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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.
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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].”
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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
Flagged first, then by citations
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Items 801–900 of 1,005
Genetic Events and Signaling Mechanisms Underlying Schwann Cell Fate in Development and Cancer
Vasudevan, H. N., Lucas, C. G., Villanueva-Meyer, J. E., Theodosopoulos, P. V., & Raleigh, D. R. (2020) · Neurosurgery · doi:10.1093/neuros/nyaa455 · Cited by 17
M-Ras is Muscle-Ras, Moderate-Ras, Mineral-Ras, Migration-Ras, and Many More-Ras
Endo, T. (2020) · Experimental Cell Research · doi:10.1016/j.yexcr.2020.112342 · Cited by 14
Pancreatic Tumorigenesis: Oncogenic KRAS and the Vulnerability of the Pancreas to Obesity
Luo, Y., Li, X., Ma, J., Abbruzzese, J. L., & Lu, W. (2021) · Cancers · doi:10.3390/cancers13040778 · Cited by 14
The fellowship of the RING: BRCA1, its partner BARD1 and their liaison in DNA repair and cancer
Russi, M., Marson, D., Fermeglia, A., Aulić, S., Fermeglia, M., Laurini, E., & Pricl, S. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.108009 · Cited by 14
TSPAN6 is a suppressor of Ras-driven cancer
Humbert, P. O., Zoranovic, T., Pranjic, B., Farrell, A. W., Fujikura, K., Simoes, R. D. M., Karim, R., Kozieradzki, I., Cronin, S. J. F., Neely, G. G., et al. (2022) · Oncogene · doi:10.1038/s41388-022-02223-y · Cited by 14
Li, Y., Han, L., & Zhang, Z. (2022) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2022.02.018 · Cited by 16
Lee, K., Fang, Z., Enomoto, M., Gasmi-Seabrook, G. M. C., Zheng, L., Koide, S., Ikura, M., & Marshall, C. B. (2020) · Angewandte Chemie · doi:10.1002/ange.202001758 · Cited by 15
KRAS Pathways: A Potential Gateway for Cancer Therapeutics and Diagnostics
Tripathi, P. K., Mittal, K. R., Jain, N., Sharma, N., & Jain, C. K. (2023) · Recent Patents on Anti-Cancer Drug Discovery · doi:10.2174/1574892818666230406085120 · Cited by 14
Chen, T., Tang, X., Tang, X., Feng, F., Xu, C., Zhao, Q., Wu, Y., Sun, H., & Chen, Y. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115828 · Cited by 14
Devanand, T., Venkatraman, P., & Vemparala, S. (2018) · Scientific Reports · doi:10.1038/s41598-018-31234-7 · Cited by 13
Llavero, F., Montoro, M. L., Sastre, A. A., Fernández‐Moreno, D., Lacerda, H. M., Parada, L. A., Lucía, A., & Zugaza, J. L. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005997 · Cited by 14
Park, S., Kim, T. M., Cho, S., Kim, S., Oh, Y., Kim, M., Keam, B., Kim, D., & Heo, D. S. (2020) · Cancer Letters · doi:10.1016/j.canlet.2020.09.018 · Cited by 14
KRAS gene polymorphisms are associated with the risk of glioma: a two-center case-control study
Guan, Q., Li, Y., Lin, A., Lin, H., Huang, X., Ruan, J., & Zhuo, Z. (2021) · Translational Pediatrics · doi:10.21037/tp-20-359 · Cited by 13
Upregulation of GTPBP4 Promotes the Proliferation of Liver Cancer Cells
Chen, J., Zhang, J., & Zhang, Z. (2021) · Journal of Oncology · doi:10.1155/2021/1049104 · Cited by 14
Shai, A., Galouk, E., Miari, R., Tareef, H., Sammar, M., Zeidan, M., Rayan, A., & Falah, M. (2022) · Oncology Letters · doi:10.3892/ol.2022.13250 · Cited by 15
The rapidly changing field of predictive biomarkers of non-small cell lung cancer
Tóth, L. J., Mokánszki, A., & Méhes, G. (2024) · Pathology & Oncology Research · doi:10.3389/pore.2024.1611733 · Cited by 15
RAS Pathway Mutations and Therapeutics in Vascular Anomalies
Alharbi, S., Merkle, S., Hammill, A. M., Waters, A. M., & Cras, T. D. L. (2025) · Pediatric Blood & Cancer · doi:10.1002/pbc.31605 · Cited by 14
Álvarez-Pérez, J. C., Sanjuán‐Hidalgo, J., Arenas, A. M., Hernández-Navas, I., Benitez‐Cantos, M. S., Andrades, Á., Fariñas, S. C., Lewintre, E. J., Paz-Ares, L. G., Ferrer, I., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-62350-4 · Cited by 15
Zhang, Z., Wang, X., Ye, J., Liu, H., Fang, J., Zhang, M., Li, Y., Huang, J., Zhang, D., Wang, J., et al. (2021) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.1c00426 · Cited by 15
Gerber, M., Goel, S., & Maitra, R. (2021) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2021.105110 · Cited by 13
Autopromotion of K-Ras4B Feedback Activation Through an SOS-Mediated Long-Range Allosteric Effect
He, X., Du, K., Wang, Y., Fan, J., Li, M., Ni, D., Lu, S., Bian, X., & Liu, Y. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.860962 · Cited by 13
Cheng, R., Lv, X., Bu, H., Xu, Q., Wu, J., Xie, K., Tang, J., Wang, L., Zhuang, J., Zhang, Y., et al. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2022.114808 · Cited by 13
Zhao, J., Yuan, X.-K., Luo, R.-Z., Wang, L., Gu, W., Yamane, D., & Feng, H. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1107239 · Cited by 14
Haynes, D., Morgan, E. E., & Chu, E. Y. (2023) · Human Pathology · doi:10.1016/j.humpath.2023.04.014 · Cited by 14
CHAC2 promotes lung adenocarcinoma by regulating ROS-mediated MAPK pathway activation
Peng, W., Wen, L., Jiang, R., Deng, J., & Chen, M. (2023) · Journal of Cancer · doi:10.7150/jca.84036 · Cited by 12
Chhichholiya, Y., Singh, H. V., Vashistha, R., Singh, S., & Munshi, A. (2023) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2023.104250 · Cited by 14
Hajjo, R., Sabbah, D. A., Bardaweel, S. K., & Zhong, H. A. (2024) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2024.2327307 · Cited by 14
Çubuk, C., Lau, R., Cutillas, P. R., Rajeeve, V., John, C. R., Surace, A. E. A., Hands, R., Fossati‐Jimack, L., Lewis, M., & Pitzalis, C. (2024) · Arthritis Research & Therapy · doi:10.1186/s13075-024-03351-4 · Cited by 13
Identification of an H-Ras nanocluster disrupting peptide
Steffen, C. L., Manoharan, G. B., Pavic, K., Yeste‐Vázquez, A., Knuuttila, M., Arora, N., Zhou, Y., Härmä, H., Gaigneaux, A., Grossmann, T. N., et al. (2024) · Communications Biology · doi:10.1038/s42003-024-06523-9 · Cited by 13
IκBα kinase inhibitor BAY 11-7082 promotes anti-tumor effect in RAS-driven cancers
Guruvaiah, P., & Gupta, R. (2024) · Journal of Translational Medicine · doi:10.1186/s12967-024-05384-4 · Cited by 14
Decoding KRAS dynamics: Exploring the impact of mutations and inhibitor binding
Pandey, D., & Roy, K. K. (2024) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2024.110279 · Cited by 12
Zaidh, S. M., Vengateswaran, H. T., Habeeb, M., Aher, K. B., Bhavar, G. B., Irfan, N., & Lakshmi, K. N. V. C. (2025) · Scientific Reports · doi:10.1038/s41598-025-91568-x · Cited by 15
Parry, C., Pellicano, F., Schüttelkopf, A. W., Beyer, K. S., Bower, J. F., Bryson, A., Cameron, K., Cerutti, N. M., Clark, J. P., Davidson, S. C., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c02929 · Cited by 12
Mutant-Specific Targeting of Ras G12C Activity by Covalently Reacting Small Molecules
Goody, R. S., Müller, M. P., & Rauh, D. (2019) · Cell chemical biology · doi:10.1016/j.chembiol.2019.07.005 · Cited by 14
Mund, J. A., Park, S.-J., Smith, A. E., He, Y., Jiang, L., Hawley, E., Roberson, M. J., Mitchell, D. K., Abu-Sultanah, M., Yuan, J., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010981 · Cited by 14
Lu, Y., Lin, J., Duan, M., Rui, Y., Zheng, H., Zhu, L., Zhu, X., & Wei, J. (2021) · Analytical Cellular Pathology · doi:10.1155/2021/5228713 · Cited by 13
Drug targeting opportunities en route to Ras nanoclusters
Pavic, K., Chippalkatti, R., & Abankwa, D. (2022) · Advances in cancer research · doi:10.1016/bs.acr.2021.07.005 · Cited by 13
Millisecond molecular dynamics simulations of KRas-dimer formation and interfaces
Ngo, V. A., & Garcı́a, A. E. (2022) · Biophysical Journal · doi:10.1016/j.bpj.2022.04.026 · Cited by 13
Wang, Y., Zhou, G., Guan, T., Wang, Y., Xuan, C., Ding, T., & Gao, J. (2022) · Briefings in Bioinformatics · doi:10.1093/bib/bbac154 · Cited by 13
Ohoka, N., Suzuki, M., Uchida, T., Tsukumo, Y., Yoshida, M., Inoué, T., Ohki, H., & Naito, M. (2022) · Cancer Science · doi:10.1111/cas.15401 · Cited by 13
Spagnuolo, A., Maione, P., & Gridelli, C. (2022) · Translational Lung Cancer Research · doi:10.21037/tlcr-21-948 · Cited by 15
Robust Strategy for Hit-to-Lead Discovery: NMR for SAR
Larda, S. T., Ayotte, Y., Denk, M. M., Coote, P. W., Heffron, G. J., Bendahan, D., Shahout, F., Girard, N., Iddir, M., Bouchard, P., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00656 · Cited by 13
Zhang, J., Zhang, Z., Zhang, J., Zheng, Z., Yao, Z., Qu, S., & Huang, Y. (2019) · Neural Plasticity · doi:10.1155/2019/7492306 · Cited by 13
Identification of lysine methylation in the core GTPase domain by GoMADScan
Yoshino, H., Yin, G., Kawaguchi, R. K., Popov, K. I., Temple, B. R. S., Sasaki, M., Kofuji, S., Wolfe, K., Kofuji, K., Okumura, K., et al. (2019) · PLoS ONE · doi:10.1371/journal.pone.0219436 · Cited by 13
A conserved, N-terminal tyrosine signal directs Ras for inhibition by Rabex-5
Washington, C., Chernet, R. L., Gokhale, R. H., Martino-Cortez, Y., Liu, H.-Y., Rosenberg, A. M., Shahar, S., & Pfleger, C. M. (2020) · PLoS Genetics · doi:10.1371/journal.pgen.1008715 · Cited by 13
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Béganton, B., Coyaud, É., Laurent, E. M. N., Mangé, A., Jacquemetton, J., Romancer, M. L., Raught, B., & Solassol, J. (2020) · Cancers · doi:10.3390/cancers12113326 · Cited by 13
Rational antibody design for undruggable targets using kinetically controlled biomolecular probes
Trkulja, C. L., Jungholm, O., Davidson, M., Jardemark, K. E., Marcus, M. M., Hägglund, J., Karlsson, A., Karlsson, R., Bruton, J. D., Ivarsson, N., et al. (2021) · Science Advances · doi:10.1126/sciadv.abe6397 · Cited by 13
Dahal, U. P., Rock, B. M., Rodgers, J., Shen, X., Wang, Z., & Wahlstrom, J. L. (2022) · Drug Metabolism and Disposition · doi:10.1124/dmd.121.000798 · Cited by 13
Small GTPases of the Ras superfamily and glycogen phosphorylase regulation in T cells
Llavero, F., Sastre, A. A., Montoro, M. L., Martín, M. A., Arenas, J., Lucía, A., & Zugaza, J. L. (2019) · Small GTPases · doi:10.1080/21541248.2019.1665968 · Cited by 14
Khawaja, H., Briggs, R., Latimer, C. H., Rassel, M., Griffin, D., Hanson, L., Bardelli, A., Di Nicolantonio, F., McDade, S. S., Scott, C. J., et al. (2023) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-22-0301 · Cited by 12
“Raw values were normalised to ACTB and GAPDH expression and were analysed using the ΔΔCT method.”
BackgroundInfluentialCharacterization of mutant versions of the R-RAS2/TC21 GTPase found in tumors
Clavaín, L., Fernández‐Pisonero, I., Movilla, N., Lorenzo‐Martín, L. F., Nieto, B., Abad, A., García‐Navas, R., Llorente-González, C., Sánchez‐Martín, M., Vicente‐Manzanares, M., et al. (2022) · Oncogene · doi:10.1038/s41388-022-02563-9 · Cited by 12
Liang, F., Kang, Z., Sun, X., Chen, J., Duan, X., He, H., & Cheng, J. (2023) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-023-00498-1 · Cited by 12
Lopez, J., Bonsor, D. A., Sale, M. J., Urisman, A., Mehalko, J. L., Cabanski-Dunning, M., Castel, P., Simanshu, D. K., & McCormick, F. P. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104789 · Cited by 11
Self-citationHou, C., Lei, Y., Li, N., Wei, M., Wang, S., Rahman, S. U., Bao, C., Bao, B., Elango, J., & Wu, W. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.125772 · Cited by 12
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Raut, N. G. R., Maile, L. A., Oswalt, L. M., Mitxelena, I., Adlakha, A., Sprague, K. L., Rupert, A. R., Bokros, L., Hofmann, M. C., Cram, J. P., et al. (2024) · JCI Insight · doi:10.1172/jci.insight.171275 · Cited by 12
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Pandey, A., Shen, C. X., Feng, S., Tuipulotu, D. E., Ngo, C., Liu, C., Kurera, M., Mathur, A., Venkataraman, S., Zhang, J., et al. (2024) · Science Advances · doi:10.1126/sciadv.adh3409 · Cited by 12
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Li, L., Jiang, D., Liu, H., Guo, C., Zhang, Q., Li, X., Chen, X., Chen, Z., Feng, J., Tan, S., et al. (2024) · Cancer Research · doi:10.1158/0008-5472.can-23-1878 · Cited by 11
Zeng, Z., & Zhu, Q. C. (2024) · Frontiers in Oncology · doi:10.3389/fonc.2024.1382183 · Cited by 12
Lee, A. A., Kim, N. H., Alvarez, S. A., Ren, H., DeGrandchamp, J. B., Lew, L. J. N., & Groves, J. T. (2024) · Science Advances · doi:10.1126/sciadv.adi0707 · Cited by 11
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Wasiak, K., Ciunowicz, D., Kierasińska, A., Węgierska, M., Pacholczyk, M., Rieske, P., & Stoczyńska-Fidelus, E. (2025) · BMC Cancer · doi:10.1186/s12885-025-14033-y · Cited by 14
Ohka, F., Shinjo, K., Deguchi, S., Matsui, Y., Okuno, Y., Katsushima, K., Suzuki, M. M., Kato, A., Ogiso, N., Yamamichi, A., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-19-1272 · Cited by 13
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Huang, M., & Wang, Y. (2020) · Mass Spectrometry Reviews · doi:10.1002/mas.21637 · Cited by 12
Szeliga, M., Karpińska, M. M., Rola, R., & Niewiadomy, A. (2020) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2020.104362 · Cited by 12
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Stöckl, J. B., Schmid, N., Flenkenthaler, F., Drummer, C., Behr, R., Mayerhofer, A., Arnold, G. J., & Fröhlich, T. (2020) · Cells · doi:10.3390/cells9112498 · Cited by 12
Thomson, C. S., Pundavela, J., Perrino, M. R., Coover, R. A., Choi, K., Chaney, K. E., Rizvi, T. A., Largaespada, D. A., & Ratner, N. (2021) · Oncogene · doi:10.1038/s41388-021-01773-x · Cited by 12
Zhou, X., Xiao, Q., Fu, D., Zhang, H., Tang, Y., He, J., Hu, Y., Kong, X., Teng, F., Liu, X., et al. (2021) · Cancer Biology and Medicine · doi:10.20892/j.issn.2095-3941.2020.0532 · Cited by 14
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Kondo, Y., Paul, J. W., Subramaniam, S., & Kuriyan, J. (2021) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2021.07.005 · Cited by 12
Ma, L., Miao, D., Lee, J. J., Li, T., Chen, Y., Su, G., & Zhao, Y. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.105365 · Cited by 12
Hanley, K. L., Liang, Y., Wang, G., Lin, X., Yang, M., Karin, M., Fu, W., & Feng, G. (2021) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-21-0479 · Cited by 13
Palanivel, C., Chaudhary, N., Seshacharyulu, P., Cox, J. L., Yan, Y., Batra, S. K., & Ouellette, M. M. (2022) · Neoplasia · doi:10.1016/j.neo.2022.01.002 · Cited by 12
Bai, Y., Yi, P., Li, F., Hu, J., & Pan, H. (2022) · Phytochemistry · doi:10.1016/j.phytochem.2022.113243 · Cited by 12
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Xie, T., Luo, Y., Wang, P., Wu, L., Cui, X., Sun, B., & Li, G. (2022) · Analytical Chemistry · doi:10.1021/acs.analchem.2c02920 · Cited by 12
Ma, H., Yu, H., Li, Z., Cao, Z., You-Wei, D., Dai, J., Zhi, D., Xu, Y., Li, N., & Wang, J. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.922183 · Cited by 12
Liu, X., Qiu, Z., Zhang, X., Su, Z., Yi, R., Zou, D., Xie, C., Jin, N., Long, W., & Liu, X. (2023) · Environmental Toxicology · doi:10.1002/tox.23949 · Cited by 12
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Ahmadi, Y., Mahmoudi, N., Yousefi, B., & Karimian, A. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.104621 · Cited by 12
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Sang, B., Ye, L. F., Hu, F., Pourfarjam, Y., Cuevas-Navarro, A., Fan, S., Fu, Z. Q., Washington, A., Rodriguez, D. J., Vides, A., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.04.24.649345 · Cited by 12
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Liu, Z., Zheng, H., Tian, Y., Li, Z., Zhang, S., Zhang, S., Ma, S., Wang, X., & Qin, C. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c01034 · Cited by 12
Jeong, H. J., Min, S., Villalon, L. A., Jeong, K., & Chung, J. K. (2025) · JACS Au · doi:10.1021/jacsau.5c00696 · Cited by 12
Wang, P., Pan, X., Feng, Q., Zou, H., Cui, J., He, Y., Luo, Y., & Yang, J.-L. (2020) · Immunotherapy · doi:10.2217/imt-2019-0222 · Cited by 11
Mohiuddin, M., & Kasahara, K. (2021) · Cancer Genomics & Proteomics · doi:10.21873/cgp.20282 · Cited by 12
Wang, Y., Zhang, H., Li, J., Niu, M., Zhou, Y., & Qu, Y. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.1094887 · Cited by 12
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Basu, A. A., & Zhang, X. (2024) · Frontiers in Chemical Biology · doi:10.3389/fchbi.2024.1352676 · Cited by 11
Chen, Y., Yu, J., Ge, S., Jia, R., Song, X., Wang, Y., & Fan, X. (2024) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.65.6.8 · Cited by 13
Lee, S., Eun, H.-J., & Lee, K. (2024) · Advanced Science · doi:10.1002/advs.202401530 · Cited by 8
Zhou, Q. H., Yang, N., Zhao, M., Huang, D., Zhao, J., Yu, Y., Yuan, Y., Sun, L., Dong, X., Zhang, T., et al. (2024) · European Journal of Cancer · doi:10.1016/j.ejca.2024.114337 · Cited by 11
Li, N., Sun, Y.-J., Huang, L.-Y., Li, R.-R., Zhang, J.-S., Qiu, A.-H., Wang, J., & Yang, L. (2024) · Drug Resistance Updates · doi:10.1016/j.drup.2024.101161 · Cited by 13
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Wang, N., Yuan, Y., Hu, T., Xu, H., & Piao, H. (2024) · Discover Oncology · doi:10.1007/s12672-024-01402-5 · Cited by 11
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Gong, L., Yang, S., Huang, J., & Li, Y. (2024) · Cancer Biology and Medicine · doi:10.20892/j.issn.2095-3941.2024.0320 · Cited by 11
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Banda, J. S. F., Gangane, S., Raza, F., & Massarelli, E. (2025) · Vaccines · doi:10.3390/vaccines13020185 · Cited by 11
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Wu, J., Xie, K., Zhang, Y., Zhang, W., Cheng, R., Zhang, Y., Xia, Y., Liu, T., Yin, R. H., Qiu, Y., et al. (2025) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-025-03369-9 · Cited by 11
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Segura, J., Sánchez-García, R., Sorzano, C. Ó. S., & Carazo, J. M. (2019) · Bioinformatics · doi:10.1093/bioinformatics/btz118 · Cited by 11
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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
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