Activation of Rac1, RhoA, and mitogen-activated protein kinases is required for Ras transformation

The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors

Ridley, A. J., & Hall, A. (1992) · Cell · doi:10.1016/0092-8674(92)90163-7 · Cited by 4,469 · see citing works

The small GTP-binding protein rac regulates growth factor-induced membrane ruffling

Ridley, A. J., Paterson, H. F., Johnston, C. L., Diekmann, D., & Hall, A. (1992) · Cell · doi:10.1016/0092-8674(92)90164-8 · Cited by 3,651 · see citing works

The GTPase superfamily: a conserved switch for diverse cell functions

Bourne, H. R., Sanders, D. A. R., & McCormick, F. P. (1990) · Nature · doi:10.1038/348125a0 · Cited by 2,336 · see citing works

Activation of MAP kinase kinase is necessary and sufficient for PC12 differentiation and for transformation of NIH 3T3 cells

Cowley, S. A. (1994) · Cell · doi:10.1016/0092-8674(94)90133-3 · Cited by 1,988 · see citing works

Phosphatidylinositol-3-OH kinase direct target of Ras

Rodriguez-Viciana, P., Warne, P. H., Dhand, R., Vanhaesebroeck, B., Gout, I., Fry, M. J., Waterfield, M. D., & Downward, J. (1994) · Nature · doi:10.1038/370527a0 · Cited by 1,954 · see citing works

Proteins regulating Ras and its relatives

Boguski, M. S., & McCormick, F. P. (1993) · Nature · doi:10.1038/366643a0 · Cited by 1,905 · see citing works

Transformation of Mammalian Cells by Constitutively Active MAP Kinase Kinase

Mansour, S. J., Matten, W. T., Hermann, A. S., Candia, J. M., Rong, S., Fukasawa, K., Woude, G. F. V., & Ahn, N. G. (1994) · Science · doi:10.1126/science.8052857 · Cited by 1,355 · see citing works

Mitogen-activated protein kinases p42mapk and p44mapk are required for fibroblast proliferation.

Pagès, G., Lenormand, P., L’Allemain, G., Chambard, J., Meloche, S., & Pouysségur, J. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.18.8319 · Cited by 984 · see citing works

Inhibition of NIH 3T3 Cell Proliferation by a Mutant ras Protein with Preferential Affinity for GDP

Feig, L. A., & Cooper, G. M. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.8.3235-3243.1988 · Cited by 799 · see citing works

The small GTP-binding protein rac regulates growth factor-induced membrane ruffling

Ridley, A. J., Paterson, H. F., Johnston, C. L., Diekmann, D., & Hall, A. (1992) · Trends in Cell Biology · doi:10.1016/0962-8924(92)90174-l · Cited by 756 · see citing works

Multiple ras functions can contribute to mammalian cell transformation

White, M. A., Nicolette, C. A., Minden, A., Polverino, A. J., Aelst, L. V., Karin, M., & Wigler, M. H. (1995) · Cell · doi:10.1016/0092-8674(95)90507-3 · Cited by 650 · see citing works

The pathway to signal achievement

Egan, S. E., & Weinberg, R. A. (1993) · Nature · doi:10.1038/365781a0 · Cited by 560 · see citing works

Biological and biochemical properties of human rasH genes mutated at codon 61

Der, C. J., Finkel, T., & Cooper, G. M. (1986) · Cell · doi:10.1016/0092-8674(86)90495-2 · Cited by 547 · see citing works

Regulation and properties of extracellular signal-regulated protein kinases 1 and 2 in vitro.

Robbins, D. J., Zhen, E., Owaki, H., Vanderbilt, C. A., Ebert, D. J., Geppert, T. D., & Cobb, M. H. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53507-9 · Cited by 499 · see citing works

Raf-1 protein kinase is required for growth of induced NIH/3T3 cells

Kölch, W., Heidecker, G., Lloyd, P. A., & Rapp, U. R. (1991) · Nature · doi:10.1038/349426a0 · Cited by 474 · see citing works

Serum-, TPA-, and Ras-induced expression from Ap-1/Ets-driven promoters requires Raf-1 kinase.Preprint

Bruder, J. T., Heidecker, G., & Rapp, U. R. (1992) · Genes & Development · doi:10.1101/gad.6.4.545 · Cited by 444 · see citing works

Catalysis of guanine nucleotide exchange on the CDC42Hs protein by the dbloncogene product

Hart, M. J., Eva, A., Evans, T., Aaronson, S. A., & Cerione, R. A. (1991) · Nature · doi:10.1038/354311a0 · Cited by 425 · see citing works

Activation of phosphoinositide 3-kinase activity by Cdc42Hs binding to p85.

Zheng, Y., Bagrodia, S., & Cerione, R. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32226-3 · Cited by 397 · see citing works

Critical tyrosine residues regulate the enzymatic and biological activity of Raf-1 kinase.

Fabian, J. R., Daar, I. O., & Morrison, D. K. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.11.7170 · Cited by 349 · see citing works

The Ras signal transduction pathway

Khosravi‐Far, R., & Der, C. J. (1994) · Cancer and Metastasis Reviews · doi:10.1007/bf00690419 · Cited by 348 · see citing works

Molecular cloning of cDNAs encoding the GAP-associated protein p190: Implications for a signaling pathway from ras to the nucleus

Settleman, J. E., Narasimhan, V., Foster, L. C., & Weinberg, R. A. (1992) · Cell · doi:10.1016/0092-8674(92)90454-k · Cited by 333 · see citing works

Cellular transformation and guanine nucleotide exchange activity are catalyzed by a common domain on the dbl oncogene product.

Hart, M. J., Eva, A., Zangrilli, D., Aaronson, S. A., Evans, T., Cerione, R. A., & Zheng, Y. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42313-1 · Cited by 315 · see citing works

Cooperative interaction of S. pombe proteins required for mating and morphogenesis

Chang, E. C., Barr, M. M., Wang, Y., et al. (1994) · Cell · doi:10.1016/0092-8674(94)90406-5 · Cited by 311 · see citing works

Activated Ras interacts with the Ral guanine nucleotide dissociation stimulator.

Hofer, F., Fields, S., Schneider, C., & Martin, G. S. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.23.11089 · Cited by 287 · see citing works

Protein-tyrosine kinases regulate the phosphorylation, protein interactions, subcellular distribution, and activity of p21ras GTPase-activating protein.

Moran, M. F., Polakis, P. G., McCormick, F. P., Pawson, T. J., & Ellis, C. A. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.4.1804 · Cited by 266 · see citing works

Identification of the guanine nucleotide dissociation stimulator for Ral as a putative effector molecule of R-ras, H-ras, K-ras, and Rap.

Spaargaren, M., & Bischoff, J. R. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.26.12609 · Cited by 265 · see citing works

ralGDS family members interact with the effector loop of ras p21.

Kikuchi, A., Demo, S. D., Ye, Z. H., Chen, Y. W., & Williams, L. T. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.11.7483 · Cited by 259 · see citing works

Two Distinct Raf Domains Mediate Interaction with Ras

Brtva, T. R., Drugan, J. K., Ghosh, S., Terrell, R. S., Campbell, S. L., Bell, R. M., & Der, C. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.17.9809 · Cited by 247 · see citing works

Mitogen-activated protein kinase/extracellular signal-regulated protein kinase activation by oncogenes, serum, and 12-O-tetradecanoylphorbol-13-acetate requires Raf and is necessary for transformation.

Troppmair, J., Bruder, J. T., Munoz, H., Lloyd, P. A., Kyriakis, J. M., Banerjee, P., Avruch, J., & Rapp, U. R. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37478-1 · Cited by 240 · see citing works

Ras-related GTPases and the cytoskeleton.

Hall, A. (1992) · Molecular Biology of the Cell · doi:10.1091/mbc.3.5.475 · Cited by 236 · see citing works

Guanine nucleotide exchange factors: Activators of the Ras superfamily of proteins

Quilliam, L. A., Khosravi‐Far, R., Huff, S. Y., & Der, C. J. (1995) · BioEssays · doi:10.1002/bies.950170507 · Cited by 221 · see citing works

ADP-ribosylation of rho p21 inhibits lysophosphatidic acid-induced protein tyrosine phosphorylation and phosphatidylinositol 3-kinase activation in cultured Swiss 3T3 cells.

Kumagai, N., Morii, N., Fujisawa, K., Nemoto, Y., & Narumiya, S. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74497-4 · Cited by 212 · see citing works

A signal chain of events

Roberts, T. M. (1992) · Nature · doi:10.1038/360534a0 · Cited by 211 · see citing works

The N‐terminal region of GAP regulates cytoskeletal structure and cell adhesion.

McGlade, J. C., Brunkhorst, B. A., Anderson, D. M., Mbamalu, G., Settleman, J. E., Dedhar, S., Rozakis-Adcock, M., Chen, L. B., & Pawson, T. J. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05976.x · Cited by 202 · see citing works

[40] Biological assays for Ras transformation

Clark, G. J., Cox, A. D., Graham, S. M., & Der, C. J. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(95)55042-9 · Cited by 198 · see citing works

Oncogenic Ras activates c-Jun via a separate pathway from the activation of extracellular signal-regulated kinases.

Westwick, J. K., Cox, A. D., Der, C. J., Cobb, M. H., Hibi, M., Karin, M., & Brenner, D. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.13.6030 · Cited by 187 · see citing works

Characterization of a guanine nucleotide dissociation stimulator for a ras‐related GTPase.

Albright, C. F., Giddings, B. W., Liu, J., Vito, M., & Weinberg, R. A. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05662.x · Cited by 174 · see citing works

Dbl and Vav mediate transformation via mitogen-activated protein kinase pathways that are distinct from those activated by oncogenic Ras.

Khosravi‐Far, R., Chrzanowska‐Wodnicka, M., Solski, P. A., Eva, A., Burridge, K., & Der, C. J. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.10.6848 · Cited by 136 · see citing works

R-Ras induces malignant, but not morphologic, transformation of NIH3T3 cells.

Cox, A. D., Brtva, T. R., Lowe, D. G., & Der, C. J. (1994) · PubMed · Cited by 111 · see citing works

Characterization and expression of the human rhoH12 gene product.

Avraham, H. K., & Weinberg, R. A. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.5.2058 · Cited by 108 · see citing works

Tumorigenic activity of rho genes from Aplysia californica.

Perona, R., Esteve, P., Jiménez, B., Ballestero, R. P., y Cajal, S. R., & Lacal, J. C. (1993) · PubMed · Cited by 106 · see citing works

Aberrant Function of the Ras-Related Protein TC21/R-Ras2 Triggers Malignant Transformation

Graham, S. M., Cox, A. D., Drivas, G., Rush, M. G., D’Eustachio, P., & Der, C. J. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.6.4108-4115.1994 · Cited by 97 · see citing works

Critical Tyrosine Residues Regulate the Enzymatic and Biological Activity of Raf-1 Kinase

Fabian, J. R., Darr, I. O., & Morrison, D. K. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.11.7170-7179.1993 · Cited by 89 · see citing works

Different structural organization of Ras and Rho effector domains.

Self, A. J., Paterson, H. F., & Hall, A. (1993) · PubMed · Cited by 84 · see citing works

Ras (CXXX) and Rab (CC/CXC) prenylation signal sequences are unique and functionally distinct.

Khosravi‐Far, R., Clark, G. J., Abe, K., et al. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35774-0 · Cited by 77 · see citing works

MAP kinase regulation — the oncogene connection

Leevers, S. J., & Marshall, C. J. (1992) · Trends in Cell Biology · doi:10.1016/0962-8924(92)90105-v · Cited by 76 · see citing works

Pathways of Ras Function: Connections to the Actin Cytoskeleton

Prendergast, G. C., & Gibbs, W. W. (1993) · Advances in cancer research · doi:10.1016/s0065-230x(08)60314-0 · Cited by 62 · see citing works

Protein-Tyrosine Kinases Regulate the Phosphorylation, Protein Interactions, Subcellular Distribution, and Activity of p21rasGTPase-Activating Protein

Moran, M. F., Polakis, P. G., McCormick, F. P., Pawson, T. J., & Ellis, C. A. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.4.1804-1812.1991 · Cited by 52 · see citing works

ralGDS Family Members Interact with the Effector Loop of ras p21

Kikuchi, A., Demo, S. D., Ye, Z.-H., et al. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.11.7483-7491.1994 · Cited by 47 · see citing works

Dbl and Vav Mediate Transformation via Mitogen-Activated Protein Kinase Pathways That are Distinct from Those Activated by Oncogenic Ras

Khosravi‐Far, R., Chrzanowska‐Wodnicka, M., Solski, P. A., et al. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.10.6848-6857.1994 · Cited by 38 · see citing works

What the papers say. Rho, rac and the actin cytoskeleton

Chrzanowska‐Wodnicka, M., & Burridge, K. (1992) · BioEssays · doi:10.1002/bies.950141110 · Cited by 23 · see citing works

Rac and Rho in control

Goldschmidt‐Clermont, P. J., Mendelsohn, M. E., & Gibbs, J. B. (1992) · Current Biology · doi:10.1016/0960-9822(92)90135-w · Cited by 22 · see citing works

Characterization and Expression of the Human rhoH12 Gene Product

Avraham, H. K., & Weinberg, R. A. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.5.2058-2066.1989 · Cited by 17 · see citing works

[23] Transcriptional activation analysis of oncogene function

Hauser, C. A., Der, C. J., & Cox, A. D. (1994) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(94)38025-2 · Cited by 13 · see citing works

p21 in cancer: Intricate networks and multiple activities

Abbas, T., & Dutta, A. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2657 · Cited by 2,712 · see citing works

Transcription factor AP-1 regulation by mitogen-activated protein kinase signal transduction pathways

Whitmarsh, A. J., & Davis, R. J. (1996) · Journal of Molecular Medicine · doi:10.1007/s001090050063 · Cited by 1,543 · see citing works

Ras oncogenes: split personalities

Karnoub, A. E., & Weinberg, R. A. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2438 · Cited by 1,467 · see citing works

KRAS: The Critical Driver and Therapeutic Target for Pancreatic Cancer

Waters, A. M., & Der, C. J. (2018) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a031435 · Cited by 875 · see citing works

Genetic analysis of Ras signalling pathways in cell proliferation, migration and survival

Drosten, M., Dhawahir, A., Sum, E. Y. M., Urosevic, J., Lechuga, C. G., Esteban, L. M., Castellano, E., Guerra, C., Santos, E., & Barbacid, M. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.7 · Cited by 347 · see citing works

Specificity and mechanism of action of EHT 1864, a novel small molecule inhibitor of Rac family small GTPases

Shutes, A., Onesto, C., Picard, V., Leblond, B., Schweighoffer, F., & Der, C. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703571200 · Cited by 336 · see citing works

The Ras-related Protein Rheb Is Farnesylated and Antagonizes Ras Signaling and Transformation

Clark, G. J., Kinch, M. S., Rogers-Graham, K., Sebti, S. M., Hamilton, A. D., & Der, C. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.16.10608 · Cited by 177 · see citing works

RAS mutations in human cancers: Roles in precision medicine

Murugan, A. K., Grieco, M., & Tsuchida, N. (2019) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2019.06.007 · Cited by 146 · see citing works

M-Ras/R-Ras3, a Transforming Ras Protein Regulated by Sos1, GRF1, and p120 Ras GTPase-activating Protein, Interacts with the Putative Ras Effector AF6

Quilliam, L. A., Castro, A. F., Rogers-Graham, K. S., Martin, C. B., Der, C. J., & Bi, C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.34.23850 · Cited by 119 · see citing works

RHOA-FAK is a required signaling axis for the maintenance of KRAS-driven lung adenocarcinomas

Konstantinidou, G., Ramadori, G., Torti, F., Kangasniemi, K., Ramirez, R. E., Cai, Y., Behrens, C., Dellinger, M. T., Brekken, R. A., Wistuba, I. I., et al. (2013) · Cancer Discovery · doi:10.1158/2159-8290.cd-12-0388 · Cited by 114 · see citing works

Genome-Wide CRISPR Screens Identify Multiple Synthetic Lethal Targets That Enhance KRASG12C Inhibitor Efficacy

Mukhopadhyay, S., Huang, H.-Y., Lin, Z., Ranieri, M., Li, S., Sahu, S., Liu, Y., Ban, Y., Guidry, K., Hu, H., et al. (2023) · Cancer Research · doi:10.1158/0008-5472.can-23-2729 · Cited by 105 · see citing works

Communication between the extracellular environment, cytoplasmic signalling cascades and the nuclear cell-cycle machinery

Peeper, D. S., & Bernards, R. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00319-0 · Cited by 36 · see citing works

RhoC GTPase Activation Assay

Lucey, M., Unger, H., & van Golen, K. L. (2010) · Journal of Visualized Experiments · doi:10.3791/2083-v · Cited by 2 · see citing works

RhoC GTPase Activation Assay

Lucey, M., Unger, H., & van Golen, K. L. (2010) · Journal of Visualized Experiments · doi:10.3791/2083 · Cited by 4 · see citing works

Rac1 and RhoA differentially regulate angiotensinogen gene expression in stretched cardiac fibroblasts

Verma, S. K., Lal, H., Golden, H. B., et al. (2010) · Cardiovascular Research · doi:10.1093/cvr/cvq385 · Cited by 54 · see citing works

RhoA/ROCK-mediated switching between Cdc42- and Rac1-dependent protrusion in MTLn3 carcinoma cells

Pertz, O. C., El‐Sibai, M., Condeelis, J. S., et al. (2020) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/21f6-jm82

Stretching Induces Overexpression of RhoA and Rac1 GTPases in Breast Cancer Cells

Yadav, S., Barton, M., & Nguyen, N. (2019) · Advanced Biosystems · doi:10.1002/adbi.201900222 · Cited by 18 · see citing works