zhang, X. (2021) · Medicine · doi:10.1097/md.0000000000026105 · Cited by 10
Yang, Y., Zhao, C.-J., Jin, Z.-F., Zheng, J., & Ma, L. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1120828 · Cited by 11
Zhang, X., Liu, Y., Yang, R., Guo, Y., Yan, M., Xiao, Y., Dong, Y., Zhang, R., Qin, Y., Bu, Y., et al. (2023) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-023-04839-4 · Cited by 10
Werner, A. N., Kumar, A. I., & Charest, P. G. (2023) · Molecular Biology of the Cell · doi:10.1091/mbc.e23-05-0152 · Cited by 12
Gluing GAP to RAS Mutants: A New Approach to an Old Problem in Cancer Drug Development
Ranđelović, I., Nyíri, K., Koppány, G., Baranyi, M., Tóvári, J., Kigyós, A., Tímár, J., Vértessy, B. G., & Grolmusz, V. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25052572 · Cited by 10
A Top-Down Proteomic Assay to Evaluate KRAS4B-Compound Engagement
D’Ippolito, R. A., Rabara, D., Blanco, M. A., Alberico, E. O., Drew, M. R., Ramakrishnan, N., Sontan, D., Widmeyer, S. R. T., Scheidemantle, G. M., Messing, S. A. J., et al. (2024) · Analytical Chemistry · doi:10.1021/acs.analchem.3c05626 · Cited by 10
Self-citationFu, G., Chazen, R. S., MacMillan, C., & Witterick, I. (2024) · JAMA Network Open · doi:10.1001/jamanetworkopen.2024.11919 · Cited by 10
Assessment of KRASG12C inhibitors for colorectal cancer
Piazza, G. A., Chandrasekaran, P., Maxuitenko, Y. Y., & Budhwani, K. I. (2024) · Frontiers in Oncology · doi:10.3389/fonc.2024.1412435 · Cited by 11
Puranik, N., Jung, H., & Song, M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252011043 · Cited by 11
Functional hydrogel empowering 3D printing titanium alloys
Zhang, W., Zhang, J., Liu, H., Liu, Y., Sheng, X., Zhou, S., Pei, T., Li, C., & Wang, J. (2024) · Materials Today Bio · doi:10.1016/j.mtbio.2024.101422 · Cited by 10
Engineered depalmitoylases enable selective manipulation of protein localization and function
Jayaraman, S., Kochiss, A. L., Alcalay, T.-L., Morfin, P. J. D. R., & Johny, M. B. (2025) · Nature Communications · doi:10.1038/s41467-025-58908-x · Cited by 10
Precision immune regulation in KRAS-mutated cancers: the final piece of the puzzle?
Fu, S., Ma, J., Cai, C., Tan, J., Deng, X., Shen, H., Zeng, S., Chen, Y., & Han, Y. (2025) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-025-03444-1 · Cited by 11
Characterization and inhibitor sensitivity of ARAF, BRAF, and CRAF kinases
Tkacik, E., Jang, D. M., Boxer, K., Ha, B. H., & Eck, M. J. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110800 · Cited by 10
Ras Multimers on the Membrane: Many Ways for a Heart-to-Heart Conversation
Özdemir, E. S., Koester, A. M., & Nan, X. (2022) · Genes · doi:10.3390/genes13020219 · Cited by 10
Luo, L., Zheng, T., Wang, Q., Liao, Y., Zheng, X., Zhong, A., Huang, Z., & Luo, H. (2022) · Pharmaceuticals · doi:10.3390/ph15050584 · Cited by 10
TGFβ-induced changes in membrane curvature influence Ras oncoprotein membrane localization
Damalas, A. F., Vonkova, I., Tutkus, M., & Stamou, D. G. (2022) · Scientific Reports · doi:10.1038/s41598-022-17482-8 · Cited by 10
Effects of Noonan Syndrome-Germline Mutations on Mitochondria and Energy Metabolism
Bajia, D., Bottani, E., & Derwich, K. (2022) · Cells · doi:10.3390/cells11193099 · Cited by 11
Miller, A. L., Perurena, N., Gardner, A., Hinoue, T., Loi, P., Laird, P. W., & Cichowski, K. M. (2023) · Cancer Research · doi:10.1158/0008-5472.can-22-0370 · Cited by 13
MicroRNA-708 emerges as a potential candidate to target undruggable NRAS
Pang, J. M., Chien, P.-C., Kao, M.-C., Chiu, P.-Y., Chen, P.-X., Hsu, Y.-L., Liu, C., Liang, X., & Lin, K. (2023) · PLoS ONE · doi:10.1371/journal.pone.0284744 · Cited by 11
Gu, X., Liu, D., Yu, Y., Wang, H., & Long, D. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c01597 · Cited by 10
Kumar, S. U., Varghese, R. P., Preethi, V. A., Doss, C. G. P., & Zayed, H. (2023) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2811288 · Cited by 11
Liu, C., Jiao, B., Wang, P., Zhang, B., Gao, J., Li, D., Xie, X., Yao, Y., Yan, L., Qin, Z., et al. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01498-w · Cited by 10
RhoB expression associated with chemotherapy response and prognosis in colorectal cancer
Kopsida, M., Liu, N., Kotti, A., Wang, J., Jensen, L. D., Jothimani, G., Hildesjö, C., Haapaniemi, S., Zhong, W., Pathak, S., et al. (2024) · Cancer Cell International · doi:10.1186/s12935-024-03236-1 · Cited by 10
Coover, R. A., Healy, T. E., Li, G., Chaney, K. E., Hennigan, R. F., Thomson, C. S., Aschbacher‐Smith, L., Jankowski, M. P., & Ratner, N. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0635-9 · Cited by 10
Zhao, H., Jiang, X., Duan, L., Yang, L., Wang, W., & Ren, Z. (2019) · Endocrine Journal · doi:10.1507/endocrj.ej19-0215 · Cited by 10
Suresh, N. T., Vimina, E. R., & Krishnakumar, U. (2020) · Current Bioinformatics · doi:10.2174/1574893615999200724145434 · Cited by 10
Merlin cooperates with neurofibromin and Spred1 to suppress the Ras–Erk pathway
Cui, Y., Ma, L., Schacke, S., Yin, J. C., Hsueh, Y., Jin, H., & Morrison, H. (2020) · Human Molecular Genetics · doi:10.1093/hmg/ddaa263 · Cited by 10
Zhou, Y., Hill, C. N., Yao, L., Li, J., Hancock, D. C., Downward, J., Jones, M. G., Davies, D. E., Ewing, R. M., Skipp, P. J. S., et al. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.595712 · Cited by 10
Sills, E. S., & Wood, S. H. (2021) · Global Medical Genetics · doi:10.1055/s-0041-1740018 · Cited by 6
Huang, J., Zhong, Y., Makohon-Moore, A. P., White, T., Jasin, M., Norell, M. A., Wheeler, W. C., & Iacobuzio–Donahue, C. A. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110771 · Cited by 8
Targeting Molecular Alterations in Non-Small-Cell Lung Cancer: What’s Next?
Castro, R. L., García-Peña, T., Mielgo-Rubio, X., Riudavets, M., Teixidó, C., Vilariño, N., Couñago, F., & Mezquita, L. (2022) · Personalized Medicine · doi:10.2217/pme-2021-0059 · Cited by 10
Koester, A. M., Tao, K. X., Szczepaniak, M., Rames, M. J., & Nan, X. (2022) · Biomolecules · doi:10.3390/biom12081033 · Cited by 10
Sun, H., Qian, X., Yang, W. P., Zhou, W.-Z., Zhou, C., Liu, S., Shi, H., & Tian, W. (2022) · PubMed Central · Cited by 10
Tyc, K. M., Kazi, A., Ranjan, A., Wang, R., & Sebti, S. M. (2023) · iScience · doi:10.1016/j.isci.2023.106082 · Cited by 10
Dynamic density functional theory of multicomponent cellular membranes
Stanton, L. G., Oppelstrup, T., Carpenter, T. S., Ingólfsson, H. I., Surh, M. P., Lightstone, F. C., & Glosli, J. N. (2023) · Physical Review Research · doi:10.1103/physrevresearch.5.013080 · Cited by 12
Durojaye, O. A., Ejaz, U., Uzoeto, H. O., Fadahunsi, A. A., Opabunmi, A. O., Ekpo, D. E., Sedzro, D. M., & Idris, M. O. (2023) · Amino Acids · doi:10.1007/s00726-023-03304-2 · Cited by 11
Mues, M., Karra, L., Romero–Moya, D., Wandler, A. M., Hangauer, M. J., Ksionda, O., Thus, Y. J., Lindenbergh, M. F., Shannon, K., McManus, M. T., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.03.045 · Cited by 10
Endogenous Gastrin Collaborates With Mutant KRAS in Pancreatic Carcinogenesis
Nadella, S., Burks, J., Huber, M., Wang, J., Cao, H., Kallakury, B., Tucker, R. D., Boca, S. M., Jermusyk, A. A., Collins, I. J., et al. (2019) · Pancreas · doi:10.1097/mpa.0000000000001360 · Cited by 12
KRAS-Targeted Therapies in Advanced Solid Cancers: Drug the Undruggable?
Saleh, K., Kordahi, M., Felefly, T., Kourié, H. R., & Khalife, N. (2021) · Pharmacogenomics · doi:10.2217/pgs-2021-0045 · Cited by 12
KRAS mutations upregulate Runx1 to promote occurrence of head and neck squamous cell carcinoma
Deng, M., Guo, J., Ling, Z., Zhang, C., He, L., Fan, Z., Cheng, B., & Xia, J. (2023) · Molecular Carcinogenesis · doi:10.1002/mc.23563 · Cited by 9
Pan, R., Dai, J., Liang, W., Wang, H., Ye, L., Ye, S., Lin, Z., Huang, S., Xiong, Y., Zhang, L., et al. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-05885-y · Cited by 9
lncRNAs and cyclin-dependent kinases: Unveiling their critical roles in cancer progression
Siddique, R., Thangavelu, L. P., RenukaJyothi, S., Almalki, W. H., Kazmi, I. A., Kumar, A., Mahajan, S., Kalra, H., Alzarea, S. I., & Pant, K. (2024) · Pathology - Research and Practice · doi:10.1016/j.prp.2024.155333 · Cited by 9
Dionysiou, M., Makri, S. C., Ahlawat, S., Güryildirim, M., Baranano, K. W., Groves, M. L., Argani, P., & Pratilas, C. A. (2024) · Frontiers in Neurology · doi:10.3389/fneur.2024.1466946 · Cited by 9
FGTI-2734 Inhibits ERK Reactivation to Overcome Sotorasib Resistance in KRAS G12C Lung Cancer
Kazi, A., Vasiyani, H., Ghosh, D., Bandyopadhyay, D., Shah, R. D., Vudatha, V., Trevino, J., & Sebti, S. M. (2024) · Journal of Thoracic Oncology · doi:10.1016/j.jtho.2024.11.022 · Cited by 10
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 8
ECM stiffness regulates lung fibroblast survival through RasGRF1-dependent signaling
Monaghan-Benson, E., Aureille, J., & Guilluy, C. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108161 · Cited by 9
Huang, Z., Liu, Z., Chen, L., Liu, Y., Yan, G., Ni, Y., Yan, Q., He, W., Liu, J., Luo, S., et al. (2025) · Frontiers in Oncology · doi:10.3389/fonc.2025.1540427 · Cited by 9
Sorafenib—Drug Delivery Strategies in Primary Liver Cancer
Szyk, P., Czarczyńska-Goślińska, B., Ziegler-Borowska, M., Larrosa, I., & Gośliński, T. A. (2025) · Journal of Functional Biomaterials · doi:10.3390/jfb16040148 · Cited by 12
Ebrahimi, S., Lohnes, B. J., Khan, S. A., Peipp, M., Bockamp, E., Klein, C., Abken, H., Wölfel, C., Theobald, M., & Hartwig, U. F. (2025) · Journal of Molecular Medicine · doi:10.1007/s00109-025-02585-2 · Cited by 9
Lu, X., Xu, S., Deng, Z., Wang, M., & Chen, F. (2025) · Precision Clinical Medicine · doi:10.1093/pcmedi/pbaf021 · Cited by 10
Vascular malformations: from genetics to therapeutics
Morin, G., Galasso, I., & Canaud, G. (2025) · EMBO Molecular Medicine · doi:10.1038/s44321-025-00344-x · Cited by 9
Melanoma: Pathogenesis and Targeted Therapy
Fu, Y., Liu, J., Mo, Z., Wang, B., Deng, Y., & Jiang, Y. (2026) · MedComm · doi:10.1002/mco2.70566 · Cited by 11
Vega-Cuesta, P., Ruiz‐Gómez, A., Molnar, C., Organista, M. F., Resnik-Docampo, M., Sanjuan, J. F., López‐Varea, A., & de Celis, J. F. (2020) · Developmental Biology · doi:10.1016/j.ydbio.2020.02.009 · Cited by 9
Structural Determinants for Light-Dependent Membrane Binding of a Photoswitchable Polybasic Domain
Li, L., He, L., Wu, B., Yu, C., Zhao, H., Zhou, Y., Wang, J., & Zhu, L. (2021) · ACS Synthetic Biology · doi:10.1021/acssynbio.0c00571 · Cited by 9
Twist1 sustains the apoptosis resistance in eosinophils in nasal mucosa of allergic rhinitis
Shao, J., Luo, X., Mo, L., Yang, G., Liu, Z., Liu, J., Liu, Z., Liu, D., & Yang, P. (2021) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2021.108828 · Cited by 9
Membrane-bound KRAS approximates an entropic ensemble of configurations
Heinrich, F., Van, Q. N., Jean-Francois, F. L., Stephen, A. G., & Lösche, M. (2021) · Biophysical Journal · doi:10.1016/j.bpj.2021.08.008 · Cited by 9
Ottaiano, A., Petito, A., Santorsola, M., Gigantino, V., Capuozzo, M., Fontanella, D., Franco, R. D., Borzillo, V., Buonopane, S., Ravo, V., et al. (2021) · Cancers · doi:10.3390/cancers13164236 · Cited by 9
Wang, S., & Sun, L. (2021) · Bioengineered · doi:10.1080/21655979.2021.1985346 · Cited by 9
Mathiot, L., Herbreteau, G., Robin, S., Fenat, C., Bennouna, J., Blanquart, C., Denis, M. G., & Tostivint, E. P. (2022) · Current Oncology · doi:10.3390/curroncol29050300 · Cited by 9
Kealey, J. T., Düßmann, H., Llorente‐Folch, I., Niewidok, N., Salvucci, M., Prehn, J. H. M., & D’Orsi, B. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.893677 · Cited by 11
Structural insights into the role of SHOC2‐MRAS‐PP1C complex in RAF activation
Bonsor, D. A., & Simanshu, D. K. (2023) · FEBS Journal · doi:10.1111/febs.16800 · Cited by 9
Self-citationLIN28B and Let-7 in Diffuse Midline Glioma: A Review
Knowles, T., Huang, T., Qi, J., An, S., Burket, N. J., Cooper, S. H., Nazarian, J., & Saratsis, A. M. (2023) · Cancers · doi:10.3390/cancers15123241 · Cited by 9
Chen, Z., Dong, Y.-Y., Yan, Q., Li, Q., Yu, C., Lai, Y., Tan, J., Fan, M., Xu, C., Liu, L., et al. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1198467 · Cited by 9
Bratei, A. A., & Staden, R. S. (2023) · Medinformatics · doi:10.47852/bonviewmedin32021546 · Cited by 9
Hydrops fetalis: Incidence, Etiologies, Management Strategies, and Outcomes
Younge, T., Ottolini, K. M., Al‐Kouatly, H. B., & Berger, S. (2023) · Research and Reports in Neonatology · doi:10.2147/rrn.s411736 · Cited by 9
Discovery of Five SOS2 Fragment Hits with Binding Modes Determined by SOS2 X-Ray Cocrystallography
Smith, C. R., Chen, D., Christensen, J. G., Coulombe, R., Féthière, J., Gunn, R. J., Hollander, J. G., Jones, B., Ketcham, J. M., Khare, S., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c02140 · Cited by 9
Zhou, Y., Zeng, Z., Li, Z., Ruan, L., Xie, H., Ye, F., Huang, L., Liu, H., & Kang, L. (2024) · Therapeutic Advances in Gastroenterology · doi:10.1177/17562848241249387 · Cited by 9
“Examining RAS pathway rewiring with a chemically inducible activator of RAS”
Rose, J. C., Dieter, E. M., Cunningham‐Bryant, D., & Maly, D. J. (2018) · Small GTPases · doi:10.1080/21541248.2018.1446697 · Cited by 8
Oncogenic KRAS hotspot mutations are rare in IDH‐mutant gliomas
Schittenhelm, J., Krischker, N., Gepfner‐Tuma, I., Behling, F., Noell, S., Eckert, F., Biskup, S., & Tabatabai, G. (2019) · Brain Pathology · doi:10.1111/bpa.12709 · Cited by 9
Localization of RalB signaling at endomembrane compartments and its modulation by autophagy
Singh, M. K., Martin, A. P. J., Joffre, C., Zago, G., Camonis, J., Coppey, M., & Parrini, M. C. (2019) · Scientific Reports · doi:10.1038/s41598-019-45443-1 · Cited by 10
G proteins: binary switches in health and disease
Afzal, M. S. (2020) · Central European Journal of Immunology · doi:10.5114/ceji.2020.101271 · Cited by 9
Li, L., Herzog, M., Möbitz, S., & Winter, R. (2021) · Physical Chemistry Chemical Physics · doi:10.1039/d1cp00007a · Cited by 9
HPLC Method to Resolve, Identify and Quantify Guanine Nucleotides Bound to the GTPase Ras
Hannan, J. P., Swisher, G. H., Martyr, J. G., Cordaro, N. J., Erbse, A. H., & Falke, J. J. (2021) · Analytical Biochemistry · doi:10.1016/j.ab.2021.114338 · Cited by 8
Zhang, H., Hao, Y., Yang, A., Xie, L. Y., Ding, N., Xu, L., Wang, Y., Yang, Y., Bai, Y., Zhang, H., et al. (2021) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2021.10.031 · Cited by 9
A Novel Ras--Related Signature Improves Prognostic Capacity in Oesophageal Squamous Cell Carcinoma
Yang, H., Liu, W., Zheng, S., Cai, H., Luo, H., Feng, Y., & Lei, Y.-Y. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.822966 · Cited by 9
Qin, W., Chen, X., Shen, H. J., Wang, Z., Cai, X., Jiang, N., & Hua, H. (2022) · Turkish Journal of Hematology · doi:10.4274/tjh.galenos.2022.2021.0641 · Cited by 9
Metadata
- Authors
- Simanshu, D. K., Nissley, D. V., & McCormick, F.
- Affiliations
- Frederick National Laboratory for Cancer Research (US)
- University of California, San Francisco (US)
- Corresponding author
- McCormick, Frank
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2017-06
- Volume
- 170
- Issue
- 1
- Pages
- 17-33
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC5555610
- OpenAlex
- W2732767128
- Cited by
- 1,943
- References
- 162
- Citations by year
- 2026: 210 · 2025: 263 · 2024: 276 · 2023: 247 · 2022: 267 · 2021: 247 · 2020: 194 · 2019: 143 · 2018: 82 · 2017: 12
- FWCI
- 11.03
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Cancer Institute
- NIH (HHSN261200800001E)
- Outstanding Investigator Award (5R35CA197709)
- 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 › Cell Biology › Cellular transport and secretion
- Keywords
- Ras proteins, Ras signaling, RASopathies, cancer, mental illness, RAS mutations, signal transduction, membrane binding, Ras activation
- MeSH terms
- Congenital Abnormalities, Animals, Mental Disorders, Cell Membrane, Humans, Mutation, Neoplasms, Phylogeny, Yeasts, Signal Transduction, ras Proteins
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
