Ras history: The saga continues

A genetic model for colorectal tumorigenesis

Fearon, E. R., & Vogelstein, B. (1990) · Cell · doi:10.1016/0092-8674(90)90186-i · Cited by 12,132 · see citing works

Mutations of the BRAF gene in human cancer

Davies, H., Bignell, G. R., Cox, C., Stephens, P., Edkins, S., Clegg, S., Teague, J., Woffendin, H., Garnett, M. J., Bottomley, W., et al. (2002) · Nature · doi:10.1038/nature00766 · Cited by 10,674 · see citing works

Cancer statistics, 2009

Jemal, A., Siegel, R., Ward, E., Hao, Y., Xu, J., & Thun, M. J. (2009) · CA: A Cancer Journal for Clinicians · doi:10.3322/caac.20006 · Cited by 9,709 · see citing works

An Integrated Genomic Analysis of Human Glioblastoma Multiforme

Parsons, D. W., Jones, S., Zhang, X., Lin, J. C.-H., Leary, R. J., Angenendt, P., Mankoo, P., Carter, H., Siu, I.-M., Gallia, G. L., et al. (2008) · Science · doi:10.1126/science.1164382 · Cited by 5,857 · see citing works

<i>IDH1</i> and <i>IDH2</i> Mutations in Gliomas

Yan, H., Parsons, D. W., Jin, G., McLendon, R., Rasheed, B. A., Yuan, W., Kos, I., Batinic-Haberle, I., Jones, S., Riggins, G. J., et al. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0808710 · Cited by 5,847 · see citing works

BAY 43-9006 Exhibits Broad Spectrum Oral Antitumor Activity and Targets the RAF/MEK/ERK Pathway and Receptor Tyrosine Kinases Involved in Tumor Progression and Angiogenesis

Wilhelm, S. M., Carter, C., Tang, L., Wilkie, D. P., McNabola, A., Rong, H., Chen, C., Zhang, X., Vincent, P. W., McHugh, M., et al. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-1443 · Cited by 4,019 · see citing works

Core Signaling Pathways in Human Pancreatic Cancers Revealed by Global Genomic Analyses

Jones, S., Zhang, X., Parsons, D. W., Lin, J. C.-H., Leary, R. J., Angenendt, P., Mankoo, P., Carter, H., Kamiyama, H., Jimeno, A., et al. (2008) · Science · doi:10.1126/science.1164368 · Cited by 3,969 · see citing works

Systematic RNA interference reveals that oncogenic KRAS-driven cancers require TBK1

Barbie, D. A., Tamayo, P., Boehm, J. S., Kim, S. Y., Moody, S. E., Dunn, I. F., Schinzel, A. C., Sandy, P., Meylan, E., Scholl, C., et al. (2009) · Nature · doi:10.1038/nature08460 · Cited by 3,869 · see citing works

Rab GTPases as coordinators of vesicle traffic

Stenmark, H. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2728 · Cited by 3,413 · see citing works

The Consensus Coding Sequences of Human Breast and Colorectal Cancers

Sjöblom, T., Jones, S., Wood, L. D., Parsons, D. W., Lin, J., Barber, T. D., Mandelker, D. L., Leary, R. J., Ptak, J., Silliman, N., et al. (2006) · Science · doi:10.1126/science.1133427 · Cited by 3,161 · see citing works

The Genomic Landscapes of Human Breast and Colorectal Cancers

Wood, L. D., Parsons, D. W., Jones, S., Lin, J., Sjöblom, T., Leary, R. J., Shen, D., Boca, S. M., Barber, T., Ptak, J., et al. (2007) · Science · doi:10.1126/science.1145720 · Cited by 2,833 · see citing works

Tumorigenic conversion of primary embryo fibroblasts requires at least two cooperating oncogenes

Land, H., Parada, L. F., & Weinberg, R. A. (1983) · Nature · doi:10.1038/304596a0 · Cited by 2,804 · see citing works

Trp53R172H and KrasG12D cooperate to promote chromosomal instability and widely metastatic pancreatic ductal adenocarcinoma in mice

Hingorani, S. R., Wang, L., Multani, A. S., Combs, C., Deramaudt, T. B., Hruban, R. H., Rustgi, A. K., Chang, S., & Tuveson, D. A. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.04.023 · Cited by 2,609 · see citing works

Creation of human tumour cells with defined genetic elements

Hahn, W. C., Counter, C. M., Lundberg, A. S., Beijersbergen, R. L., Brooks, M. W., & Weinberg, R. A. (1999) · Nature · doi:10.1038/22780 · Cited by 2,345 · see citing works

Most human carcinomas of the exocrine pancreas contain mutant c-K-ras genes

Almoguera, C., Shibata, D. K., Forrester, K., Wj, M., Arnheim, N., & Perucho, M. (1988) · Cell · doi:10.1016/0092-8674(88)90571-5 · Cited by 2,100 · see citing works

Mammalian Ras interacts directly with the serine/threonine kinase Raf.

Vojtek, A., Hollenberg, S., & Cooper, J. A. (1993) · Cell · doi:10.1016/0092-8674(93)90307-c · Cited by 1,971 · 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

RAS oncogenes: the first 30 years

Malumbres, M., & Barbacid, M. (2003) · Nature Reviews Cancer · doi:10.1038/nrc1097 · Cited by 1,902 · see citing works

Prevalence of ras gene mutations in human colorectal cancers

Bos, J. L., Fearon, E. R., Hamilton, S. R., Vries, M. V., BOOM, J. H. V., van der Eb, A. J., & Vogelstein, B. (1987) · Nature · doi:10.1038/327293a0 · Cited by 1,860 · see citing works

RAF inhibitors transactivate RAF dimers and ERK signalling in cells with wild-type BRAF

Poulikakos, P. I., Zhang, C., Bollag, G. E., Shokat, K. M., & Rosen, N. X. (2010) · Nature · doi:10.1038/nature08902 · Cited by 1,818 · see citing works

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 · see citing works

GEF means go: turning on RHO GTPases with guanine nucleotide-exchange factors

Rossman, K. L., Der, C. J., & Sondek, J. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1587 · Cited by 1,697 · see citing works

The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling

Lowenstein, E. J., Daly, R. J., Batzer, A., Li, W., Margolis, B. L., Lammers, R., Ullrich, A., Skolnik, E. Y., Bar‐Sagi, D., & Schlessinger, J. (1992) · Cell · doi:10.1016/0092-8674(92)90167-b · Cited by 1,632 · see citing works

RAF inhibitors prime wild-type RAF to activate the MAPK pathway and enhance growth

Hatzivassiliou, G., Song, K. W., Yen, I., Brandhuber, B. J., Anderson, D. J., Alvarado, R., Ludlam, M. J. C., Stokoe, D., Gloor, S. L., Vigers, G. P. A., et al. (2010) · Nature · doi:10.1038/nature08833 · Cited by 1,614 · see citing works

The Ras superfamily at a glance

Wennerberg, K., Rossman, K. L., & Der, C. J. (2005) · Journal of Cell Science · doi:10.1242/jcs.01660 · Cited by 1,549 · see citing works

Kinase-Dead BRAF and Oncogenic RAS Cooperate to Drive Tumor Progression through CRAF

Heidorn, S. J., Milagre, C. S., Whittaker, S. R., Nourry, A., Niculescu‐Duvaz, I., Dhomen, N. S., Hussain, J., Reis-Filho, J. S., Springer, C. J., Pritchard, C. A., et al. (2010) · Cell · doi:10.1016/j.cell.2009.12.040 · Cited by 1,468 · 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

Mechanism of activation of a human oncogene

Tabin, C. J., Bradley, S. M., Bargmann, C. I., Weinberg, R. A., Papageorge, A. G., Scolnick, E. M., Dhar, R., Lowy, D. R., & Chang, E. H. (1982) · Nature · doi:10.1038/300143a0 · Cited by 1,393 · see citing works

A point mutation is responsible for the acquisition of transforming properties by the T24 human bladder carcinoma oncogene

Reddy, E. P., Reynolds, R. K., Santos, E., & Barbacid, M. (1982) · Nature · doi:10.1038/300149a0 · Cited by 1,391 · see citing works

DNA related to the transforming gene(s) of avian sarcoma viruses is present in normal avian DNA

STEHELIN, D., VARMUS, H. E., BISHOP, J. M., & VOGT, P. K. (1976) · Nature · doi:10.1038/260170a0 · Cited by 1,321 · see citing works

Raf-1 activates MAP kinase-kinase

Kyriakis, J. M., App, H., Zhang, X., Banerjee, P. T., Brautigan, D. L., Rapp, U. R., & Avruch, J. (1992) · Nature · doi:10.1038/358417a0 · Cited by 1,263 · see citing works

Adenovirus early region 1A enables viral and cellular transforming genes to transform primary cells in culture

Ruley, H. E. (1983) · Nature · doi:10.1038/304602a0 · Cited by 1,248 · see citing works

A Cytoplasmic Protein Stimulates Normal N- <i>ras</i> p21 GTPase, But Does Not Affect Oncogenic Mutants

Trahey, M., & McCormick, F. (1987) · Science · doi:10.1126/science.2821624 · Cited by 1,211 · see citing works

Biochemical transfer of single-copy eucaryotic genes using total cellular DNA as donor

Wigler, M. H., Pellicer, À., Silverstein, S. J., & Axel, R. (1978) · Cell · doi:10.1016/0092-8674(78)90254-4 · Cited by 1,210 · see citing works

Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation

Egan, S. E., Giddings, B. W., Brooks, M. W., Buday, L., Sizeland, A. M., & Weinberg, R. A. (1993) · Nature · doi:10.1038/363045a0 · Cited by 1,200 · see citing works

In yeast, RAS proteins are controlling elements of adenylate cyclase

Toda, T., Uno, I., Ishikawa, T., Powers, S., Kataoka, T., Broek, D., Cameron, S., Broach, J. R., Matsumoto, K., & Wigler, M. H. (1985) · Cell · doi:10.1016/0092-8674(85)90305-8 · Cited by 1,108 · see citing works

Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor

Buday, L., & Downward, J. (1993) · Cell · doi:10.1016/0092-8674(93)90146-h · Cited by 1,064 · see citing works

Molecular Switch for Signal Transduction: Structural Differences Between Active and Inactive Forms of Protooncogenic ras Proteins

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 · see citing works

Detection of high incidence of K-ras oncogenes during human colon tumorigenesis

Forrester, K., Almoguera, C., Han, K., Grizzle, W. E., & Perucho, M. (1987) · Nature · doi:10.1038/327298a0 · Cited by 1,061 · see citing works

A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane

Hancock, J. F., Paterson, H., & Marshall, C. J. (1990) · Cell · doi:10.1016/0092-8674(90)90294-o · Cited by 1,042 · see citing works

Activated Kras and <i>Ink4a/Arf</i> deficiency cooperate to produce metastatic pancreatic ductal adenocarcinoma

Aguirre, A. J., Bardeesy, N., Sinha, M., Lopez, L., Tuveson, D. A., Horner, J., Redston, M. S., & DePinho, R. A. (2003) · Genes &amp; Development · doi:10.1101/gad.1158703 · Cited by 1,033 · see citing works

A Genome-wide RNAi Screen Identifies Multiple Synthetic Lethal Interactions with the Ras Oncogene

Luo, J., Emanuele, M. J., Li, D., Creighton, C. J., Schlabach, M. R., Westbrook, T. F., Wong, K.-K., & Elledge, S. J. (2009) · Cell · doi:10.1016/j.cell.2009.05.006 · Cited by 1,017 · see citing works

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 1,016 · see citing works

The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1

Rozakis-Adcock, M., Fernley, R. T., Wade, J. D., Pawson, T. J., & Bowtell, D. D. L. (1993) · Nature · doi:10.1038/363083a0 · Cited by 1,009 · see citing works

The GAP-related domain of the neurofibromatosis type 1 gene product interacts with ras p21

Martin, G. A., Viskoohil, D., Bollag, G. E., McCabe, P. C., Crosier, W. J., Haubruck, H., Conroy, L., Clark, R., O'Connell, P., Cawthon, R., et al. (1990) · Cell · doi:10.1016/0092-8674(90)90150-d · Cited by 983 · see citing works

Activation of Raf as a Result of Recruitment to the Plasma Membrane

Stokoe, D., Macdonald, S. G., Cadwallader, K. A., Symons, M. H., & Hancock, J. F. (1994) · Science · doi:10.1126/science.7811320 · Cited by 976 · see citing works

Complexes of Ras⋅GTP with Raf-1 and Mitogen-Activated Protein Kinase Kinase

Moodie, S. A., Willumsen, B. M., Weber, M. J., & Wolfman, A. (1993) · Science · doi:10.1126/science.8503013 · Cited by 968 · see citing works

Human EJ bladder carcinoma oncogene is homologue of Harvey sarcoma virus ras gene

Parada, L. F., Tabin, C. J., Shih, C., & Weinberg, R. A. (1982) · Nature · doi:10.1038/297474a0 · Cited by 947 · see citing works

Guanine-nucleotide-releasing factor hSos1 binds to Grb2 and links receptor tyrosine kinases to Ras signalling

Li, N., Batzer, A., Daly, R. J., Yajnik, V., Skolnik, E. Y., Chardin, P., Bar‐Sagi, D., Margolis, B. L., & Schlessinger, J. (1993) · Nature · doi:10.1038/363085a0 · Cited by 938 · see citing works

ras mediates nerve growth factor receptor modulation of three signal-transducing protein kinases: MAP kinase, Raf-1, and RSK

Wood, K. W., Sarnecki, C., Roberts, T. M., & Blenis, J. (1992) · Cell · doi:10.1016/0092-8674(92)90076-o · Cited by 903 · see citing works

K- and N-Ras Are Geranylgeranylated in Cells Treated with Farnesyl Protein Transferase Inhibitors

Whyte, D. B., Kirschmeier, P., Hockenberry, T. N., Nunez-Oliva, I., James, L., Catino, J. J., Bishop, W. R., & Pai, J.-K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.22.14459 · Cited by 884 · see citing works

Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation

PAI, E. F., Kabsch, W., Krengel, U., Holmes, K. C., John, J., & Wittinghofer, A. (1989) · Nature · doi:10.1038/341209a0 · Cited by 879 · see citing works

Progression model for pancreatic cancer.

Hruban, R. H., Goggins, M., Parsons, J., & Kern, S. E. (2000) · PubMed · Cited by 872 · see citing works

An Acylation Cycle Regulates Localization and Activity of Palmitoylated Ras Isoforms

Rocks, O., Peyker, A., Kahms, M., Verveer, P., Koerner, C., Lumbierres, M., Kuhlmann, J., Waldmann, H., Wittinghofer, A., & Bastiaens, P. (2005) · Science · doi:10.1126/science.1105654 · Cited by 866 · see citing works

Normal and oncogenic p21ras proteins bind to the amino-terminal regulatory domain of c-Raf-1

Zhang, X., Settleman, J. E., Kyriakis, J. M., Takeuchi-Suzuki, E., Elledge, S. J., Marshall, M. S., Bruder, J. T., Rapp, U. R., & Avruch, J. (1993) · Nature · doi:10.1038/364308a0 · Cited by 859 · see citing works

p21ras is modified by a farnesyl isoprenoid.

Casey, P. J., Solski, P. A., Der, C. J., & Buss, J. E. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.21.8323 · Cited by 856 · see citing works

The NF1 locus encodes a protein functionally related to mammalian GAP and yeast IRA proteins.

Ballester, R., Marchuk, D., Boguski, M., Saulino, A., Letcher, R., Wigler, M., & Collins, F. (1990) · Cell · doi:10.1016/0092-8674(90)90151-4 · Cited by 847 · see citing works

Requirement for ras proto-oncogene function during serum-stimulated growth of NIH 3T3 cells

Mulcahy, L. S., Smith, M. R., & Stacey, D. W. (1985) · Nature · doi:10.1038/313241a0 · Cited by 842 · see citing works

A Gene Expression Signature Associated with “K-Ras Addiction” Reveals Regulators of EMT and Tumor Cell Survival

Singh, A., Greninger, P., Rhodes, D., Koopman, L., Violette, S., Bardeesy, N., & Settleman, J. (2009) · Cancer Cell · doi:10.1016/j.ccr.2009.03.022 · Cited by 841 · see citing works

Human RAS Superfamily Proteins and Related GTPases

Colicelli, J. (2004) · Science s STKE · doi:10.1126/stke.2502004re13 · Cited by 837 · see citing works

Murine Sarcoma and Leukemia Viruses: Assay Using Clonal Lines of Contact-Inhibited Mouse Cells

Jainchill, J. L., Aaronson, S. A., & Todaro, G. J. (1969) · Journal of Virology · doi:10.1128/jvi.4.5.549-553.1969 · Cited by 826 · see citing works

Inhibition of purified p21 farnesyl:protein transferase by Cys-AAX tetrapeptides

Reiss, Y., Goldstein, J. L., Seabra, M. C., Casey, P. J., & Brown, M. S. (1990) · Cell · doi:10.1016/0092-8674(90)90242-7 · Cited by 817 · see citing works

Activation of the MAP kinase pathway by the protein kinase raf

Howe, L. R., Leevers, S. J., Gómez, N., Nakielny, S., Cohen, P., & Marshall, C. J. (1992) · Cell · doi:10.1016/0092-8674(92)90361-f · Cited by 801 · see citing works

The structural basis of the activation of Ras by Sos

Boriack-Sjodin, P. A., Margarit, S. M., Bar-Sagi, D., & Kuriyan, J. (1998) · Nature · doi:10.1038/28548 · Cited by 799 · see citing works

Human Sos1: a Guanine Nucleotide Exchange Factor for Ras that Binds to GRB2

Chardin, P., Camonis, J., Gale, N. W., Aelst, L. V., Schlessinger, J., Wigler, M. H., & Bar‐Sagi, D. (1993) · Science · doi:10.1126/science.8493579 · Cited by 799 · see citing works

Endogenous oncogenic K-rasG12D stimulates proliferation and widespread neoplastic and developmental defects

Tuveson, D. A., Shaw, A. T., Willis, N. A., Silver, D. P., Jackson, E. L., Chang, S., Mercer, K. L., Grochow, R., Hock, H., Crowley, D., et al. (2004) · Cancer Cell · doi:10.1016/s1535-6108(04)00085-6 · Cited by 798 · see citing works

Transforming genes of carcinomas and neuroblastomas introduced into mouse fibroblasts

Shih, C., Padhy, L. C., Murray, M. J., & Weinberg, R. A. (1981) · Nature · doi:10.1038/290261a0 · Cited by 791 · see citing works

Transforming genes of human bladder and lung carcinoma cell lines are homologous to the ras genes of Harvey and Kirsten sarcoma viruses.

Der, C. J., Krontiris, T. G., & Cooper, G. M. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.11.3637 · Cited by 785 · see citing works

Coexpression of MMTV/v-Ha-ras and MMTV/c-myc genes in transgenic mice: Synergistic action of oncogenes in vivo

Sinn, E., Muller, W. J., Pattengale, P. K., Tepler, I., Wallace, R., & Leder, P. (1987) · Cell · doi:10.1016/0092-8674(87)90449-1 · Cited by 784 · see citing works

The RASopathies: developmental syndromes of Ras/MAPK pathway dysregulation

Tidyman, W. E., & Rauen, K. A. (2009) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2009.04.001 · Cited by 780 · see citing works

The GTP-binding protein Ran/TC4 is required for protein import into the nucleus

Moore, M. S., & Blobel, G. (1993) · Nature · doi:10.1038/365661a0 · Cited by 766 · see citing works

Endomembrane Trafficking of Ras

Choy, E., Chiu, V. K., Silletti, J., Feoktistov, M., Morimoto, T., Michaelson, D., Ivanov, I. E., & Philips, M. R. (1999) · Cell · doi:10.1016/s0092-8674(00)80607-8 · Cited by 754 · see citing works

Germline KRAS mutations cause Noonan syndrome

Schubbert, S., Zenker, M., Rowe, S. L., Böll, S., Klein, C., Bollag, G., van der Burgt, I., Musante, L., Kalscheuer, V., Wehner, L.-E., et al. (2006) · Nature Genetics · doi:10.1038/ng1748 · Cited by 730 · see citing works

Direct interaction of Ras and the amino-terminal region of Raf-1 in vitro

Warne, P. H., Vician, P. R., & Downward, J. (1993) · Nature · doi:10.1038/364352a0 · Cited by 729 · see citing works

The p21 src genes of Harvey and Kirsten sarcoma viruses originate from divergent members of a family of normal vertebrate genes

Ellis, R. W., DeFeo, D., Shih, T. Y., Gonda, M. A., Young, H. A., Tsuchida, N., Lowy, D. R., & Scolnick, E. M. (1981) · Nature · doi:10.1038/292506a0 · Cited by 723 · see citing works

Induction of mammary carcinomas in rats by nitroso-methylurea involves malignant activation of H-ras-1 locus by single point mutations

Sukumar, S. V., Notario, V., Martı́n-Zanca, D., & Barbacid, M. (1983) · Nature · doi:10.1038/306658a0 · Cited by 706 · see citing works

Activation of the T24 bladder carcinoma transforming gene is linked to a single amino acid change

Taparowsky, E. J., Suard, Y. M. L., Fasano, O., Shimizu, K., Goldfarb, M. P., & Wigler, M. H. (1982) · Nature · doi:10.1038/300762a0 · Cited by 703 · see citing works

Comparative biochemical properties of normal and activated human ras p21 protein

McGrath, J. P., Capon, D. J., Goeddel, D. V., & Levinson, A. D. (1984) · Nature · doi:10.1038/310644a0 · Cited by 699 · see citing works

The catalytic domain of the neurofibromatosis type 1 gene product stimulates ras GTPase and complements ira mutants of S. cerevisiae

Xu, G., Lin, B. K., Tanaka, K., Dunn, D. M., Wood, D. R., Gesteland, R. F., White, R. L., Weiss, R. B., & Tamanoi, F. (1990) · Cell · doi:10.1016/0092-8674(90)90149-9 · Cited by 681 · see citing works

Germline mutations in HRAS proto-oncogene cause Costello syndrome

Aoki, Y., Niihori, T., Kawame, H., Kurosawa, K., Ohashi, H., Tanaka, Y., Filocamo, M., Kato, K., Suzuki, Y., Kure, S., et al. (2005) · Nature Genetics · doi:10.1038/ng1641 · Cited by 678 · see citing works

RasGRP, a Ras Guanyl Nucleotide- Releasing Protein with Calcium- and Diacylglycerol-Binding Motifs

Ebinu, J. O., Bottorff, D. A., Chan, E. Y. W., Stang, S. L., Dunn, R. J., & Stone, J. C. (1998) · Science · doi:10.1126/science.280.5366.1082 · Cited by 675 · see citing works

<i>Smad4</i> is dispensable for normal pancreas development yet critical in progression and tumor biology of pancreas cancer

Bardeesy, N., Cheng, K.-H., Berger, J. H., Chu, G. C., Pahler, J., Olson, P., Hezel, A. F., Horner, J., Lauwers, G. Y., Hanahan, D., et al. (2006) · Genes &amp; Development · doi:10.1101/gad.1478706 · Cited by 674 · see citing works

Activation of Mitogen-Activated Protein Kinase Kinase by v-Raf in NIH 3T3 Cells and in Vitro

Dent, P., Haser, W. G., Haystead, T., Vincent, L. A., Roberts, T. M., & Sturgill, T. W. (1992) · Science · doi:10.1126/science.1326789 · Cited by 668 · see citing works

Requirement for c-ras proteins during viral oncogene transformation

Smith, M. R., DeGudicibus, S. J., & Stacey, D. W. (1986) · Nature · doi:10.1038/320540a0 · Cited by 653 · see citing works

Cloning of bovine GAP and its interaction with oncogenic ras p21

Vogel, U. S., Dixon, R. A. F., Schaber, M. D., Diehl, R. E., Marshall, M. S., Scolnick, E. M., Sigal, I. S., & Gibbs, W. W. (1988) · Nature · doi:10.1038/335090a0 · Cited by 649 · see citing works

Multicenter Phase II Study of the Oral MEK Inhibitor, CI-1040, in Patients With Advanced Non-Small-Cell Lung, Breast, Colon, and Pancreatic Cancer

Rinehart, J., Adjei, A. A., LoRusso, P. M., Waterhouse, D., Hecht, J. R., Natale, R. B., Hamid, O., Varterasian, M., Asbury, P., Kaldjian, E. P., et al. (2004) · Journal of Clinical Oncology · doi:10.1200/jco.2004.01.185 · Cited by 645 · see citing works

Analysis of the Small GTPase Gene Superfamily of Arabidopsis

Vernoud, V., Horton, A. C., Yang, Z., & Nielsen, E. (2003) · PLANT PHYSIOLOGY · doi:10.1104/pp.013052 · Cited by 636 · see citing works

The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with RaplA and a GTP analogue

Nassar, N. N., Horn, G., Herrmann, C., Scherer, A., McCormick, F. P., & Wittinghofer, A. (1995) · Nature · doi:10.1038/375554a0 · Cited by 635 · see citing works

Benzodiazepine Peptidomimetics: Potent Inhibitors of Ras Farnesylation In Animal Cells

James, G. L., Goldstein, J. L., Brown, M. S., Rawson, T. E., Somers, T. C., McDowell, R. S., Crowley, C. W., Lucas, B. K., Levinson, A. D., & Marsters, J. C. (1993) · Science · doi:10.1126/science.8316834 · Cited by 630 · see citing works

KRAS codon 12 mutations occur very frequently in pancreatic adenocarcinomas

Smit, V. T. H. B. M., Boot, A. J., de Vries-Smits, A. M. M., Fleuren, G. J., Cornelisse, C. J., & Bos, J. L. (1988) · Nucleic Acids Research · doi:10.1093/nar/16.16.7773 · Cited by 625 · see citing works

T24 human bladder carcinoma oncogene is an activated form of the normal human homologue of BALB- and Harvey-MSV transforming genes

Santos, E., Tronick, S. R., Aaronson, S. A., Pulciani, S., & Barbacid, M. (1982) · Nature · doi:10.1038/298343a0 · Cited by 624 · see citing works

Complex formation between RAS and RAF and other protein kinases.

Aelst, L. V., Barr, M. M., Marcus, S., Polverino, A. J., & Wigler, M. H. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.13.6213 · Cited by 623 · see citing works

Intrinsic GTPase activity distinguishes normal and oncogenic ras p21 molecules.

Gibbs, W. W., Sigal, I. S., Poe, M., & Scolnick, E. M. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.18.5704 · Cited by 611 · see citing works

Differential effects of oncogenic K-Ras and N-Ras on proliferation, differentiation and tumor progression in the colon

Haigis, K. M., Kendall, K. R., Wang, Y., Cheung, A., Haigis, M. C., Glickman, J. N., Niwa-Kawakita, M., Sweet-Cordero, A., Sebolt-Leopold, J., Shannon, K. M., et al. (2008) · Nature Genetics · doi:10.1038/ng.115 · Cited by 610 · see citing works

Enumeration of the Simian Virus 40 Early Region Elements Necessary for Human Cell Transformation

Hahn, W. C., Dessain, S. K., Brooks, M. W., King, J. E., Elenbaas, B., Sabatini, D. M., DeCaprio, J. A., & Weinberg, R. A. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.7.2111-2123.2002 · Cited by 603 · see citing works

Crystal Structure and Functional Analysis of Ras Binding to Its Effector Phosphoinositide 3-Kinase γ

Pacold, M. E., Suire, S., Perišić, O., Lara‐González, S., Davis, C. T., Walker, E. H., Hawkins, P. T., Stephens, L., Eccleston, J. F., & Williams, R. L. (2000) · Cell · doi:10.1016/s0092-8674(00)00196-3 · Cited by 603 · see citing works

Germline KRAS and BRAF mutations in cardio-facio-cutaneous syndrome

Niihori, T., Aoki, Y., Narumi, Y., Neri, G., Cavé, H., Verloès, A., Okamoto, N., Hennekam, R. C. M., Gillessen‐Kaesbach, G., Wieczorek, D., et al. (2006) · Nature Genetics · doi:10.1038/ng1749 · Cited by 599 · see citing works

Ras signalling on the endoplasmic reticulum and the Golgi

Chiu, V. K., Bivona, T., Hach, A., Sajous, J. B., Silletti, J., Wiener, H., Johnson, R. L., Cox, A. D., & Philips, M. R. (2002) · Nature Cell Biology · doi:10.1038/ncb783 · Cited by 594 · see citing works

Tumorigenic transformation of mammalian cells induced by a normal human gene homologous to the oncogene of Harvey murine sarcoma virus

Chang, E. H., Furth, M. E., Scolnick, E. M., & Lowy, D. R. (1982) · Nature · doi:10.1038/297479a0 · Cited by 588 · see citing works

The p21 ras C-terminus is required for transformation and membrane association

Willumsen, B. M., Christensen, A., Hubbert, N. L., Papageorge, A. G., & Lowy, D. R. (1984) · Nature · doi:10.1038/310583a0 · Cited by 584 · see citing works

Selective Inhibition of ras -Dependent Transformation by a Farnesyltransferase Inhibitor

Kohl, N. E., Mosser, S. D., DeSolms, S. J., Giuliani, E. A., Pompliano, D. L., Graham, S. L., Smith, R. L., Scolnick, E. M., Oliff, A. I., & Gibbs, W. W. (1993) · Science · doi:10.1126/science.8316833 · Cited by 579 · see citing works

Tumor induction by an endogenous K-ras oncogene is highly dependent on cellular context

Guerra, C. E., Mijimolle, N., Dhawahir, A., Dubus, P. R., Barradas, M., Serrano, M., Campuzano, V., & Barbacid, M. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00191-0 · Cited by 566 · see citing works

Grb2 mediates the EGF-dependent activation of guanine nucleotide exchange on Ras

Gale, N. W., Kaplan, S., Lowenstein, E. J., Schlessinger, J., & Bar‐Sagi, D. (1993) · Nature · doi:10.1038/363088a0 · Cited by 563 · see citing works

Protein kinase A phosphorylation of RhoA mediates the morphological and functional effects of cyclic AMP in cytotoxic lymphocytes

Lang, P., Gesbert, F., Delespine‐Carmagnat, M., Stancou, R., Pouchelet, M., & Bertoglio, J. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00383.x · Cited by 558 · see citing works

Spatio-temporal images of growth-factor-induced activation of Ras and Rap1

Mochizuki, N., Yamashita, S., Kurokawa, K., Ohba, Y., Nagai, T., Miyawaki, A., & Matsuda, M. (2001) · Nature · doi:10.1038/35082594 · Cited by 556 · see citing works

An Unidentified Virus which causes the Rapid Production of Tumours in Mice

Harvey, J. J. (1964) · Nature · doi:10.1038/2041104b0 · Cited by 554 · see citing works

Activation of Ki-ras2 gene in human colon and lung carcinomas by two different point mutations

Capon, D. J., Seeburg, P. H., McGrath, J. P., Hayflick, J. S., Edman, U., Levinson, A. D., & Goeddel, D. V. (1983) · Nature · doi:10.1038/304507a0 · Cited by 551 · 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

The protein cofactor necessary for ADP-ribosylation of Gs by cholera toxin is itself a GTP binding protein.

Kahn, R., & Gilman, A. G. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)57489-0 · Cited by 545 · see citing works

Inhibition of nuclear protein import by nonhydrolyzable analogues of GTP and identification of the small GTPase Ran/TC4 as an essential transport factor [published erratum appears in J Cell Biol 1994 Jan;124(1-2):217]

Melchior, F. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.123.6.1649 · Cited by 544 · see citing works

Inhibition of farnesyltransferase induces regression of mammary and salivary carcinomas in ras transgenic mice

Kohl, N. E., Omer, C. A., Conner, M. W., Anthony, N. J., Davide, J. P., DeSolms, S. J., Giuliani, E. A., Gomez, R. P., Graham, S. L., Hamilton, K., et al. (1995) · Nature Medicine · doi:10.1038/nm0895-792 · Cited by 540 · see citing works

K-ras is an essential gene in the mouse with partial functional overlap with N-rasPreprint

Johnson, L., Greenbaum, D. C., Cichowski, K. M., Mercer, K. L., Murphy, E. A., Schmitt, E. S., Bronson, R. T., Umanoff, H., Edelmann, W., Kucherlapati, R., et al. (1997) · Genes & Development · doi:10.1101/gad.11.19.2468 · Cited by 540 · see citing works

Synthetic Lethal Interaction between Oncogenic KRAS Dependency and STK33 Suppression in Human Cancer Cells

Scholl, C., Fröhling, S., Dunn, I. F., Schinzel, A. C., Barbie, D. A., Kim, S. Y., Silver, S. J., Tamayo, P., Wadlow, R. C., Ramaswamy, S., et al. (2009) · Cell · doi:10.1016/j.cell.2009.03.017 · Cited by 539 · see citing works

A Drosophila SH2-SH3 adaptor protein implicated in coupling the sevenless tyrosine kinase to an activator of Ras guanine nucleotide exchange, Sos

Olivier, J. P. (1993) · Cell · doi:10.1016/0092-8674(93)90170-u · Cited by 537 · see citing works

The product of ras is a GTPase and the T24 oncogenic mutant is deficient in this activity

Sweet, R. W., Yokoyama, S., Kamata, T., Feramisco, J. R., Rosenberg, M. J., & Gross, M. S. (1984) · Nature · doi:10.1038/311273a0 · Cited by 532 · see citing works

Mutational Activation of the K-rasOncogene

Rodenhuis, S., van de Wetering, M. L., Mooi, W. J., Evers, S. G., van Zandwijk, N., & Bos, J. L. (1987) · New England Journal of Medicine · doi:10.1056/nejm198710083171504 · Cited by 532 · see citing works

Genetic and Pharmacological Suppression of Oncogenic Mutations in RAS Genes of Yeast and Humans

Schafer, W. R., Kim, R., Sterne, R. E., Thorner, J. W., Kim, S., & Rine, J. (1989) · Science · doi:10.1126/science.2569235 · Cited by 530 · see citing works

Three-Dimensional Structure of an Oncogene Protein: Catalytic Domain of Human c-H- ras P21

de Vos, A. M., Tong, L., Milburn, M. V., Matias, P. M., Jancarik, J., Noguchi, S., Nishimura, S., Miura, K., Ohtsuka, E., & Kim, S. (1988) · Science · doi:10.1126/science.2448879 · Cited by 529 · see citing works

A novel ras-related gene family

Madaule, P., & Axel, R. (1985) · Cell · doi:10.1016/0092-8674(85)90058-3 · Cited by 502 · see citing works

Passage of phenotypes of chemically transformed cells via transfection of DNA and chromatin.

Shih, C., Shilo, B., Goldfarb, M. P., Dannenberg, A. J., & Weinberg, R. A. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.11.5714 · Cited by 487 · see citing works

Time-resolved X-ray crystallographic study of the conformational change in Ha-Ras p21 protein on GTP hydrolysis

Schlichting, I., Almo, S. C., Rapp, G., Wilson, K. S., Petratos, K., Lentfer, A., Wittinghofer, A., Kabsch, W., PAI, E. F., Petsko, G. A., et al. (1990) · Nature · doi:10.1038/345309a0 · Cited by 487 · see citing works

Homologies Between Signal Transducing G Proteins and ras Gene Products

Hurley, J. B., Simon, M. I., Teplow, D. B., Robishaw, J. D., & Gilman, A. G. (1984) · Science · doi:10.1126/science.6436980 · Cited by 483 · see citing works

A CAAX or a CAAL motif and a second signal are sufficient for plasma membrane targeting of ras proteins.

Hancock, J. F., Cadwallader, K. A., Paterson, H., & Marshall, C. J. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb04979.x · Cited by 482 · see citing works

Oncogenes in solid human tumours

Pulciani, S., Santos, E., Lauver, A. V., Long, L. K., Aaronson, S. A., & Barbacid, M. (1982) · Nature · doi:10.1038/300539a0 · Cited by 479 · see citing works

The S. cerevisiae CDC25 gene product regulates the RAS/adenylate cyclase pathway

Broek, D., Toda, T., Michaeli, T., Levin, L. R., Birchmeier, C., Zoller, M. J., Powers, S., & Wigler, M. H. (1987) · Cell · doi:10.1016/0092-8674(87)90076-6 · Cited by 478 · see citing works

Molecular Cloning of Two Types of GAP Complementary DNA from Human Placenta

Trahey, M., Wong, G. A., Halenbeck, R., Rubinfeld, B., Martin, G. A., Ladner, M. B., Long, C. M., Crosier, W. J., Watt, K., Koths, K. E., et al. (1988) · Science · doi:10.1126/science.3201259 · Cited by 468 · see citing works

H-ras, K-ras, and inner plasma membrane raft proteins operate in nanoclusters with differential dependence on the actin cytoskeleton

Plowman, S. J., Muncke, C., Parton, R. G., & Hancock, J. F. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504114102 · Cited by 468 · see citing works

Structure and biological activity of v-raf, a unique oncogene transduced by a retrovirus.

Rapp, U. R., Goldsborough, M. D., Mark, G. E., Bonner, T. I., Groffen, J., Reynolds, F. H., & Stephenson, J. R. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.14.4218 · Cited by 467 · see citing works

PKC Regulates a Farnesyl-Electrostatic Switch on K-Ras that Promotes its Association with Bcl-Xl on Mitochondria and Induces Apoptosis

Bivona, T. G., Quatela, S. E., Bodemann, B. O., Ahearn, I. M., Soskis, M. J., Mor, A., Miura, J., Wiener, H. H., Wright, L. P., Saba, S. G., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.012 · Cited by 467 · see citing works

Post‐translational processing of p21ras is two‐step and involves carboxyl‐methylation and carboxy‐terminal proteolysis.

Gutierrez, L., Magee, A. I., Marshall, C. J., & Hancock, J. F. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03478.x · Cited by 460 · see citing works

Genes in S. cerevisiae encoding proteins with domains homologous to the mammalian ras proteins

Powers, S., Kataoka, T., Fasano, O., Goldfarb, M. P., Strathem, J., Broach, J. R., & Wigler, M. H. (1984) · Cell · doi:10.1016/0092-8674(84)90340-4 · Cited by 460 · see citing works

Membrane targeting of the nucleotide exchange factor Sos is sufficient for activating the Ras signaling pathway

Aronheim, A., Engelberg, D., Li, N., Al-Alawi, N., Schlessinger, J., & Karin, M. (1994) · Cell · doi:10.1016/0092-8674(94)90271-2 · Cited by 458 · see citing works

An SH3-SH2-SH3 protein is required for p21Ras1 activation and binds to sevenless and Sos proteins in vitro

Simon, M. C. (1993) · Cell · doi:10.1016/0092-8674(93)90169-q · Cited by 452 · see citing works

A novel GTP-binding protein, Sar1p, is involved in transport from the endoplasmic reticulum to the Golgi apparatus.

Nakano, A., & Muramatsu, M. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.109.6.2677 · Cited by 452 · see citing works

Human-tumor-derived cell lines contain common and different transforming genes

Perucho, M., Goldfarb, M. P., Shimizu, K., Lama, C., Fogh, J., & Wigler, M. H. (1981) · Cell · doi:10.1016/0092-8674(81)90388-3 · Cited by 447 · see citing works

Identification of transforming gene in two human sarcoma cell lines as a new member of the ras gene family located on chromosome 1

Hall, A., Marshall, C. J., Spurr, N. K., & Weiss, R. A. (1983) · Nature · doi:10.1038/303396a0 · Cited by 438 · see citing works

Distinct requirements for Ras oncogenesis in human versus mouse cellsPreprint

Hamad, N. M., Elconin, J. H., Karnoub, A. E., Bai, W., Rich, J. N., Abraham, R. T., Der, C. J., & Counter, C. M. (2002) · Genes & Development · doi:10.17615/zkd7-3774 · Cited by 430 · see citing works

Mouse skin carcinomas induced in vivo by chemical carcinogens have a transforming Harvey-ras oncogene

Balmain, A., & Pragnell, I. B. (1983) · Nature · doi:10.1038/303072a0 · Cited by 424 · see citing works

Malignant Activation of a K- <i>ras</i> Oncogene in Lung Carcinoma But Not in Normal Tissue of the Same Patient

Santos, E., Martin-Zanca, D., Reddy, E. P., Pierotti, M. A., Della Porta, G., & Barbacid, M. (1984) · Science · doi:10.1126/science.6695174 · Cited by 418 · see citing works

Purification of a protein cofactor required for ADP-ribosylation of the stimulatory regulatory component of adenylate cyclase by cholera toxin.

Kahn, R., & Gilman, A. G. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)82130-9 · Cited by 417 · see citing works

H-ras but Not K-ras Traffics to the Plasma Membrane through the Exocytic Pathway

Apolloni, A., Prior, I. A., Lindsay, M. R., Parton, R. G., & Hancock, J. F. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.7.2475-2487.2000 · Cited by 416 · see citing works

The let-23 gene necessary for Caenorhabditis elegans vulval induction encodes a tyrosine kinase of the EGF receptor subfamily

Aroian, R. V., Koga, M., Mendel, J., Ohshima, Y., & Sternberg, P. W. (1990) · Nature · doi:10.1038/348693a0 · Cited by 416 · see citing works

Discovery of a novel Raf kinase inhibitor.

Lyons, J. F., Wilhelm, S. M., Hibner, B., & Bollag, G. E. (2001) · Endocrine Related Cancer · doi:10.1677/erc.0.0080219 · Cited by 415 · see citing works

Caenorhabditis elegans ras gene let-60 acts as a switch in the pathway of vulval induction

Beitel, G. J., Clark, S. G., & Horvitz, H. (1990) · Nature · doi:10.1038/348503a0 · Cited by 414 · see citing works

Plasma membrane nanoswitches generate high-fidelity Ras signal transduction

Tian, T., Harding, A. S., Inder, K. L., Plowman, S. J., Parton, R. G., & Hancock, J. F. (2007) · Nature Cell Biology · doi:10.1038/ncb1615 · Cited by 407 · see citing works

Signaling Interplay in Ras Superfamily Function

Mitin, N., Rossman, K. L., & Der, C. J. (2005) · Current Biology · doi:10.1016/j.cub.2005.07.010 · Cited by 402 · see citing works

Phospholipase Cγ activates Ras on the Golgi apparatus by means of RasGRP1

Bivona, T. G., de Castro, I. P., Ahearn, I. M., Grana, T. M., Chiu, V. K., Lockyer, P. J., Cullen, P. J., Pellicer, À., Cox, A. D., & Philips, M. R. (2003) · Nature · doi:10.1038/nature01806 · Cited by 401 · see citing works

A yeast gene encoding a protein homologous to the human c-has/bas proto-oncogene product

Gallwitz, D., Donath, C., & Sander, C. (1983) · Nature · doi:10.1038/306704a0 · Cited by 401 · see citing works

Galectin-1 binds oncogenic H-Ras to mediate Ras membrane anchorage and cell transformation

Paz, A., Haklai, R., Elad‐Sfadia, G., Ballan, E., & Kloog, Y. (2001) · Oncogene · doi:10.1038/sj.onc.1204950 · Cited by 400 · see citing works

Harvey murine sarcoma virus p21 ras protein: biological and biochemical significance of the cysteine nearest the carboxy terminus.

Willumsen, B. M., Norris, K. E., Papageorge, A. G., Hubbert, N. L., & Lowy, D. R. (1984) · The EMBO Journal · doi:10.1002/j.1460-2075.1984.tb02177.x · Cited by 399 · see citing works

Localization of the src gene product of the Harvey strain of MSV to plasma membrane of transformed cells by electron microscopic immunocytochemistry

Willingham, M. C., Pastan, I. H., Shih, T. Y., & Scolnick, E. M. (1980) · Cell · doi:10.1016/0092-8674(80)90091-4 · Cited by 398 · see citing works

let-60, a gene that specifies cell fates during C. elegans vulval induction, encodes a ras protein

Han, M., & Sternberg, P. W. (1990) · Cell · doi:10.1016/0092-8674(90)90495-z · Cited by 394 · see citing works

Three human transforming genes are related to the viral ras oncogenes.

Shimizu, K., Goldfarb, M. P., Suard, Y. M. L., Perucho, M., Li, Y., Kamata, T., Feramisco, J. R., Stavnezer, E., Fogh, J. M., & Wigler, M. H. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.8.2112 · Cited by 389 · see citing works

Mice deficient in the Rac activator Tiam1 are resistant to Ras-induced skin tumours

Malliri, A., van der Kammen, R. A., Clark, K., van der Valk, M., Michiels, F., & Collard, J. G. (2002) · Nature · doi:10.1038/nature00848 · Cited by 384 · see citing works

A peptidomimetic inhibitor of farnesyl:protein transferase blocks the anchorage-dependent and -independent growth of human tumor cell lines.

Sepp‐Lorenzino, L., Ma, Z., Rands, E., Kohl, N. E., Gibbs, W. W., Oliff, A. I., & Rosen, N. X. (1995) · PubMed · Cited by 383 · see citing works

Cell cycle-dependent activation of Ras

Taylor, S. J., & Shalloway, D. I. (1996) · Current Biology · doi:10.1016/s0960-9822(02)70785-9 · Cited by 383 · see citing works

Posttranslational modification of the Ha-ras oncogene protein: evidence for a third class of protein carboxyl methyltransferases.

Clarke, S. G., Vogel, J. P., Deschenes, R. J., & Stock, J. B. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.13.4643 · Cited by 380 · see citing works

KrasG12D and Smad4/Dpc4 Haploinsufficiency Cooperate to Induce Mucinous Cystic Neoplasms and Invasive Adenocarcinoma of the Pancreas

Izeradjene, K., Combs, C., Best, M., Gopinathan, A., Wagner, A., Grady, W. M., Deng, C.-X., Hruban, R. H., Adsay, N. V., Tuveson, D. A., et al. (2007) · Cancer Cell · doi:10.1016/j.ccr.2007.01.017 · Cited by 379 · see citing works

Transforming activity of human tumor DNAs.

Krontiris, T. G., & Cooper, G. M. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.2.1181 · Cited by 373 · see citing works

ADP-ribosylation factor is functionally and physically associated with the Golgi complex.

Stearns, T., Willingham, M. C., Botstein, D., & Kahn, R. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.3.1238 · Cited by 372 · see citing works

Direct Demonstration of Geranylgeranylation and Farnesylation of Ki-Ras in Vivo

Rowell, C. A., Kowalczyk, J. J., Lewis, M. D., & Garcia, A. M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.22.14093 · Cited by 368 · see citing works

RalB GTPase-Mediated Activation of the IκB Family Kinase TBK1 Couples Innate Immune Signaling to Tumor Cell Survival

Chien, Y., Kim, S., Bumeister, R., Loo, Y., Kwon, S. W., Johnson, C., Balakireva, M. G., Roméo, Y., Kopelovich, L., Gale, M., et al. (2006) · Cell · doi:10.1016/j.cell.2006.08.034 · Cited by 367 · see citing works

Phospholipase Cϵ: a novel Ras effector

Kelley, G. G., Reks, S. E., Ondrako, J. M., & Smrcka, A. V. (2001) · The EMBO Journal · doi:10.1093/emboj/20.4.743 · Cited by 361 · see citing works

Identification of a Novel Ras-Regulated Proapoptotic Pathway

Khokhlatchev, A. V., Rabizadeh, S., Xavier, R. J., Nedwidek, M., Chen, T., Zhang, X., Seed, B., & Avruch, J. (2002) · Current Biology · doi:10.1016/s0960-9822(02)00683-8 · Cited by 357 · see citing works

K-Ras is essential for the development of the mouse embryo

Koera, K., Nakamura, K. D., Nakao, K., Miyoshi, J., Toyoshima, K., Hatta, T., Otani, H., Aiba, A., & Katsuki, M. (1997) · Oncogene · doi:10.1038/sj.onc.1201284 · Cited by 355 · see citing works

Molecular cloning of cDNAs encoding a guanine-nucleotide-releasing factor for Ras p21

Shou, C., Farnsworth, C. L., Neel, B. G., & Feig, L. A. (1992) · Nature · doi:10.1038/358351a0 · Cited by 353 · see citing works

Differential activation of yeast adenylate cyclase by wild type and mutant RAS proteins

Broek, D., Samiy, N., Fasano, O., Fujiyama, A., Tamanoi, F., Northup, J. K., & Wigler, M. H. (1985) · Cell · doi:10.1016/s0092-8674(85)80057-x · Cited by 353 · see citing works

The transforming proteins of Rous sarcoma virus, Harvey sarcoma virus and Abelson virus contain tightly bound lipid

Sefton, B. M., Trowbridge, I. S., Cooper, J. A., & Scolnick, E. M. (1982) · Cell · doi:10.1016/0092-8674(82)90139-8 · Cited by 352 · see citing works

Four additional members of the ras gene superfamily isolated by an oligonucleotide strategy: molecular cloning of YPT-related cDNAs from a rat brain library.

Touchot, N., Chardin, P., & Tavitian, A. (1987) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.84.23.8210 · Cited by 351 · see citing works

Quantitative Analysis of the Complex between p21 and the Ras-binding Domain of the Human Raf-1 Protein Kinase

Herrmann, C., Martin, G. A., & Wittinghofer, A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.7.2901 · Cited by 351 · see citing works

Guanine nucleotide-binding and autophosphorylating activities associated with the p21src protein of Harvey murine sarcoma virus

Shih, T. Y., Papageorge, A. G., Stokes, P. E., Weeks, M. O., & Scolnick, E. M. (1980) · Nature · doi:10.1038/287686a0 · Cited by 348 · see citing works

RAS proteins can induce meiosis in xenopus oocytes

Birchmeier, C., Broek, D., & Wigler, M. H. (1985) · Cell · doi:10.1016/0092-8674(85)90233-8 · Cited by 342 · see citing works

Human cDNAs rap1 and rap2 homologous to the Drosophila gene Dras3 encode proteins closely related to ras in the 'effector' region.

Pizon, V., Chardin, P., Janoueix‐Lerosey, I., Olofsson, B., & Tavitian, A. (1988) · PubMed · Cited by 336 · see citing works

Ral‐GTPases mediate a distinct downstream signaling pathway from Ras that facilitates cellular transformation.

Urano, T., Emkey, R., & Feig, L. A. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00416.x · Cited by 332 · see citing works

Tiam1 mediates Ras activation of Rac by a PI(3)K-independent mechanism

Lambert, J. M., Lambert, Q. T., Reuther, G. W., Malliri, A., Siderovski, D. P., Sondek, J., Collard, J. G., & Der, C. J. (2002) · Nature Cell Biology · doi:10.1038/ncb833 · Cited by 326 · see citing works

Human genome contains four genes homologous to transforming genes of Harvey and Kirsten murine sarcoma viruses.

Chang, E. H., Gonda, M. A., Ellis, R. W., Scolnick, E. M., & Lowy, D. R. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.16.4848 · Cited by 324 · see citing works

Regulation of a Novel Human Phospholipase C, PLCε, through Membrane Targeting by Ras

Song, C., Hu, C., Masago, M., Kariya, K., Yamawaki‐Kataoka, Y., Shibatohge, M., Wu, D., Satoh, T., & Kataoka, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008324200 · Cited by 320 · see citing works

Functional homology of mammalian and yeast RAS genes

Kataoka, T., Powers, S., Cameron, S., Fasano, O., Goldfarb, M. P., Broach, J. R., & Wigler, M. H. (1985) · Cell · doi:10.1016/0092-8674(85)90304-6 · Cited by 318 · see citing works

Signalling by the sevenless protein tyrosine kinase is mimicked by Rasl activation

Fortini, M. E., Simon, M. A., & Rubin, G. M. (1992) · Nature · doi:10.1038/355559a0 · Cited by 317 · see citing works

Guanine nucleotide-binding activity as an assay for src protein of rat-derived murine sarcoma viruses

Scolnick, E. M., Papageorge, A. G., & Shih, T. Y. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.10.5355 · Cited by 316 · see citing works

A restricted spectrum of NRAS mutations causes Noonan syndrome

Cirstea, I. C., Kutsche, K., Dvorský, R., Gremer, L., Carta, C., Horn, D., Roberts, A. E., Lepri, F. R., Merbitz-Zahradnik, T., König, R., et al. (2009) · Nature Genetics · doi:10.1038/ng.497 · Cited by 315 · see citing works

Raf functions downstream of Rasl in the Sevenless signal transduction pathway

Dickson, B. J., Sprenger, F., Morrison, D. K., & Hafen, E. (1992) · Nature · doi:10.1038/360600a0 · Cited by 312 · see citing works

Characterization of Four Novel ras -Like Genes Expressed in a Human Teratocarcinoma Cell Line

Drivas, G., Shih, A., Coutavas, E. E., Rush, M. G., & D’Eustachio, P. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.4.1793-1798.1990 · Cited by 310 · see citing works

Depalmitoylated Ras traffics to and from the Golgi complex via a nonvesicular pathway

Goodwin, J., Drake, K. R., Rogers, C., Wright, L. P., Lippincott-Schwartz, J., Philips, M., & Kenworthy, A. (2005) · Journal of Cell Biology · doi:10.1083/jcb.200502063 · Cited by 308 · see citing works

Dynamic fatty acylation of p21N‐ras.

Magee, A. I., Gutierrez-Gonzalez, L. A., McKay, I. A., Marshall, C. J., & Hall, A. (1987) · The EMBO Journal · doi:10.1002/j.1460-2075.1987.tb02656.x · Cited by 307 · see citing works

Morphologic Responses to a Murine Erythroblastosis Virus 2

KIRSTEN, W. H., & Mayer, L. A. (1967) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/39.2.311 · Cited by 306 · see citing works

Galectin-3 Augments K-Ras Activation and Triggers a Ras Signal That Attenuates ERK but Not Phosphoinositide 3-Kinase Activity*

Elad-Sfadia, G., Haklai, R., Balan, E., & Kloog, Y. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312697200 · Cited by 305 · see citing works

Renewing the conspiracy theory debate: does Raf function alone to mediate Ras oncogenesis?

Repasky, G. A., Chenette, E. J., & Der, C. J. (2004) · Trends in Cell Biology · doi:10.1016/j.tcb.2004.09.014 · Cited by 299 · see citing works

Targeted Genomic Disruption of H-ras and N-ras, Individually or in Combination, Reveals the Dispensability of Both Loci for Mouse Growth and Development

Esteban, L. M., Vicario‐Abejón, C., Fernández‐Salguero, P. M., Fernández‐Medarde, A., Swaminathan, N., Yienger, K., Lopez, E., Malumbres, M., McKay, R. D. G., Ward, J. M., et al. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.5.1444-1452.2001 · Cited by 298 · see citing works

rheb, a growth factor- and synaptic activity-regulated gene, encodes a novel Ras-related protein.

Yamagata, K., Sanders, L. K., Kaufmann, W. E., Yee, W. M., Barnes, C. A., Nathans, D., & Worley, P. F. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34012-7 · Cited by 297 · see citing works

Modulation of guanine nucleotides bound to Ras in NIH3T3 cells by oncogenes, growth factors, and the GTPase activating protein (GAP)

Gibbs, W. W., Marshall, M. S., Scolnick, E. M., Dixon, R. A., & Vogel, U. S. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30523-9 · Cited by 296 · see citing works

Ras Uses the Novel Tumor Suppressor RASSF1 as an Effector to Mediate Apoptosis

Vos, M. D., Ellis, C. A., Bell, A., Birrer, M. J., & Clark, G. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000463200 · Cited by 290 · see citing works

Polylysine and CVIM Sequences of K-RasB Dictate Specificity of Prenylation and Confer Resistance to Benzodiazepine Peptidomimetic in Vitro

James, G. L., Goldstein, J. L., & Brown, M. S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.11.6221 · Cited by 290 · 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

Identification of murine homologues of the Drosophila son of sevenless gene: potential activators of ras.

Bowtell, D. D. L., Fu, P., Simon, M., & Senior, P. V. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.14.6511 · Cited by 287 · see citing works

A membrane glycoprotein, Sec12p, required for protein transport from the endoplasmic reticulum to the Golgi apparatus in yeast.

Nakano, A., Brada, D., & Schekman, R. W. (1988) · The Journal of Cell Biology · doi:10.1083/jcb.107.3.851 · Cited by 279 · see citing works

Platelet-derived growth factor stimulates formation of active p21ras.GTP complex in Swiss mouse 3T3 cells.

Satoh, T., Endo, M., Nakafuku, M., Nakamura, S., & Kaziro, Y. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.15.5993 · Cited by 277 · see citing works

A Novel Bifunctional Phospholipase C That Is Regulated by Gα12 and Stimulates the Ras/Mitogen-activated Protein Kinase Pathway

López, I., Mak, E. C., Ding, J., Hamm, H. E., & Lomasney, J. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008119200 · Cited by 276 · see citing works

The Son of sevenless Gene Product: a Putative Activator of Ras

Bonfini, L., Karlovich, C., Dasgupta, C., & Banerjee, U. K. (1992) · Science · doi:10.1126/science.1736363 · Cited by 274 · see citing works

Identification of a sarcoma virus-coded phosphoprotein in nonproducer cells transformed by Kirsten or Harvey murine sarcoma virus

Shih, T. Y., Weeks, M. O., Young, H. A., & Scolnick, E. M. (1979) · Virology · doi:10.1016/0042-6822(79)90173-9 · Cited by 273 · see citing works

A Comprehensive Survey of Ras Mutations in Cancer

Prior, I. A., Lewis, P. D., & Mattos, C. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-2612 · Cited by 2,063 · see citing works

Drugging the undruggable RAS: Mission Possible?

Cox, A. D., Fesik, S. W., Kimmelman, A. C., Luo, J., & Der, C. J. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4389 · Cited by 1,997 · see citing works

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 · see citing works

RAS isoforms and mutations in cancer at a glance

Hobbs, G. A., Der, C. J., & Rossman, K. L. (2016) · Journal of Cell Science · doi:10.1242/jcs.182873 · Cited by 973 · see citing works

Prostate Cancer Review: Genetics, Diagnosis, Treatment Options, and Alternative Approaches

Sekhoacha, M. P., Riet, K., Motloung, P., Gumenku, L., Adegoke, A. M., & Mashele, S. S. (2022) · Molecules · doi:10.3390/molecules27175730 · Cited by 947 · see citing works

Targeting the RAS/RAF/MAPK pathway for cancer therapy: from mechanism to clinical studies

Bahar, M. E., Kim, H. J., & Kim, D. R. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01705-z · Cited by 888 · 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

Ras superfamily GEFs and GAPs: validated and tractable targets for cancer therapy?

Vigil, D., Cherfils, J., Rossman, K. L., & Der, C. J. (2010) · Nature reviews. Cancer · doi:10.1038/nrc2960 · Cited by 816 · see citing works

Immunogenicity of somatic mutations in human gastrointestinal cancers

Tran, E., Ahmadzadeh, M., Lu, Y.-C., Gros, A., Turcotte, S., Robbins, P. F., Gartner, J. J., Zheng, Z., Li, Y. F., Ray, S., et al. (2015) · Science · doi:10.1126/science.aad1253 · Cited by 729 · see citing works

KRAS: feeding pancreatic cancer proliferation

Bryant, K. L., Mancias, J. D., Kimmelman, A. C., & Der, C. J. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.12.004 · Cited by 675 · see citing works

Regulating the regulator: post-translational modification of RAS

Ahearn, I. M., Haigis, K. M., Bar‐Sagi, D., & Philips, M. R. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3255 · Cited by 560 · see citing works

The current state of the art and future trends in RAS-targeted cancer therapies

Punekar, S. R., Velcheti, V., Neel, B. G., & Wong, K.-K. (2022) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-022-00671-9 · Cited by 549 · see citing works

Targeting Aberrant RAS/RAF/MEK/ERK Signaling for Cancer Therapy

Degirmenci, U., Wang, M., & Hu, J. (2020) · Cells · doi:10.3390/cells9010198 · Cited by 542 · see citing works

Proteomic Analysis of Exosomes from Mutant KRAS Colon Cancer Cells Identifies Intercellular Transfer of Mutant KRAS

Beckler, M. D., Higginbotham, J. N., Franklin, J. L., Ham, A. L., Halvey, P. J., Imasuen, I., Whitwell, C. A., Li, M., Liebler, D. C., & Coffey, R. J. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m112.022806 · Cited by 514 · see citing works

The MAPK and AMPK signalings: interplay and implication in targeted cancer therapy

Yuan, J., Dong, X., Yap, J., & Hu, J. (2020) · Journal of Hematology & Oncology · doi:10.1186/s13045-020-00949-4 · Cited by 500 · see citing works

A RASopathy gene commonly mutated in cancer: the neurofibromatosis type 1 tumour suppressor

Ratner, N., & Miller, S. J. (2015) · Nature reviews. Cancer · doi:10.1038/nrc3911 · Cited by 488 · see citing works

Differential association of STK11 and TP53 with KRAS mutation-associated gene expression, proliferation and immune surveillance in lung adenocarcinoma

Schabath, M. B., Welsh, E. A., Fulp, W. J., Chen, L., Teer, J. K., Thompson, Z., Engel, B. E., Xie, M., Berglund, A., Creelan, B., et al. (2015) · Oncogene · doi:10.1038/onc.2015.375 · Cited by 421 · see citing works

Therapeutic strategies to target RAS-mutant cancers

Ryan, M. B., & Corcoran, R. B. (2018) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-018-0105-0 · Cited by 420 · see citing works

Drugging RAS: know the enemy

Papke, B., & Der, C. J. (2017) · Science · doi:10.1126/science.aam7622 · Cited by 399 · see citing works

Inhibition of Ras for Cancer Treatment: The Search Continues

Baines, A. T., Xu, D., & Der, C. J. (2011) · Future Medicinal Chemistry · doi:10.4155/fmc.11.121 · Cited by 384 · see citing works

Rho guanine nucleotide exchange factors: regulators of Rho GTPase activity in development and disease

Cook, D. R., Rossman, K. L., & Der, C. J. (2014) · Oncogene · doi:10.1038/onc.2013.362 · Cited by 378 · see citing works

KRAS Alleles: The Devil Is in the Detail

Haigis, K. M. (2017) · Trends in Cancer · doi:10.1016/j.trecan.2017.08.006 · Cited by 373 · see citing works

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 · see citing works

Targeting RAS Membrane Association: Back to the Future for Anti-RAS Drug Discovery?

Cox, A. D., Der, C. J., & Philips, M. R. (2015) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-3214 · Cited by 351 · see citing works

Myeloid cells are required for PD-1/PD-L1 checkpoint activation and the establishment of an immunosuppressive environment in pancreatic cancer

Zhang, Y., Velez-Delgado, A., Mathew, E., Li, D., Mendez, F., Flannagan, K., Rhim, A. D., Simeone, D. M., Beatty, G. L., & di Magliano, M. P. (2016) · Gut · doi:10.1136/gutjnl-2016-312078 · Cited by 338 · see citing works

MEK inhibition exhibits efficacy in human and mouse neurofibromatosis tumors

Jessen, W. J., Miller, S. J., Jousma, E., Wu, J., Rizvi, T. A., Brundage, M. E., Eaves, D. W., Widemann, B. C., Kim, M., Dombi, E., et al. (2012) · Journal of Clinical Investigation · doi:10.1172/jci60578 · Cited by 336 · see citing works

Molecular epidemiology and diagnostics of KRAS mutations in human cancer

Timar, J., & Kashofer, K. (2020) · Cancer and Metastasis Reviews · doi:10.1007/s10555-020-09915-5 · Cited by 334 · see citing works

KRAS-Mutant non-small cell lung cancer: From biology to therapy

Ferrer, I., Zugazagoitia, J., Herbertz, S., John, W. J., Paz-Ares, L. G., & Schmid‐Bindert, G. (2018) · Lung Cancer · doi:10.1016/j.lungcan.2018.07.013 · Cited by 311 · see citing works

The current understanding of KRAS protein structure and dynamics

Pantsar, T. (2019) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2019.12.004 · Cited by 288 · see citing works

Inhibition of RAS function through targeting an allosteric regulatory site

Spencer-Smith, R., Koide, A., Zhou, Y., Eguchi, R. R., Sha, F., Gajwani, P., Santana, D., Gupta, A., Jacobs, M., Herrero-Garcia, E., et al. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2231 · Cited by 283 · see citing works

The Ras/ MAPK pathway and hepatocarcinoma: pathogenesis and therapeutic implications

Delire, B., & Stärkel, P. (2015) · European Journal of Clinical Investigation · doi:10.1111/eci.12441 · Cited by 275 · see citing works

Ras-GTP dimers activate the Mitogen-Activated Protein Kinase (MAPK) pathway

Nan, X., Tamgüney, T. M., Collisson, E. A., Lin, L.-J., Pitt, C., Galeas, J., Lewis, S., Gray, J. W., McCormick, F., & Chu, S. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1509123112 · Cited by 273 · see citing works

Targeting wild-type KRAS-amplified gastroesophageal cancer through combined MEK and SHP2 inhibition

Wong, G. S., Zhou, J., Liu, J. B., Wu, Z., Xu, X., Li, T., Xu, D., Schumacher, S. E., Puschhof, J., McFarland, J., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0022-x · Cited by 266 · see citing works

Inhibition of SHP2-mediated dephosphorylation of Ras suppresses oncogenesis

Bunda, S., Burrell, K., Heir, P., Zeng, L., Alamsahebpour, A., Kano, Y., Raught, B., Zhang, Z.-Y., Zadeh, G., & Ohh, M. (2015) · Nature Communications · doi:10.1038/ncomms9859 · Cited by 249 · see citing works

Enhancing CRISPR/Cas gene editing through modulating cellular mechanical properties for cancer therapy

Zhang, D., Wang, G., Yu, X., Wei, T., Farbiak, L., Johnson, L. T., Taylor, A. M., Xu, J., Hong, Y., Zhu, H., et al. (2022) · Nature Nanotechnology · doi:10.1038/s41565-022-01122-3 · Cited by 243 · see citing works

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 231 · see citing works

Tipifarnib in Head and Neck Squamous Cell Carcinoma With<i>HRAS</i>Mutations

Ho, A. L., Brana, I., Haddad, R., Bauman, J., Bible, K., Oosting, S., Wong, D. J., Ahn, M.-J., Boni, V., Even, C., et al. (2021) · Journal of Clinical Oncology · doi:10.1200/jco.20.02903 · Cited by 208 · see citing works

The path to the clinic: a comprehensive review on direct KRASG12C inhibitors

Kwan, A. K., Piazza, G. A., Keeton, A. B., & Leite, C. A. (2022) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-021-02225-w · Cited by 192 · see citing works

Drugging Ras GTPase: a comprehensive mechanistic and signaling structural view

Lu, S., Jang, H., Gu, S., Zhang, J., & Nussinov, R. (2016) · Chemical Society Reviews · doi:10.1039/c5cs00911a · Cited by 188 · see citing works

The Ras Superfamily of Small GTPases: The Unlocked Secrets

Goitre, L., Trapani, E., Trabalzini, L., & Retta, S. F. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-791-4_1 · Cited by 186 · see citing works

KRAS Mutant Pancreatic Cancer: No Lone Path to an Effective Treatment

Zeitouni, D., Pylayeva‐Gupta, Y., Der, C. J., & Bryant, K. L. (2016) · Cancers · doi:10.3390/cancers8040045 · Cited by 179 · see citing works

Structural basis of recognition of farnesylated and methylated KRAS4b by PDEδ

Dharmaiah, S., Bindu, L. K., Tran, T. H., Gillette, W., Frank, P. H., Ghirlando, R., Nissley, D. V., Esposito, D., McCormick, F. P., Stephen, A. G., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1615316113 · Cited by 176 · see citing works

The RASopathies: from pathogenetics to therapeutics

Hebron, K. E., Hernandez, E. R., & Yohe, M. E. (2022) · Disease Models & Mechanisms · doi:10.1242/dmm.049107 · Cited by 167 · see citing works

H-Ras forms dimers on membrane surfaces via a protein–protein interface

Lin, W., Iversen, L., Tu, H., Rhodes, C., Christensen, S. M., Iwig, J. S., Hansen, S. D., Huang, W. Y. C., & Groves, J. T. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321155111 · Cited by 157 · see citing works

Biology of colorectal cancer

Arvelo, F. A. (2015) · ecancermedicalscience · doi:10.3332/ecancer.2015.520 · Cited by 152 · see citing works

Extracellular-Signal Regulated Kinase: A Central Molecule Driving Epithelial–Mesenchymal Transition in Cancer

Olea‐Flores, M., Zuñiga‐Eulogio, M. D., Catalán, M. A. M., Rodríguez-Ruiz, H. A., Castañeda-Saucedo, E., Ortuño‐Pineda, C., Padilla‐Benavides, T., & Navarro‐Tito, N. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20122885 · Cited by 149 · see citing works

Targeting the Small GTPase Superfamily through Their Regulatory Proteins

Gray, J. L., von Delft, F., & Brennan, P. E. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201900585 · Cited by 142 · see citing works

Oncogenic K-Ras Binds to an Anionic Membrane in Two Distinct Orientations: A Molecular Dynamics Analysis

Prakash, P., Zhou, Y., Hong, L., Hancock, J. F., & Gorfe, A. A. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2016.01.019 · Cited by 140 · see citing works

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 · see citing works

Targeting KRAS Mutant Non-Small-Cell Lung Cancer: Past, Present and Future

Uras, I. Z., Moll, H. P., & Casanova, E. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21124325 · Cited by 134 · see citing works

The small GTPases K-Ras, N-Ras, and H-Ras have distinct biochemical properties determined by allosteric effects

Johnson, C. W., Reid, D., Parker, J. A., Salter, S., Knihtila, R., Kuzmic, P., & Mattos, C. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.778886 · Cited by 133 · see citing works

Targeting RAS-mutant cancers: is ERK the key?

Ryan, M. B., Der, C., Wang-Gillam, A., & Cox, A. (2015) · Trends in Cancer · doi:10.1016/j.trecan.2015.10.001 · Cited by 125 · see citing works

Transforming mutations of RAC guanosine triphosphatases in human cancers

Kawazu, M., Ueno, T., Kontani, K., Ogita, Y., Ando, M., Fukumura, K., Yamato, A., Soda, M., Takeuchi, K., Miki, Y., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1216141110 · Cited by 131 · see citing works

The role of wild type RAS isoforms in cancer

Zhou, B., Der, C. J., & Cox, A. D. (2016) · Seminars in Cell &amp; Developmental Biology · doi:10.1016/j.semcdb.2016.07.012 · Cited by 130 · see citing works

The RalGEF-Ral Effector Signaling Network: The Road Less Traveled for Anti-Ras Drug Discovery

Neel, N. F., Martin, T. D., Stratford, J. K., Zand, T. P., Reiner, D. J., & Der, C. J. (2011) · Genes & Cancer · doi:10.1177/1947601911407329 · Cited by 130 · see citing works

Structural insights into the BRAF monomer-to-dimer transition mediated by RAS binding

Fiesco, J. A. M., Durrant, D., Morrison, D. K., & Zhang, P. (2022) · Nature Communications · doi:10.1038/s41467-022-28084-3 · Cited by 130 · see citing works

Molecular Mechanisms of Conidial Germination in Aspergillus spp

Baltussen, T. J. H., Zoll, J., Verweij, P. E., & Melchers, W. J. G. (2019) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00049-19 · Cited by 129 · see citing works

Malignant peripheral nerve sheath tumor: models, biology, and translation

Somatilaka, B. N., Sadek, A. H., McKay, R. M., & Le, L. Q. (2022) · Oncogene · doi:10.1038/s41388-022-02290-1 · Cited by 128 · see citing works

Membrane curvature enables N-Ras lipid anchor sorting to liquid-ordered membrane phases

Larsen, J. B., Jensen, M. B., Bhatia, V. K., Pedersen, S. L., Bjørnholm, T., Iversen, L., Uline, M. J., Szleifer, I. G., Jensen, K. J., Hatzakis, N. S., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1733 · Cited by 126 · see citing works

Racial and Ethnic Differences in the Epidemiology and Genomics of Lung Cancer

Schabath, M. B., Cress, W. D., & Muñoz-Antonia, T. (2016) · Cancer Control · doi:10.1177/107327481602300405 · Cited by 126 · see citing works

The Importance of Being PI3K in the RAS Signaling Network

Cuesta, C., Arévalo-Alameda, C., & Castellano, E. (2021) · Genes · doi:10.3390/genes12071094 · Cited by 123 · see citing works

The complex landscape of pancreatic cancer metabolism

Sousa, C. M., & Kimmelman, A. C. (2014) · Carcinogenesis · doi:10.1093/carcin/bgu097 · Cited by 123 · see citing works

Emerging roles of allosteric modulators in the regulation of protein‐protein interactions (PPIs): A new paradigm for PPI drug discovery

Ni, D., Lu, S., & Zhang, J. (2019) · Medicinal Research Reviews · doi:10.1002/med.21585 · Cited by 116 · see citing works

Distinct Binding Preferences between Ras and Raf Family Members and the Impact on Oncogenic Ras Signaling

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 115 · see citing works

Ral small GTPase signaling and oncogenesis: More than just 15minutes of fame

Gentry, L. R., Martin, T. D., Reiner, D. J., & Der, C. J. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.09.004 · Cited by 110 · see citing works

Vascular smooth muscle cell proliferation as a therapeutic target. Part 1: molecular targets and pathways

Wang, D., Uhrín, P., Mocan, A., Waltenberger, B., Breuss, J. M., Tewari, D., Mihaly‐Bison, J., Huminiecki, Ł., Starzyński, R. R., Tzvetkov, N. T., et al. (2018) · Biotechnology Advances · doi:10.1016/j.biotechadv.2018.04.006 · Cited by 110 · see citing works

Therapeutic targeting of RAS: New hope for drugging the “undruggable”

Khan, I., Rhett, J. M., & O’Bryan, J. P. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.118570 · Cited by 111 · see citing works

Efficient targeted oncogenic KRASG12C degradation via first reversible-covalent PROTAC

Yang, F., Wen, Y., Wang, C., Zhou, Y., Zhou, Y., Zhang, Z.-M., Liu, T., & Lu, X. (2022) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.114088 · Cited by 109 · see citing works

RAF Suppression Synergizes with MEK Inhibition in KRAS Mutant Cancer Cells

Lamba, S., Russo, M., Sun, C., Lazzari, L., Cancelliere, C., Grernrum, W., Lieftink, C., Bernards, R., Nicolantonio, F. D., & Bardelli, A. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.07.033 · Cited by 109 · see citing works

Ras and autophagy in cancer development and therapy

Schmukler, E., Kloog, Y., & Pinkas‐Kramarski, R. (2014) · Oncotarget · doi:10.18632/oncotarget.1775 · Cited by 108 · see citing works

Ras signaling through RASSF proteins

Donninger, H., Schmidt, M., Mezzanotte-Sharpe, J., Barnoud, T., & Clark, G. J. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.06.007 · Cited by 106 · see citing works

RAL GTPases: Biology and Potential as Therapeutic Targets in Cancer

Yan, C., & Theodorescu, D. (2018) · Pharmacological Reviews · doi:10.1124/pr.117.014415 · Cited by 119 · see citing works

Predictive in vivo animal models and translation to clinical trials

Cook, N., Jodrell, D. I., & Tuveson, D. A. (2012) · Drug Discovery Today · doi:10.1016/j.drudis.2012.02.003 · Cited by 104 · see citing works

Crucial Role of Oncogenic KRAS Mutations in Apoptosis and Autophagy Regulation: Therapeutic Implications

Ferreira, A. I., Pereira, F. D. S., Reis, C. A., Oliveira, M. J., Sousa, M. J., & Preto, A. (2022) · Cells · doi:10.3390/cells11142183 · Cited by 103 · see citing works

Small-Molecule Inhibitors Directly Targeting KRAS as Anticancer Therapeutics

Chen, H., Smaill, J. B., Liu, T., Ding, K., & Lu, X. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01312 · Cited by 100 · see citing works

Src promotes GTPase activity of Ras via tyrosine 32 phosphorylation

Bunda, S., Heir, P., Srikumar, T., Cook, J. D., Burrell, K. E., Kano, Y., Lee, J. E., Zadeh, G. M., Raught, B., & Ohh, M. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1406559111 · Cited by 100 · see citing works

Vascular mimicry: Triggers, molecular interactions and in vivo models

Wechman, S. L., Emdad, L., Sarkar, D., Das, S. K., & Fisher, P. B. (2020) · Advances in cancer research · doi:10.1016/bs.acr.2020.06.001 · Cited by 99 · see citing works

Structural analysis of the Ras‐like G protein MglA and its cognate GAP MglB and implications for bacterial polarity

Miertzschke, M., Koerner, C., Vetter, I. R., Keilberg, D., Hot, E., Leonardy, S., Søgaard‐Andersen, L., & Wittinghofer, A. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.291 · Cited by 98 · see citing works

Targeting mutant <i>KRAS</i> with CRISPR-Cas9 controls tumor growth

Kim, W., Lee, S., Kim, H. S., Song, M., Cha, Y. H., Kim, Y.-H., Shin, J., Lee, E.-S., Joo, Y., Song, J. J., et al. (2018) · Genome Research · doi:10.1101/gr.223891.117 · Cited by 97 · see citing works

Computational and biochemical characterization of two partially overlapping interfaces and multiple weak-affinity K-Ras dimers

Prakash, P., Sayyed–Ahmad, A., Cho, K.-J., Dolino, D. M., Chen, W., Li, H., Grant, B. J., Hancock, J. F., & Gorfe, A. A. (2017) · Scientific Reports · doi:10.1038/srep40109 · Cited by 93 · see citing works

A New View of Ras Isoforms in Cancers

Nussinov, R., Tsai, C., Chakrabarti, M., & Jang, H. (2015) · Cancer Research · doi:10.1158/0008-5472.can-15-1536 · Cited by 92 · see citing works

The discovery of modular binding domains: building blocks of cell signalling

Mayer, B. J. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm4068 · Cited by 89 · see citing works

Discovery of High-Affinity Noncovalent Allosteric KRAS Inhibitors That Disrupt Effector Binding

McCarthy, M. J., Pagba, C. V., Prakash, P., Naji, A. K., van der Hoeven, D., Liang, H., Gupta, A. K., Zhou, Y., Cho, K.-J., Hancock, J. F., et al. (2019) · ACS Omega · doi:10.1021/acsomega.8b03308 · Cited by 90 · see citing works

Nrf2, but not β‐catenin, mutation represents an early event in rat hepatocarcinogenesis

Zavattari, P., Perra, A., Menegon, S., Kowalik, M. A., Petrelli, A., Angioni, M. M., Follenzi, A., Quagliata, L., Ledda‐Columbano, G. M., Terracciano, L., et al. (2015) · Hepatology · doi:10.1002/hep.27790 · Cited by 88 · see citing works

Crosstalk of Ras and Rho: activation of RhoA abates Kras-induced liver tumorigenesis in transgenic zebrafish models

Chew, T. W., Liu, X. J., Liu, L., Spitsbergen, J. M., Gong, Z., & Low, B. C. (2013) · Oncogene · doi:10.1038/onc.2013.240 · Cited by 88 · see citing works

Reconstructing targetable pathways in lung cancer by integrating diverse omics data

Balbin, O. A., Prensner, J. R., Sahu, A., Yocum, A. K., Shankar, S., Malik, R., Fermin, D., Dhanasekaran, S. M., Chandler, B. C., Thomas, D. G., et al. (2013) · Nature Communications · doi:10.1038/ncomms3617 · Cited by 88 · see citing works

The Ras switch in structural and historical perspective

Gasper, R., & Wittinghofer, F. (2019) · Biological Chemistry · doi:10.1515/hsz-2019-0330 · Cited by 88 · see citing works

Posttranslational Modifications of RAS ProteinsPreprint

Ahearn, I. M., Zhou, M., & Philips, M. R. (2018) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a031484 · Cited by 86 · see citing works

Targeting small GTPases: emerging grasps on previously untamable targets, pioneered by KRAS

Yin, G., Huang, J., Petela, J., Jiang, H., Zhang, Y., Gong, S., Wu, J., Liu, B., Shi, J., & Gao, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01441-4 · Cited by 87 · see citing works

Oncogene-Driven Metabolic Alterations in Cancer

Min, H., & Lee, H. (2017) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2017.211 · Cited by 87 · see citing works

Rho GTPases—Emerging Regulators of Glucose Homeostasis and Metabolic Health

Møller, L. L. V., Klip, A., & Sylow, L. (2019) · Cells · doi:10.3390/cells8050434 · Cited by 83 · see citing works

Computational Modeling Reveals that Signaling Lipids Modulate the Orientation of K-Ras4A at the Membrane Reflecting Protein Topology

Li, Z., & Buck, M. (2017) · Structure · doi:10.1016/j.str.2017.02.007 · Cited by 81 · see citing works

Spatiotemporal Analysis of K-Ras Plasma Membrane Interactions Reveals Multiple High Order Homo-oligomeric Complexes

Sarkar‐Banerjee, S., Sayyed–Ahmad, A., Prakash, P., Cho, K., Waxham, M. N., Hancock, J. F., & Gorfe, A. A. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b06292 · Cited by 81 · see citing works

K-Ras Populates Conformational States Differently from Its Isoform H-Ras and Oncogenic Mutant K-RasG12D

Parker, J. A., Volmar, A. Y., Pavlopoulos, S., & Mattos, C. (2018) · Structure · doi:10.1016/j.str.2018.03.018 · Cited by 81 · see citing works

A Landscape of Therapeutic Cooperativity in KRAS Mutant Cancers Reveals Principles for Controlling Tumor Evolution

Anderson, G. R., Winter, P. S., Lin, K. H., Nussbaum, D. P., Cakir, M., Stein, E. M., Soderquist, R. S., Crawford, L., Leeds, J. C., Newcomb, R., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.07.006 · Cited by 80 · see citing works

The Ras Superfamily of Small GTPases in Non-neoplastic Cerebral Diseases

Qu, L., Pan, C., He, S., Lang, B., Gao, G.-D., Wang, X., & Wang, Y. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00121 · Cited by 80 · see citing works

Two Distinct Structures of Membrane‐Associated Homodimers of GTP‐ and GDP‐Bound KRAS4B Revealed by Paramagnetic Relaxation Enhancement

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 79 · see citing works

The Key Role of Calmodulin in KRAS-Driven Adenocarcinomas

Nussinov, R., Muratcioğlu, S., Tsai, C., Jang, H., Gürsoy, A., & Keskin, Ö. (2015) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-15-0165 · Cited by 77 · see citing works

Direct Modulation of Small GTPase Activity and Function

Cromm, P. M., Spiegel, J., Grossmann, T. N., & Waldmann, H. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201504357 · Cited by 78 · see citing works

YAP/TAZ Activation Drives Uveal Melanoma Initiation and Progression

Li, H., Li, Q., Dang, K., Ma, S., Cotton, J. L., Yang, S., Zhu, L. J., DENG, A. C., Ip, Y. T., Johnson, R. L., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.03.021 · Cited by 77 · see citing works

Flashback in the history of Ras research

Chaldaiopoulou, G., Γουλιελμάκη, Μ., Khoury, N., Ζουμπουρλής, Β., & Zoumpourlis (2017) · National Hellenic Research Foundation Helios Repository (National Hellenic Research Foundation)

Ras Stories: The State of the Art

Roberts, P. J., & Der, C. J. (2006) · Springer eBooks · doi:10.1007/1-4020-4708-8_1

The Ras Superfamily of Small GTPases: The Unlocked Secrets

Goitre, L., Trapani, E., Trabalzini, L., & Retta, S. F. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-791-4_1 · Cited by 186 · see citing works

40 Years of RAS—A Historic Overview

Fernández‐Medarde, A., Rivas, J. D. L., & Santos, E. (2021) · Genes · doi:10.3390/genes12050681 · Cited by 53 · see citing works

Ras Proteins☆

George, S., & Der, C. J. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.98756-7