The DOI matches its Crossref record; 60 of the 60 references it cites were found in a registry or an index.
Genetic analysis of Ras signalling pathways in cell proliferation, migration and survival
Open accessAbstract
We have used mouse embryonic fibroblasts (MEFs) devoid of Ras proteins to illustrate that they are essential for proliferation and migration, but not for survival, at least in these cells. These properties are unique to the Ras subfamily of proteins because ectopic expression of other Ras-like small GTPases, even when constitutively active, could not compensate for the absence of Ras proteins. Only constitutive activation of components of the Raf/Mek/Erk pathway was sufficient to sustain normal proliferation and migration of MEFs devoid of Ras proteins. Activation of the phosphatidylinositol 3-kinase (PI3K)/PTEN/Akt and Ral guanine exchange factor (RalGEF)/Ral pathways, either alone or in combination, failed to induce proliferation or migration of Rasless cells, although they cooperated with Raf/Mek/Erk signalling to reproduce the full response mediated by Ras signalling. In contrast to current hypotheses, Ras signalling did not induce proliferation by inducing expression of D-type Cyclins. Rasless MEFs had normal levels of Cyclin D1/Cdk4 and Cyclin E/Cdk2. However, these complexes were inactive. Inactivation of the pocket proteins or knock down of pRb relieved MEFs from their dependence on Ras signalling to proliferate.
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?
In the citing paper
“the ablation of all RAS isoform expression causes death of adult mice within a few weeks of induction (60, 61).”
From Expanding the Reach of Precision Oncology by Drugging All KRAS Mutants (2022) · cites this paper as [60]
In the citing paper
“The activated state of KRAS accumulating in vivo results in the activation of downstream signaling pathways and is associated with tumorigenesis, aggressive disease, and poor prognosis [14, 15].”
From Targeting KRAS mutant cancers: from druggable therapy to drug resistance (2022) · cites this paper as [15]
In the citing paper
“The activated state of KRAS accumulating in vivo results in the activation of downstream signaling pathways and is associated with tumorigenesis, aggressive disease, and poor prognosis [14, 15].”
From Targeting KRAS mutant cancers: from druggable therapy to drug resistance (2022) · cites this paper as [15]
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
Marshall, C. J. (1995) · Cell · doi:10.1016/0092-8674(95)90401-8 · Cited by 3,906
The evolution of phosphatidylinositol 3-kinases as regulators of growth and metabolism
Engelman, J. A., Luo, J., & Cantley, L. C. (2006) · Nature Reviews Genetics · doi:10.1038/nrg1879 · Cited by 3,330
Targeting the Raf-MEK-ERK mitogen-activated protein kinase cascade for the treatment of cancer
Roberts, P. J., & Der, C. J. (2007) · Oncogene · doi:10.1038/sj.onc.1210422 · Cited by 2,788
The ErbB signaling network: receptor heterodimerization in development and cancer
Olayioye, M. A., Neve, R. M., Lane, H. A., & Hynes, N. E. (2000) · The EMBO Journal · doi:10.1093/emboj/19.13.3159 · Cited by 2,489
Glycogen synthase kinase-3β regulates cyclin D1 proteolysis and subcellular localization
Diehl, J. A., Cheng, M., Roussel, M. F., & Sherr, C. J. (1998) · Genes & Development · doi:10.1101/gad.12.22.3499 · Cited by 2,130
RAS oncogenes: the first 30 years
Malumbres, M., & Barbacid, M. (2003) · Nature Reviews Cancer · doi:10.1038/nrc1097 · Cited by 1,902 · cited 1×
“These studies have illustrated how Ras proteins become activated by growth factor receptors and have unveiled those pathways implicated in mediating downstream signalling to their ultimate effectors (reviewed in Malumbres and Barbacid, 2003).”
BackgroundSelf-citationBeyond PTEN mutations: the PI3K pathway as an integrator of multiple inputs during tumorigenesis
Cully, M., You, H., Levine, A. J., & Mak, T. W. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1819 · Cited by 1,267
The RAF proteins take centre stage
Wellbrock, C., Karasarides, M., & Marais, R. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1498 · Cited by 1,223
Rodriguez‐Viciana, P., Warne, P. H., Khwaja, A., Marte, B. M., Pappin, D., Das, P., Waterfield, M. D., Ridley, A. J., & Downward, J. (1997) · Cell · doi:10.1016/s0092-8674(00)80226-3 · Cited by 1,060
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
Cited by
Sorted by citations
RAS Proteins and Their Regulators in Human Disease
Simanshu, D. K., Nissley, D. V., & McCormick, F. (2017) · Cell · doi:10.1016/j.cell.2017.06.009 · Cited by 1,943
ERK signalling: A master regulator of cell behaviour, life and fate
Lavoie, H., Gagnon, J., & Therrien, M. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0255-7 · Cited by 1,185
RAS-targeted therapies: is the undruggable drugged?
Moore, A. R., Rosenberg, S. C., McCormick, F., & Malek, S. (2020) · Nature Reviews Drug Discovery · doi:10.1038/s41573-020-0068-6 · Cited by 1,103
A Pericyte Origin of Spinal Cord Scar Tissue
Göritz, C., Dias, D. O., Tomilin, N., Barbacid, M., Shupliakov, O., & Frisén, J. (2011) · Science · doi:10.1126/science.1203165 · Cited by 858
Self-citationDirect small-molecule inhibitors of KRAS: from structural insights to mechanism-based design
Ostrem, J. M. L., & Shokat, K. M. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2016.139 · Cited by 641
Cellular mechanotransduction in health and diseases: from molecular mechanism to therapeutic targets
Di, X., Gao, X., Peng, L., Ai, J., Jin, X., Qi, S., Li, H., Wang, K., & Luo, D. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01501-9 · Cited by 715
Rapid non-uniform adaptation to conformation-specific KRAS(G12C) inhibition
Xue, J. Y., Zhao, Y., Aronowitz, J., Mai, T. T., Vides, A., Qeriqi, B., Kim, D., Li, C., de Stanchina, E., Mazutis, L., et al. (2020) · Nature · doi:10.1038/s41586-019-1884-x · Cited by 543
RAF-MEK-ERK pathway in cancer evolution and treatment
Ullah, R., Yin, Q., Snell, A. H., & Wan, L. (2022) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2021.05.010 · Cited by 553
Tumours with class 3 BRAF mutants are sensitive to the inhibition of activated RAS
Yao, Z., Yaeger, R., Rodrik-Outmezguine, V. S., Tao, A., Torres, N. M., Chang, M. T., Drosten, M., Zhao, H., Cecchi, F., Hembrough, T., et al. (2017) · Nature · doi:10.1038/nature23291 · Cited by 562
Self-citationIhle, N. T., Byers, L. A., Kim, E. S., Saintigny, P., Lee, J. J., Blumenschein, G. R., Tsao, A., Liu, S., Larsen, J. E., Wang, J., et al. (2012) · JNCI: Journal of the National Cancer Institute · doi:10.1093/jnci/djr523 · Cited by 532
Pan-KRAS Inhibitor Disables Oncogenic Signalling and Tumour Growth
Kim, D., Herdeis, L., Rudolph, D., Zhao, Y., Böttcher, J., Vides, A., Ayala-Santos, C. I., Pourfarjam, Y., Cuevas-Navarro, A., Xue, J. Y., et al. (2023) · Nature · doi:10.1038/s41586-023-06123-3 · Cited by 534
Nichols, R. J., Haderk, F., Stahlhut, C., Schulze, C. J., Hemmati, G., Wildes, D., Tzitzilonis, C., Mordec, K., Marquez, A., Romero, J., et al. (2018) · Nature Cell Biology · doi:10.1038/s41556-018-0169-1 · Cited by 415
Reducing Pericyte-Derived Scarring Promotes Recovery after Spinal Cord Injury
Dias, D. O., Kim, H., Holl, D., Solnestam, B. W., Lundeberg, J., Carlén, M., Göritz, C., & Frisén, J. (2018) · Cell · doi:10.1016/j.cell.2018.02.004 · Cited by 406
Concurrent inhibition of oncogenic and wild-type RAS-GTP for cancer therapy
Holderfield, M., Lee, B. J., Jiang, J., Tomlinson, A., Seamon, K. J., Mira, A., Patrucco, E., Goodhart, G., Dilly, J., Gindin, Y., et al. (2024) · Nature · doi:10.1038/s41586-024-07205-6 · Cited by 369
Ras Conformational Ensembles, Allostery, and Signaling
Lu, S., Jang, H., Muratcioglu, S., Gursoy, A., Keskin, O., Nussinov, R., & Zhang, J. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00542 · Cited by 355
Translational and therapeutic evaluation of RAS-GTP inhibition by RMC-6236 in RAS-driven cancers
Jiang, J., Jiang, L., Maldonato, B. J., Wang, Y., Holderfield, M., Aronchik, I., Winters, I. P., Salman, Z., Blaj, C., Menard, M., et al. (2024) · Cancer Discovery · doi:10.1158/2159-8290.cd-24-0027 · Cited by 343
McCormick, F. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-2662 · Cited by 320
Expanding the Reach of Precision Oncology by Drugging All KRAS Mutants
Hofmann, M. H., Gerlach, D., Misale, S., Petronczki, M., & Kraut, N. (2022) · Cancer Discovery · doi:10.1158/2159-8290.cd-21-1331 · Cited by 336
SHP2 inhibition prevents adaptive resistance to MEK inhibitors in multiple cancer models
Fedele, C., Ran, H., Diskin, B., Wei, W., Jen, J., Geer, M. J., Araki, K., Ozerdem, U., Simeone, D. M., Miller, G., et al. (2018) · Cancer Discovery · doi:10.1158/2159-8290.cd-18-0444 · Cited by 315
Therapeutic Strategies for Targeting Ras Proteins
Gysin, S., Salt, M. B., Young, A. E., & McCormick, F. (2011) · Genes & Cancer · doi:10.1177/1947601911412376 · Cited by 329
Lim, J. K. M., Delaidelli, A., Minaker, S. W., Zhang, H., Čolović, M., Yang, H., Negri, G. L., von Karstedt, S., Lockwood, W. W., Schaffer, P. C., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1821323116 · Cited by 321
Resident Neural Stem Cells Restrict Tissue Damage and Neuronal Loss After Spinal Cord Injury in Mice
Sabelström, H., Stenudd, M., Réu, P., Dias, D. O., Elfineh, M., Zdunek, S., Damberg, P., Göritz, C., & Frisén, J. (2013) · Science · doi:10.1126/science.1242576 · Cited by 314
Functional Specificity of Ras Isoforms: So Similar but So Different
Castellano, E., & Santos, E. (2011) · Genes & Cancer · doi:10.1177/1947601911408081 · Cited by 290
Self-citationKRAS Dimerization Impacts MEK Inhibitor Sensitivity and Oncogenic Activity of Mutant KRAS
Ambrogio, C., Köhler, J., Zhou, Z.-W., Wang, H., Paranal, R., Li, J., Capelletti, M., Caffarra, C., Li, S., Lv, Q., et al. (2018) · Cell · doi:10.1016/j.cell.2017.12.020 · Cited by 270
Allosteric Effects of the Oncogenic RasQ61L Mutant on Raf-RBD
Fetics, S., Guterres, H., Kearney, B. M., Buhrman, G., Ma, B., Nussinov, R., & Mattos, C. (2015) · Structure · doi:10.1016/j.str.2014.12.017 · Cited by 225
Targeting KRAS mutant cancers: from druggable therapy to drug resistance
Zhu, C., Guan, X., Zhang, X., Luan, X., Song, Z., Cheng, X., Zhang, W., & Qin, J.-J. (2022) · Molecular Cancer · doi:10.1186/s12943-022-01629-2 · Cited by 231
Pericyte-derived fibrotic scarring is conserved across diverse central nervous system lesions
Dias, D. O., Kalkitsas, J., Kelahmetoglu, Y., Estrada, C. P., Tatarishvili, J., Holl, D., Jansson, L., Banitalebi, S., Amiry-Moghaddam, M. R., Ernst, A., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25585-5 · Cited by 214
O’Hayre, M., Eichel, K., Avino, S., Zhao, X., Steffen, D. J., Feng, X., Kawakami, K., Aoki, J., Messer, K. S., Sunahara, R. K., et al. (2017) · Science Signaling · doi:10.1126/scisignal.aal3395 · Cited by 201
Metabolism and proliferation share common regulatory pathways in cancer cells
Fritz, V., & Fajas, L. (2010) · Oncogene · doi:10.1038/onc.2010.182 · Cited by 196
The current understanding on the impact of KRAS on colorectal cancer
Meng, M., Zhong, K., Jiang, T., Liu, Z., Kwan, H. Y., & Su, T. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111717 · Cited by 171
RAS Synthetic Lethal Screens Revisited: Still Seeking the Elusive Prize?
Downward, J. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-2180 · Cited by 168
NRAS-mutant melanoma: current challenges and future prospect
Muñoz‐Couselo, E., Zamora, E., Ortiz, C., Soberino-García, J., & Pérez-García, J. M. (2017) · OncoTargets and Therapy · doi:10.2147/ott.s117121 · Cited by 181
Potent and Selective Covalent Quinazoline Inhibitors of KRAS G12C
Zeng, M., Lu, J., Li, L., Feru, F., Quan, C., Gero, T. W., Ficarro, S. B., Xiong, Y., Ambrogio, C., Paranal, R. M., et al. (2017) · Cell Chemical Biology · doi:10.1016/j.chembiol.2017.06.017 · Cited by 136
Elevated FSP1 protects KRAS-mutated cells from ferroptosis during tumor initiation
Müller, F., Lim, J. K. M., Bebber, C. M., Seidel, E., Tishina, S., Dahlhaus, A., Stroh, J., Beck, J., Yapici, F. I., Nakayama, K., et al. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-01096-8 · Cited by 140
Mutant K-Ras Activation of the Proapoptotic MST2 Pathway Is Antagonized by Wild-Type K-Ras
Matallanas, D., Romano, D., Al‐Mulla, F., O’Neill, E. E., Al-Ali, W., Crespo, P., Doyle, B. J., Nixon, C., Sansom, O. J., Drosten, M., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.10.016 · Cited by 133
Self-citationTakashima, A., & Faller, D. V. (2013) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2013.764990 · Cited by 140
MAP kinase and autophagy pathways cooperate to maintain RAS mutant cancer cell survival
Lee, C.-S., Lee, L. C., Yuan, T. L., Chakka, S., Fellmann, C., Lowe, S. W., Caplen, N. J., McCormick, F., & Luo, J. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1817494116 · Cited by 126
A potent KRAS macromolecule degrader specifically targeting tumours with mutant KRAS
Bery, N., Miller, A., & Rabbitts, T. (2020) · Nature Communications · doi:10.1038/s41467-020-17022-w · Cited by 132
Functional characterization of a PROTAC directed against BRAF mutant V600E
Posternak, G., Tang, X., Maisonneuve, P., Jin, T., Lavoie, H., Daou, S., Orlicky, S. M., de Rugy, T. G., Caldwell, L., Chan, K., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0609-7 · Cited by 134
Navigating the ERK1/2 MAPK Cascade
Martín-Vega, A., & Cobb, M. H. (2023) · Biomolecules · doi:10.3390/biom13101555 · Cited by 127
Mechanisms of Resistance to KRASG12C Inhibitors
Dunnett-Kane, V., Nicola, P. A., Blackhall, F. H., & Lindsay, C. R. (2021) · Cancers · doi:10.3390/cancers13010151 · Cited by 122
Hermann, P., Sancho, P., Cañamero, M., Martinelli, P., Madriles, F., Michl, P., Gress, T., de Pascual, R., Gandía, L., Guerra, C., et al. (2014) · Gastroenterology · doi:10.1053/j.gastro.2014.08.002 · Cited by 113
Self-citationMontor, W. R., Salas, A. R. O. S. E., & de Melo, F. H. M. (2018) · Molecular Cancer · doi:10.1186/s12943-018-0792-2 · Cited by 118
Terrell, E. M., Durrant, D., Ritt, D. A., Sealover, N. E., Sheffels, E., Spencer-Smith, R., Esposito, D., Zhou, Y., Hancock, J. F., Kortum, R. L., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.09.004 · Cited by 110
Development of siRNA Payloads to Target KRAS -Mutant Cancer
Yuan, T. L., Fellmann, C., Lee, C.-S., Ritchie, C. D., Thapar, V., Lee, L. C., Hsu, D. J., Grace, D., Carver, J. O., Zuber, J., et al. (2014) · Cancer Discovery · doi:10.1158/2159-8290.cd-13-0900 · Cited by 113
“To test dose-dependent off-target effects of such Sensor-derived siRNAs, we transfected siKRAS_234 and siKRAS_355, which target both human and mouse KRAS, into Kras mouse embryonic fibroblasts (23) at 0.”
Role of mitofusin 2 (Mfn2) in controlling cellular proliferation
Chen, K., Dasgupta, A., Ding, J., Indig, F. E., Ghosh, P., & Longo, D. L. (2013) · The FASEB Journal · doi:10.1096/fj.13-230037 · Cited by 115
Schroeder, G. N., Petty, N. K., Mousnier, A., Harding, C. R., Vogrin, A. J., Wee, B. A., Fry, N. K., Harrison, T. G., Newton, H. J., Thomson, N. R., et al. (2010) · Journal of Bacteriology · doi:10.1128/jb.00778-10 · Cited by 110
Genetic Heterogeneity of BRAF Fusion Kinases in Melanoma Affects Drug Responses
Botton, T., Talevich, E., Mishra, V. K., Zhang, T., Shain, A. H., Berquet, C., Gagnon, A., Judson, R. L., Ballotti, R., Ribas, A., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.09.009 · Cited by 113
Hu, H., Cheng, R., Wang, Y., Wang, X., Wu, J., Kong, Y., Zhan, S., Zhou, Z., Zhu, H., Yu, R., et al. (2022) · Journal of Clinical Investigation · doi:10.1172/jci153470 · Cited by 111
K-Ras protein as a drug target
McCormick, F. (2016) · Journal of Molecular Medicine · doi:10.1007/s00109-016-1382-7 · Cited by 105
ERK signaling for cell migration and invasion
Samson, S. C., Khan, A. M., & Mendoza, M. C. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.998475 · Cited by 111
Drosten, M., Sum, E. Y. M., Lechuga, C. G., Simón-Carrasco, L., Jacob, H. K. C., García-Medina, R., Huang, S., Beijersbergen, R. L., Bernards, R., & Barbacid, M. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417549111 · Cited by 103
Self-citationKRAS G12V neoantigen specific T cell receptor for adoptive T cell therapy against tumors
Lu, D., Chen, Y., Jiang, M., Wang, J., Li, Y., Ma, K., Sun, W., Zheng, X., Qi, J., Jin, W., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42010-1 · Cited by 101
SOS GEFs in health and disease
Baltanás, F. C., Zarich, N., Rojas-Cabañeros, J. M., & Santos, E. (2020) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2020.188445 · Cited by 100
Self-citationSoriano, O., Pérez, M. A., Vicente‐Manzanares, M., & Castellano, E. (2021) · Genes · doi:10.3390/genes12060819 · Cited by 107
Self-citationA New View of Pathway-Driven Drug Resistance in Tumor Proliferation
Nussinov, R., Tsai, C., & Jang, H. (2017) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2017.02.001 · Cited by 94
Pan, X., Pei, J., Wang, A., Wen, S., Feng, L., Bu, F., Zhu, Y., Zhang, L., Wang, G., & Ouyang, L. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.12.022 · Cited by 95
Direct inhibition of RAS: Quest for the Holy Grail?
Spencer-Smith, R., & O’Bryan, J. P. (2017) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2017.12.005 · Cited by 90
A novel protein RASON encoded by a lncRNA controls oncogenic RAS signaling in KRAS mutant cancers
Cheng, R., Li, F., Zhang, M., Xia, X., Wu, J., Gao, X., Zhou, H., Zhang, Z., Huang, N., Yang, X., et al. (2022) · Cell Research · doi:10.1038/s41422-022-00726-7 · Cited by 87
Peschard, P., McCarthy, A., Leblanc-Dominguez, V., Yeo, M., Guichard, S., Stamp, G., & Marshall, C. J. (2012) · Current Biology · doi:10.1016/j.cub.2012.09.013 · Cited by 82
Critical role for PI3-kinase in regulating the use of proteins as an amino acid source
Palm, W., Araki, J., King, B., Dematteo, R. G., & Thompson, C. B. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1712726114 · Cited by 80
Kelleher, F. C., & McArthur, G. A. (2012) · The Cancer Journal · doi:10.1097/ppo.0b013e31824ba4df · Cited by 82
Lee, K., Fang, Z., Enomoto, M., Gasmi-Seabrook, G. M. C., Zheng, L., Koide, S., Ikura, M., & Marshall, C. B. (2020) · Angewandte Chemie International Edition · doi:10.1002/anie.202001758 · Cited by 78
Structure of the RAF1-HSP90-CDC37 complex reveals the basis of RAF1 regulation
García‐Alonso, S., Mesa, P., Ovejero, L. D. L. P., Aizpurua, G., Lechuga, C. G., Zarzuela, E., Santiveri, C. M., Sanclemente, M., Muñoz, J., Musteanu, M., et al. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.08.012 · Cited by 74
Self-citationAlvarez-Moya, B., López-Alcalá, C., Drosten, M., Bachs, O., & Agell, N. (2010) · Oncogene · doi:10.1038/onc.2010.298 · Cited by 75
Self-citationThe Function of RAS Mutation in Cancer and Advances in its Drug Research
Chen, S., Li, F., Xu, D., Hou, K., Fang, W., & Li, Y. (2019) · Current Pharmaceutical Design · doi:10.2174/1381612825666190506122228 · Cited by 75
Mlakar, V., Morel, E., Mlakar, S. J., Ansari, M., & Gumy‐Pause, F. (2021) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-021-01967-x · Cited by 72
Germline and sporadic cancers driven by the RAS pathway: parallels and contrasts
Dunnett-Kane, V., Burkitt-Wright, E., Blackhall, F. H., Malliri, A., Evans, D. G., & Lindsay, C. R. (2020) · Annals of Oncology · doi:10.1016/j.annonc.2020.03.291 · Cited by 66
Oncogenic KRAS signaling and YAP1/β-catenin: Similar cell cycle control in tumor initiation
Nussinov, R., Tsai, C., Jang, H., Korcsmáros, T., & Csermely, P. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.04.001 · Cited by 70
A structural model of a Ras–Raf signalosome
Mysore, V. P., Zhou, Z.-W., Ambrogio, C., Li, L., Kapp, J. N., Lu, C., Wang, Q., Tucker, M. R., Okoro, J. J., Nagy‐Davidescu, G., et al. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-021-00667-6 · Cited by 69
Allostery: Allosteric Cancer Drivers and Innovative Allosteric Drugs
Nussinov, R., Zhang, M., Maloney, R., Liu, Y., Tsai, C.-J., & Jang, H. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167569 · Cited by 66
Martin, C. A., Cullinane, C. M., Kirby, L., AbuHammad, S., Lelliott, E. J., Waldeck, K., Young, R. J., Brajanovski, N., Cameron, D. P., Walker, R., et al. (2017) · International Journal of Cancer · doi:10.1002/ijc.31220 · Cited by 70
Wang, Y., Ji, D., Lei, C., Chen, Y., Qiu, Y., Li, X., Li, M., Ni, D., Pu, J., Zhang, J., et al. (2021) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2021.01.044 · Cited by 64
Bronte, E., Bronte, G., Novo, G., Bronte, F., Bavetta, M. G., Re, G. L., Brancatelli, G., Bazan, V., Natoli, C., Novo, S., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.5853 · Cited by 64
Stopping the beating heart of cancer: KRAS reviewed
Herdeis, L., Gerlach, D., McConnell, D. B., & Kessler, D. (2021) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2021.06.013 · Cited by 65
Structural insight into the rearrangement of the switch I region in GTP-bound G12A K-Ras
Xu, S., Long, B. N., Boris, G. H., Chen, A., Ni, S., & Kennedy, M. A. (2017) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798317015418 · Cited by 62
Tanaka, T. U., & Rabbitts, T. H. (2010) · Oncogene · doi:10.1038/onc.2010.346 · Cited by 63
Functional Redundancy of Sos1 and Sos2 for Lymphopoiesis and Organismal Homeostasis and Survival
Baltanás, F. C., Pérez‐Andrés, M., Ginel-Picardo, A., Díaz, D., Jimeno, D., Liceras-Boillos, P., Kortum, R. L., Samelson, L. E., Órfão, A., & Santos, E. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01026-13 · Cited by 60
Self-citationEfficacy of CDK4 inhibition against sarcomas depends on their levels of CDK4 and p16ink4 mRNA
Pérez, M., Muñoz-Galván, S., Jiménez-García, M. P., Marín, J., & Carnero, A. (2015) · Oncotarget · doi:10.18632/oncotarget.5829 · Cited by 62
Evaluation of the selectivity and sensitivity of isoform- and mutation-specific RAS antibodies
Waters, A. M., Ozkan‐Dagliyan, I., Vaseva, A. V., Fer, N. D., Strathern, L. A., Hobbs, G. A., Tessier‐Cloutier, B., Gillette, W., Bagni, R., Whiteley, G., et al. (2017) · Science Signaling · doi:10.1126/scisignal.aao3332 · Cited by 62
Inactivation of Capicua in adult mice causes T-cell lymphoblastic lymphomaPreprint
Simón-Carrasco, L., Graña‐Castro, O., Salmón, M., Jacob, H. K. C., Gutiérrez, A., Jiménez, G., Drosten, M., & Barbacid, M. (2017) · Genes & Development · doi:10.1101/gad.300244.117 · Cited by 61
Self-citationZhou, Z.-W., Ambrogio, C., Bera, A. K., Li, Q., Li, X.-X., Li, L., Son, J., Gondi, S., Li, J., Campbell, E., et al. (2020) · Cancer Research · doi:10.1158/0008-5472.can-20-0448 · Cited by 60
Oncogenic mutant RAS signaling activity is rescaled by the ERK/MAPK pathway
Gillies, T. E., Pargett, M., Silva, J. M., Teragawa, C., McCormick, F. P., & Albeck, J. G. (2020) · Molecular Systems Biology · doi:10.15252/msb.20209518 · Cited by 54
Liu, R., Tang, J., Pan, M., Zhuang, Y., Zhang, Y., Liao, H., Zhao, D., Lei, Y., Lei, R.-X., Wang, S., et al. (2018) · Neurochemical Research · doi:10.1007/s11064-018-2558-z · Cited by 54
Mutations in RABL3 alter KRAS prenylation and are associated with hereditary pancreatic cancer
Nissim, S., Leshchiner, I., Mancias, J. D., Greenblatt, M. B., Maertens, O., Cassa, C. A., Rosenfeld, J. A., Cox, A. G., Hedgepeth, J., Wucherpfennig, J. I., et al. (2019) · Nature Genetics · doi:10.1038/s41588-019-0475-y · Cited by 54
Holl, D., Hau, W. F., Julien, A., Banitalebi, S., Kalkitsas, J., Savant, S., Llorens-Bobadilla, E., Hérault, Y., Pavlovic, G., Amiry-Moghaddam, M. R., et al. (2024) · Nature Neuroscience · doi:10.1038/s41593-024-01678-4 · Cited by 52
KRAS Switch Mutants D33E and A59G Crystallize in the State 1 Conformation
Lu, J., Bera, A. K., Gondi, S. R., & Westover, K. D. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00974 · Cited by 51
Liceras-Boillos, P., García‐Navas, R., Ginel-Picardo, A., Anta, B., Pérez‐Andrés, M., Lillo, C., Gómez, C., Jimeno, D., Fernández‐Medarde, A., Baltanás, F. C., et al. (2016) · Oncogene · doi:10.1038/onc.2016.169 · Cited by 49
Self-citationBisperoxovandium (pyridin‐2‐squaramide) targets both PTEN and ERK1/2 to confer neuroprotection
Zhang, Z., Chen, J., Han, X., Zhang, Y., Liao, H., Lei, R., Zhuang, Y., Wang, Z., Li, Z., Chen, J., et al. (2017) · British Journal of Pharmacology · doi:10.1111/bph.13727 · Cited by 49
Briffa, R., Um, I. H., Faratian, D., Zhou, Y. Y., Turnbull, A., Langdon, S. P., & Harrison, D. J. (2015) · PLoS ONE · doi:10.1371/journal.pone.0144708 · Cited by 51
A KRAS GTPase K104Q Mutant Retains Downstream Signaling by Offsetting Defects in Regulation
Yin, G., Kistler, S., George, S. D., Kuhlmann, N., Garvey, L. A., Huynh, M. V., Bagni, R., Lammers, M., Der, C. J., & Campbell, S. L. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.762435 · Cited by 48
Torres‐Collado, A. X., Knott, J., & Jazirehi, A. R. (2018) · Cancers · doi:10.3390/cancers10060157 · Cited by 48
Ras signaling is essential for skin development
Drosten, M., Lechuga, C. G., & Barbacid, M. (2014) · Oncogene · doi:10.1038/onc.2013.254 · Cited by 46
Self-citationKRAS Engages AGO2 to Enhance Cellular Transformation
Shankar, S., Pitchiaya, S., Malik, R., Kothari, V., Hosono, Y., Yocum, A. K., Gundlapalli, H., White, Y. N., Firestone, A. J., Cao, X., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.01.034 · Cited by 46
Sun, T., Li, M. Y., Zhang, Z. H., Wang, J. Y., Xing, Y., Ri, M., Jin, C. H., Xu, G. H., Piao, L. X., Jin, H. L., et al. (2021) · Phytotherapy Research · doi:10.1002/ptr.7103 · Cited by 45
Targeting the RAS upstream and downstream signaling pathway for cancer treatment
Hossain, M. A. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.176727 · Cited by 51
The Capicua tumor suppressor: a gatekeeper of Ras signaling in development and cancer
Simón-Carrasco, L., Jiménez, G., Barbacid, M., & Drosten, M. (2018) · Cell Cycle · doi:10.1080/15384101.2018.1450029 · Cited by 46
Self-citationKhaled, M., Gorfe, A. A., & Sayyed–Ahmad, A. (2019) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.9b05768 · Cited by 45
Roles of palmitoylation in structural long-term synaptic plasticity
Ji, B., & Skup, M. (2021) · Molecular Brain · doi:10.1186/s13041-020-00717-y · Cited by 44
Alberghina, L., Gaglio, D., Gelfi, C., Moresco, R. M., Mauri, G., Bertolazzi, P., Messa, C., Gilardi, M. C., Chiaradonna, F., & Vanoni, M. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00362 · Cited by 45
Metadata
- Authors
- Drosten, M., Dhawahir, A., Sum, E. Y. M., Urosevic, J., Lechuga, C. G., Esteban, L. M., Castellano, E., Guerra, C., Santos, E., & Barbacid, M.
- Affiliations
- Spanish National Cancer Research Centre (ES)
- Universidad de Salamanca (ES)
- Corresponding author
- Barbacid, Mariano
- ORCID
- Venue
- The EMBO Journal
- Published
- 2010-02-11
- Volume
- 29
- Issue
- 6
- Pages
- 1091-1104
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC2845279
- OpenAlex
- W2113609800
- Cited by
- 347
- References
- 60
- Citations by year
- 2026: 19 · 2025: 24 · 2024: 33 · 2023: 22 · 2022: 35 · 2021: 38 · 2020: 23 · 2019: 13 · 2018: 23 · 2017: 21 · 2016: 11 · 2015: 15 · 2014: 9 · 2013: 17 · 2012: 25
- FWCI
- 7.81
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- DIGITAL.CSIC (Spanish National Research Council (CSIC)) (submittedVersion)
- 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 › Melanoma and MAPK Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- Ras signaling, Ras proteins, cell proliferation, cell migration, cell survival, mouse embryonic fibroblasts, Raf/MEK/ERK pathway, PI3K/Akt signaling, cyclin D1/CDK4, cyclin E/CDK2, pocket proteins, retinoblastoma protein, cell cycle regulation
- MeSH terms
- Animals, Cell Movement, Cell Survival, Fibroblasts, Signal Transduction, ras Proteins, Phosphatidylinositol 3-Kinases, Extracellular Signal-Regulated MAP Kinases, raf Kinases, Cell Proliferation, Mice
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