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
Flagged first, then by citations
5 of the 162 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Items 601–700 of 1,005
Disrupted molecular glue complex drives RAS inhibitor resistance
Sang, B., Ye, L. F., Fu, Z., Pourfarjam, Y., Cuevas-Navarro, A., Fan, S., Hu, F., Washington, A., Rodriguez, D. J., Vides, A., et al. (2026) · Cell · doi:10.1016/j.cell.2026.03.031 · Cited by 43
Mottini, C., Tomihara, H., Carrella, D., Lamolinara, A., Iezzi, M., Huang, J. K.-L., Amoreo, C. A., Buglioni, S., Manni, I., Robinson, F. S., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-19-0187 · Cited by 22
Li, L., Zhao, H., Liao, H., Chen, J., Liu, J., & Chen, J. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.104825 · Cited by 22
KRAS-related long noncoding RNAs in human cancers
Saliani, M., Mirzaiebadizi, A., Javadmanesh, A., Siavoshi, A., & Ahmadian, M. R. (2021) · Cancer Gene Therapy · doi:10.1038/s41417-021-00381-x · Cited by 25
Biology of Melanocytes and Primary Melanoma
Zaidi, M. R., Fisher, D. E., & Rizos, H. (2020) · Springer eBooks · doi:10.1007/978-3-030-05070-2_42 · Cited by 23
Zhuang, H., Fan, J., Li, M., Zhang, H., Yang, X., Lin, L., Lu, S., Wang, Q., & Liu, Y. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.915512 · Cited by 23
Fluorescent Biosensor for Measuring Ras Activity in Living Cells
Weeks, R., Zhou, X., Yuan, T. L., & Zhang, J. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.2c05203 · Cited by 24
Emerging treatments for myelodysplastic syndromes: Biological rationales and clinical translation
Rodríguez‐Sevilla, J. J., Ademà, V., Garcia‐Manero, G., & Colla, S. (2023) · Cell Reports Medicine · doi:10.1016/j.xcrm.2023.100940 · Cited by 23
Origin and Evolution of RAS Membrane Targeting
García‐España, A., & Philips, M. R. (2023) · Oncogene · doi:10.1038/s41388-023-02672-z · Cited by 23
Structural characterization of 14-3-3ζ in complex with the human Son of sevenless homolog 1 (SOS1)
Ballone, A., Centorrino, F., Wolter, M., & Ottmann, C. (2018) · Journal of Structural Biology · doi:10.1016/j.jsb.2018.01.011 · Cited by 20
Motta, M., Giancotti, A., Mastromoro, G., Chandramouli, B., Pinna, V., Pantaleoni, F., Giosaffatte, N. D., Petrini, S., Mazza, T., D’Ambrosio, V., et al. (2019) · Human Mutation · doi:10.1002/humu.23767 · Cited by 21
NF1 patient missense variants predict a role for ATM in modifying neurofibroma initiation
Yu, Y., Choi, K., Wu, J., Andreassen, P. R., Dexheimer, P. J., Keddache, M. A., Brems, H., Spinner, R. J., Cancelas, J. A., Martin, L. J., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02086-w · Cited by 22
DEPDC1 up‐regulates RAS expression to inhibit autophagy in lung adenocarcinoma cells
Wang, W., Li, A., Han, X., Wang, Q., Guo, J., Wu, Y., Wang, C., & Huang, G. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15947 · Cited by 21
Saturno, G., Lopes, F., Niculescu-Duvaz, I., Niculescu-Duvaz, D., Zambon, A., Davies, L., Johnson, L., Preece, N., Lee, R., Viros, A., et al. (2021) · Annals of Oncology · doi:10.1016/j.annonc.2020.10.483 · Cited by 21
Targeting the SHOC2–RAS interaction in RAS-mutant cancers
Hauseman, Z. J., Stauffer, F., Beyer, K. S., Mollé, S., Cavicchioli, E., Marchand, J., Fodor, M., Viscomi, J., Dhembi, A., Katz, S., et al. (2025) · Nature · doi:10.1038/s41586-025-08931-1 · Cited by 25
Orally effective FDA-approved protein kinase targeted covalent inhibitors (TCIs): A 2025 update
Roskoski, R. J. (2025) · Pharmacological Research · doi:10.1016/j.phrs.2025.107805 · Cited by 21
Alexander, P., Chan, A. H., Rabara, D., Swain, M., Larsen, E. K., Dyba, M. D., Chertov, O., Ashraf, M., Champagne, A., Lin, K. Y., et al. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110331 · Cited by 24
Self-citationSciver, R. E. V., Lee, M., Lee, C. G. L., Lafever, A., Svyatova, E. A., Kanda, K., Collier, A. L., van Reesema, L. L. S., Tang-Tan, A. M., Zheleva, V. P., et al. (2018) · Cancers · doi:10.3390/cancers10050142 · Cited by 21
Chen, C., Pino, M. R., Haller, P. R., & Verde, F. (2019) · Molecular Biology of the Cell · doi:10.1091/mbc.e19-03-0172 · Cited by 19
Weidle, U. H., Birzele, F., & Nopora, A. (2019) · Cancer Genomics & Proteomics · doi:10.21873/cgp.20149 · Cited by 21
Molecular Biology of Pediatric and Adult Male Germ Cell Tumors
Pinto, M. T., Cárcano, F. M., Vieira, A. G. S., Cabral, E. R. M., & Lopes, L. F. (2021) · Cancers · doi:10.3390/cancers13102349 · Cited by 21
Colorectal Cancer, Liver Metastases and Biotherapies
Osei‐Bordom, D., Kamarajah, S. K., & Christou, N. (2021) · Biomedicines · doi:10.3390/biomedicines9080894 · Cited by 22
Regulation of GTPase function by autophosphorylation
Johnson, C. W., Seo, H., Terrell, E. M., Yang, M.-H., KleinJan, F., Gebregiworgis, T., Gasmi-Seabrook, G. M. C., Geffken, E. A., Lakhani, J., Song, K., et al. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.02.011 · Cited by 21
Novoplansky, O., Jagadeeshan, S., Regev, O., Menashe, I., & Elkabets, M. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.838911 · Cited by 23
Genetics, molecular control and clinical relevance of habituation learning
Blok, L. E. R., Boon, M., van Reijmersdal, B., Höffler, K. D., Fencková, M., & Schenck, A. (2022) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2022.104883 · Cited by 23
Ma, Y., Schulz, B., Trakooljul, N., Alammar, M., Sekora, A., Sender, S., Hadlich, F., Zechner, D., Weiß, F. U., Lerch, M. M., et al. (2022) · Cancers · doi:10.3390/cancers14184467 · Cited by 21
Covalent inhibitors: An ambitious approach for the discovery of newer oncotherapeutics
Cheke, R. S., & Kharkar, P. S. (2023) · Drug Development Research · doi:10.1002/ddr.22132 · Cited by 23
Chen, Q., Lin, W., Zhou, X.-X., Cao, Z., Feng, X., Gao, Y., & He, J. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107060 · Cited by 22
Targeting KRASG12C in Non-Small-Cell Lung Cancer: Current Standards and Developments
Torres-Jiménez, J., Espinar, J. B., Bote, H., Berjaga, M. Z., Esteban-Villarrubia, J., Fraile, J. Z., & Paz-Ares, L. G. (2024) · Drugs · doi:10.1007/s40265-024-02030-7 · Cited by 24
TRPML1 and RAS-driven cancers – exploring a link with great therapeutic potential
Jung, J., & Venkatachalam, K. (2019) · Channels · doi:10.1080/19336950.2019.1666457 · Cited by 21
Multiple versus solitary giant cell lesions of the jaw: Similar or distinct entities?
Schreuder, W. H., van der Wal, J. E., de Lange, J., & van den Berg, H. (2021) · Bone · doi:10.1016/j.bone.2021.115935 · Cited by 22
Toward Understanding the Mechanisms of Malignant Peripheral Nerve Sheath Tumor Development
Mohamad, T., Plante, C., & Brosseau, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168620 · Cited by 21
Muthusamy, M., Ramani, P., Arumugam, P., Rudrapathy, P., Kangusamy, B., Veeraraghavan, V. P., Jayaraman, S., Kannan, B., & Pandi, A. (2025) · BMC Oral Health · doi:10.1186/s12903-024-05406-z · Cited by 26
Treatment of KRAS-Mutated Pancreatic Cancer: New Hope for the Patients?
Krupa, K., Fudalej, M. M., Włoszek, E., Miski, H., Badowska-Kozakiewicz, A. M., Mękal, D., Budzik, M. P., Czerw, A. I., & Deptała, A. (2025) · Cancers · doi:10.3390/cancers17152453 · Cited by 21
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
Tateo, V., Manuzzi, L., Parisi, C., Giglio, A. D., Campana, D., Pantaleo, M. A., & Lamberti, G. (2021) · Pharmaceuticals · doi:10.3390/ph14040316 · Cited by 20
KRAS and MET in non-small-cell lung cancer: two of the new kids on the ‘drivers’ block
García-Robledo, J. E., Rosell, R., Ruíz-Patiño, A., Sotelo, C., Arrieta, O. G., Zatarain-Barrón, L., Ordóñez‐Reyes, C., Jaller, E., Rojas, L., Russo, A., et al. (2022) · Therapeutic Advances in Respiratory Disease · doi:10.1177/17534666211066064 · Cited by 22
XBP1 is required in Th2 polarization induction in airway allergy
Zeng, X., Xiao, X., Hu, S., He, W., Wu, G., Geng, X., Fan, J., Ma, L., Liu, J., Liu, Z., et al. (2022) · Theranostics · doi:10.7150/thno.75100 · Cited by 19
PHLDA1 promotes glioblastoma cell growth via sustaining the activation state of Ras
Wang, J., Yao, N., Hu, Y., Lei, M., Wang, M., Yang, L., Patel, S., Li, X., Liu, K., & Dong, Z. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04538-1 · Cited by 20
Crystal Structure of an i‐Motif from the HRAS Oncogene Promoter
Li, S. K., Jordan, D., Lin, L. Y., McCarthy, S. E., Schneekloth, J. S., & Yatsunyk, L. A. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202301666 · Cited by 20
Zhang, Q., Zheng, L., Bai, Y., Su, C., Che, Y., Xu, J., Sun, K., Ni, J., Huang, L., Shen, Y., et al. (2023) · Cancer Letters · doi:10.1016/j.canlet.2023.216426 · Cited by 20
Xiao, X., Feng, J., Ma, J., Xia, X., Liu, X., Zhang, J., Ding, C., Pang, X., & Zhang, A. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c01724 · Cited by 21
Insights into optic pathway glioma vision loss from mouse models of neurofibromatosis type 1
Freret, M. E., & Gutmann, D. H. (2018) · Journal of Neuroscience Research · doi:10.1002/jnr.24250 · Cited by 20
Effects of MIR143 on rat sarcoma signaling networks in solid tumors: A brief overview
Tokumaru, Y., Takabe, K., Yoshida, K., & Akao, Y. (2020) · Cancer Science · doi:10.1111/cas.14357 · Cited by 18
Inhibition of RAS: proven and potential vulnerabilities
Zuberi, M., Khan, I., & O’Bryan, J. P. (2020) · Biochemical Society Transactions · doi:10.1042/bst20190023 · Cited by 20
Huang, J., Zang, Q., Wen, Y., Pan, Z., Yao, Z., Huang, M., Huang, J., Chen, J., & Wang, R. (2021) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2021.103308 · Cited by 21
Targeting KRAS mutations with HLA class II-restricted TCRs for the treatment of solid tumors
Dillard, P., Casey, N. P., Pollmann, S., Vernhoff, P., Gaudernack, G., Kvalheim, G., Wälchli, S., & Inderberg, E. M. (2021) · OncoImmunology · doi:10.1080/2162402x.2021.1936757 · Cited by 20
Clinical Translation of Combined MAPK and Autophagy Inhibition in RAS Mutant Cancer
Lee, J. J., Jain, V., & Amaravadi, R. K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222212402 · Cited by 20
Li, Y., Pan, M., Lu, T., Yu, D., Liu, C., Wang, Z., & Hu, G. (2022) · Journal of Translational Medicine · doi:10.1186/s12967-022-03468-7 · Cited by 20
Recent advances in the design of small molecular drugs with acrylamides covalent warheads
Liang, L., Zhang, Z., You, Q., & Guo, X. (2024) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2024.117902 · Cited by 20
Šereš, M., Spacayova, K., Sulová, Z., Špaldová, J., Breier, A., & Pavlíková, L. (2025) · Cancers · doi:10.3390/cancers17020248 · Cited by 28
Park, S., Kim, D., Song, J., & Joo, J. W. J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22063216 · Cited by 19
KRAS4A induces metastatic lung adenocarcinomas in vivo in the absence of the KRAS4B isoform
Salmón, M., Paniagua, G., Lechuga, C. G., Fernández-García, F., Zarzuela, E., Álvarez, R., Musteanu, M., Guerra, C. E., Caleiras, E. J., Muñoz, J., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2023112118 · Cited by 19
Cram, J. P., Wu, J., Kuninaka, S., Coover, R. A., Hennigan, R. F., Rizvi, T. A., Chaney, K. E., Ravindran, R., Cancelas, J. A., Spinner, R. J., et al. (2022) · eLife · doi:10.7554/elife.73511 · Cited by 19
Genomic and Epigenomic Landscape of Juvenile Myelomonocytic Leukemia
Fiñana, C., Gómez-Molina, N., Alonso-Moreno, S., & Belver, L. (2022) · Cancers · doi:10.3390/cancers14051335 · Cited by 20
Lv, M., Hu, W., Zhang, S., He, L., Hu, C., & Yang, S. (2022) · Cancer Letters · doi:10.1016/j.canlet.2022.215716 · Cited by 19
The rexinoid V-125 reduces tumor growth in preclinical models of breast and lung cancer
Reich, L. A., Moerland, J. A., Leal, A. S., Zhang, D., Carapellucci, S., Lockwood, B., Jurutka, P. W., Marshall, P. A., Wagner, C. E., & Liby, K. T. (2022) · Scientific Reports · doi:10.1038/s41598-021-04415-0 · Cited by 19
Pancreatic Tumorigenesis: Precursors, Genetic Risk Factors and Screening
Badheeb, M. A., Abdelrahim, A., Esmail, A., Umoru, G., Abboud, K., Al-Najjar, E., Rasheed, G. O., Alkhulaifawi, M., Abudayyeh, A., & Abdelrahim, M. (2022) · Current Oncology · doi:10.3390/curroncol29110686 · Cited by 20
Bao, H., Wang, W., Sun, H. B., & Chen, J. Z. (2023) · SAR and QSAR in environmental research · doi:10.1080/1062936x.2023.2165542 · Cited by 18
Kazi, A., Ranjan, A., Vasantha Kumar, M. V., Agianian, B., Chavez, M. G., Vudatha, V., Wang, R., Vangipurapu, R., Chen, L., Kennedy, P., et al. (2023) · Cancer Research Communications · doi:10.1158/2767-9764.crc-23-0222 · Cited by 16
Advances in the role and mechanism of fibroblasts in fracture healing
Wang, H., Qi, L., Shema, C., Jiang, K.-Y., Ren, P., Wang, H., & Wang, L. (2024) · Frontiers in Endocrinology · doi:10.3389/fendo.2024.1350958 · Cited by 22
Circular RNAs in the KRAS pathway: Emerging players in cancer progression
Hussain, M. S., Moglad, E. H. O., Afzal, M., Bansal, P., Kaur, H., Deorari, M., Ali, H., Shahwan, M. J., Almalki, W. H., Kazmi, I. A., et al. (2024) · Pathology - Research and Practice · doi:10.1016/j.prp.2024.155259 · Cited by 21
Wu, Y., Cao, Y., Chen, L., Lai, X., Zhang, S., & Wang, S. (2024) · Biological Procedures Online · doi:10.1186/s12575-024-00245-2 · Cited by 20
Endogenous IQGAP1 and IQGAP3 do not functionally interact with Ras
Morgan, C. J., Hedman, A. C., Li, Z., & Sacks, D. B. (2019) · Scientific Reports · doi:10.1038/s41598-019-46677-9 · Cited by 19
Systemic MEK inhibition enhances the efficacy of 5-aminolevulinic acid-photodynamic therapy
Chelakkot, V. S., Som, J., Yoshioka, E., Rice, C. P. J., Rutihinda, S. G., & Hirasawa, K. (2019) · British Journal of Cancer · doi:10.1038/s41416-019-0586-3 · Cited by 19
A subset of flavaglines inhibits KRAS nanoclustering and activation
Yurugi, H., Zhuang, Y., Siddiqui, F. A., Hong, L., Rosigkeit, S., Zeng, Y., Hamdan, H. A., Bockamp, E., Zhou, Y., Abankwa, D., et al. (2020) · Journal of Cell Science · doi:10.1242/jcs.244111 · Cited by 20
Oncogenic N-Ras Mitigates Oxidative Stress–Induced Apoptosis of Hematopoietic Stem Cells
Ney, G. M., Yang, K. B., Ng, V., Liu, L., Zhao, M., Kuk, W., Alaka, L., Sampang, L., Ross, A., Jones, M. A., et al. (2021) · Cancer Research · doi:10.1158/0008-5472.can-20-0118 · Cited by 19
Mohmmed, E. A., Shousha, W. G., EL-Saiid, A. S., & Ramadan, S. S. (2021) · Asian Pacific Journal of Cancer Prevention · doi:10.31557/apjcp.2021.22.11.3513 · Cited by 19
Discovery of novel Quinazoline-based KRAS G12C inhibitors as potential anticancer agents
Li, L., Zhao, H., Peng, X., Liu, J., Mai, R., Chen, J., Lin, L., Chen, T., Yan, J., Shi, J., et al. (2022) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2022.116962 · Cited by 19
Shimizu, M., Shibuya, H., & Tanaka, N. (2022) · Scientific Reports · doi:10.1038/s41598-022-06916-y · Cited by 18
The Next Generation of KRAS Targeting: Reasons for Excitement and Concern
Akhave, N. S., Biter, A. B., & Hong, D. S. (2022) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-22-0356 · Cited by 17
Past, Present, and Future Therapeutic Strategies for NF-1-Associated Tumors
Na, B. S., Shah, S. R., & Vasudevan, H. N. (2024) · Current Oncology Reports · doi:10.1007/s11912-024-01527-4 · Cited by 18
Tripathi, B. K., Hirsh, N. H., Qian, X., Durkin, M. E., Wang, D., Papageorge, A. G., Lake, R. G., Evrard, Y. A., Marcus, A. I., Ramalingam, S. S., et al. (2024) · Nature Cancer · doi:10.1038/s43018-024-00847-5 · Cited by 19
Zhang, F., Wang, B., Wu, M., Zhang, L., & Ji, M. Q. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1509173 · Cited by 20
Carvalho, B. C., de Oliveira, L. C., Rocha, C. D., Fernandes, H. D. B., de Oliveira, I. M., Leão, F. B., Valverde, T. M., Rego, I. M. G., Ghosh, S., & Silva, A. M. (2019) · Molecular Immunology · doi:10.1016/j.molimm.2019.02.015 · Cited by 22
Tisi, R., Gaponenko, V., Vanoni, M., & Sacco, E. (2020) · Biomolecules · doi:10.3390/biom10111535 · Cited by 18
Nikitidis, G., Carlsson, A. C., Karlsson, S., Campbell, A. D., Cook, C., Dai, K., Emtenäs, H., Jonson, A. C., Leek, H., Malmgren, M., et al. (2021) · Organic Process Research & Development · doi:10.1021/acs.oprd.1c00179 · Cited by 18
Targeting Mutated KRAS Genes to Treat Solid Tumours
Krishnan, T., Roberts‐Thomson, R., Broadbridge, V. T., & Price, T. J. (2021) · Molecular Diagnosis & Therapy · doi:10.1007/s40291-021-00564-0 · Cited by 18
Boosting Antitumor Immunity with an Expanded Neoepitope Landscape
Nagel, R., Pataskar, A., Champagne, J., & Agami, R. (2022) · Cancer Research · doi:10.1158/0008-5472.can-22-1525 · Cited by 21
Targeting protein conformations with small molecules to control protein complexes
Zacharioudakis, E., & Gavathiotis, E. (2022) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2022.07.002 · Cited by 19
Licoricidin combats gastric cancer by targeting the ICMT/Ras pathway in vitro and in vivo
Ma, H., Wu, F., Bai, Y., Wang, T., Ma, S., Guo, L., Liu, G., Leng, G., Kong, Y., & Zhang, Y. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.972825 · Cited by 21
Prostaglandin E2 in neuroblastoma: Targeting synthesis or signaling?
Hou, R., Yu, Y., & Jiang, J. (2022) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2022.113966 · Cited by 18
Liu, Y., Zhang, Q., Zou, M., Cui, J., Shi, X., Li, L., Wu, F., & Xu, X. (2023) · Veterinary Microbiology · doi:10.1016/j.vetmic.2023.109672 · Cited by 18
Martini, G., Ciardiello, D., Napolitano, S., Martinelli, E., Troiani, T., Latiano, T. P., Avallone, A., Normanno, N., Maïo, M. D., Maiello, E., et al. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1069370 · Cited by 18
Chen, X., Tang, G.-X., Dai, J., Dai, L.-T., Wu, T.-Y., Li, W., Ou, T., Huang, Z., Tan, J., & Chen, S.-B. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00094 · Cited by 18
The ErbB Signaling Network and Its Potential Role in Endometrial Cancer
Georgios, A., Styliara, I., Zarogianni, E., Lazurko, N., Valasoulis, G., Michail, G., & Adonakis, G. (2023) · Epigenomes · doi:10.3390/epigenomes7040024 · Cited by 21
Targeting RAF dimers in RAS mutant tumors: From biology to clinic
Yin, H., Tang, Q., Xia, H., & Bi, F. (2024) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2024.02.018 · Cited by 18
Chemical Proteomics–Guided Discovery of Covalent Ligands for Cancer Proteins
Zhang, X., & Cravatt, B. F. (2024) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-061421-041946 · Cited by 19
Connecting the dots: LncRNAs in the KRAS pathway and cancer
Maqbool, M., Hussain, M. S., Bisht, A. S., Kumari, A., Kamran, A., Sultana, A., Kumar, R., Khan, Y., & Gupta, G. (2024) · Pathology - Research and Practice · doi:10.1016/j.prp.2024.155570 · Cited by 19
RAS GTPase-dependent pathways in developmental diseases: old guys, new lads, and current challenges
Bustelo, X. R., Crespo, P., Fernández‐Pisonero, I., & Rodríguez‐Fdez, S. (2018) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2018.06.007 · Cited by 19
Zhang, F., Zakaria, S. M., Tabor, V., Singh, M., Tronnersjö, S., Goodwin, J., Selivanova, G., Bártek, J., Castell, A., & Larsson, L. (2018) · Cell Cycle · doi:10.1080/15384101.2018.1553339 · Cited by 18
Mutation-Specific and Common Phosphotyrosine Signatures of KRAS G12D and G13D Alleles
Tahir, R., Renuse, S., Udainiya, S., Madugundu, A. K., Cutler, J. A., Nirujogi, R. S., Na, C. H., Xu, Y., Wu, X., & Pandey, A. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00587 · Cited by 21
Maynard, K., LoPresti, M. A., Iacobas, I., Kan, P., & Lam, S. K. (2019) · Journal of Neurosurgery Pediatrics · doi:10.3171/2019.7.peds1976 · Cited by 18
Oncogenic K-Ras4B Dimerization Enhances Downstream Mitogen-activated Protein Kinase Signaling
Muratcioğlu, S., Aydın, C., Odabasi, E., Özdemir, E. S., Firat‐Karalar, E. N., Jang, H., Tsai, C., Nussinov, R., Kavaklı, İ. H., Gürsoy, A., et al. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.01.002 · Cited by 19
Analysis of Ras-effector interaction competition in large intestine and colorectal cancer context
Gaspar, V. I., Catozzi, S., Ternet, C., Luthert, P. J., & Kiel, C. (2020) · Small GTPases · doi:10.1080/21541248.2020.1724596 · Cited by 18
Cancer stem cell generation by silenced MAPK enhancing PI3K/AKT signaling
Hassan, G., Du, J., Afify, S. M., Seno, A., & Seno, M. (2020) · Medical Hypotheses · doi:10.1016/j.mehy.2020.109742 · Cited by 19
KRAS mutations are negatively correlated with immunity in colon cancer
Fu, X., Wang, X., Duanmu, J., Li, T., & Jiang, Q. (2020) · Aging · doi:10.18632/aging.202182 · Cited by 21
Ford, K. M., Panwala, R., Chen, D.-H., Portell, A. J., Palmer, N. D., & Mali, P. (2021) · Cell Systems · doi:10.1016/j.cels.2021.05.002 · Cited by 22
Xu, Z., Duan, F., Lu, H., Dragh, M. A. K., Xia, Y., Liang, H., & Hong, L. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-1215-4 · Cited by 19
Ji, J., Ye, P., Sun, N., Zhu, W., Yang, M., Yu, M., Yu, J., Zhang, H., Gao, Z., Zhang, N., et al. (2024) · 癌症：英文版 · doi:10.1002/cac2.12609 · Cited by 19
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
