Ras oncogenes: split personalities
Open accessAbstract
Extensive research on the Ras proteins and their functions in cell physiology over the past 30 years has led to numerous insights that have revealed the involvement of Ras not only in tumorigenesis but also in many developmental disorders. Despite great strides in our understanding of the molecular and cellular mechanisms of action of the Ras proteins, the expanding roster of their downstream effectors and the complexity of the signalling cascades that they regulate indicate that much remains to be learnt.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
PDEδ has a large hydrophobic pocket that can bind farnesyl proteins, especially the lipid portion of KRAS protein, thereby preventing the farnesyl modification of KRAS protein from binding to cell membrane and inhibiting tumor cell proliferation and growth.
“PDEδ has a large hydrophobic pocket that can bind farnesyl proteins, especially the lipid portion of KRAS protein, thereby preventing the farnesyl modification of KRAS protein from binding to cell membrane and inhibiting tumor cell proliferation and growth.339,340”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [339]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Functional rafts in cell membranes
Simons, K., & Ikonen, E. (1997) · Nature · doi:10.1038/42408 · Cited by 9,757 · see citing works
G PROTEINS: TRANSDUCERS OF RECEPTOR-GENERATED SIGNALS
Gilman, A. G. (1987) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.56.070187.003151 · Cited by 6,405 · see citing works
Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a
Serrano, M., Lin, A. W., McCurrach, M. E., Beach, D., & Lowe, S. W. (1997) · Cell · doi:10.1016/s0092-8674(00)81902-9 · Cited by 5,178 · see citing works
Srimaroeng, C., Cecile, J. P., Walden, R., & Pritchard, J. B. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350077 · Cited by 2,989 · 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
Self-citationCreation 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
Self-citationMammalian 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
Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome
Tartaglia, M., Mehler, E. L., Goldberg, R. B., Zampino, G., Brunner, H. G., Kremer, H., van der Burgt, I., Crosby, A. H., Ion, A., Jeffery, S., et al. (2001) · Nature Genetics · doi:10.1038/ng772 · Cited by 1,736 · see citing works
The Ras-RasGAP Complex: Structural Basis for GTPase Activation and Its Loss in Oncogenic Ras Mutants
Scheffzek, K., Ahmadian, M. R., Kabsch, W., Wiesmüller, L., Lautwein, A., Schmitz, F., & Wittinghofer, A. (1997) · Science · doi:10.1126/science.277.5324.333 · Cited by 1,543 · see citing works
Type 1 Neurofibromatosis Gene: Identification of a Large Transcript Disrupted in Three NF1 Patients
Wallace, M. R., Marchuk, D. A., Andersen, L. B., Letcher, R., Odeh, H. M., Saulino, A. M., Fountain, J. W., Brereton, A., Nicholson, J. M., Mitchell, A. L., et al. (1990) · Science · doi:10.1126/science.2134734 · Cited by 1,476 · 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
Self-citationReddy, 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
Ruley, H. E. (1983) · Nature · doi:10.1038/304602a0 · Cited by 1,248 · see citing works
RAF/RAS oncogenes and mismatch-repair status
Rajagopalan, H., Bardelli, A., Lengauer, C., Kinzler, K. W., Vogelstein, B., & Velculescu, V. E. (2002) · Nature · doi:10.1038/418934a · Cited by 1,224 · see citing works
Trahey, M., & McCormick, F. (1987) · Science · doi:10.1126/science.2821624 · Cited by 1,211 · see citing works
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
Self-citationSomatic activation of the K-ras oncogene causes early onset lung cancer in mice
Johnson, L., Mercer, K., Greenbaum, D., Bronson, R. T., Crowley, D., Tuveson, D. A., & Jacks, T. (2001) · Nature · doi:10.1038/35074129 · Cited by 1,179 · see citing works
The neurofibromatosis type 1 gene encodes a protein related to GAP
Xu, G., O'Connell, P., Viskochil, D., Cawthon, R., Robertson, M., Culver, M., Dunn, D., Stevens, J., Gesteland, R., White, R., et al. (1990) · Cell · doi:10.1016/0092-8674(90)90024-9 · Cited by 1,095 · cited 1× · see citing works
“Soon thereafter, the second RasGAP, neurofibromin-1 ( NF1 ), was identified and found to be disrupted in patients with neurofibromatosi”
Cawthon, R., Weiss, R. B., Xu, G., Viskochil, D. H., Culver, M., Stevens, J., Robertson, M. A., Dunn, D. M., Gesteland, R. F., O'Connell, P., et al. (1990) · Cell · doi:10.1016/0092-8674(90)90253-b · Cited by 1,093 · see citing works
Deletions and a translocation interrupt a cloned gene at the neurofibromatosis type 1 locus
Viskochil, D. H., Buchberg, A. M., Xu, G., Cawthon, R., Stevens, J., Wolff, R. K., Culver, M., Carey, J. C., Copeland, N. G., Jenkins, N. A., et al. (1990) · Cell · doi:10.1016/0092-8674(90)90252-a · Cited by 1,082 · see citing works
Increasing complexity of Ras signaling
Campbell, S. L., Khosravi-Far, R., Rossman, K. L., Clark, G. J., & Der, C. J. (1998) · Oncogene · doi:10.1038/sj.onc.1202174 · Cited by 1,079 · see citing works
Buday, L., & Downward, J. (1993) · Cell · doi:10.1016/0092-8674(93)90146-h · Cited by 1,064 · see citing works
Rodriguez‐Viciana, P., Warne, P. H., Khwaja, A., Marte, B. M., Pappin, D., Das, P., Waterfield, M. D., Ridley, A. J., & Downward, J. (1997) · Cell · doi:10.1016/s0092-8674(00)80226-3 · Cited by 1,063 · see citing works
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
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
Khwaja, A., Rodriguez‐Viciana, P., Wennström, S., Warne, P. H., & Downward, J. (1997) · The EMBO Journal · doi:10.1093/emboj/16.10.2783 · Cited by 1,039 · 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
Complete nucleotide sequences of the T24 human bladder carcinoma oncogene and its normal homologue
Capon, D. J., Chen, E. Y., Levinson, A. D., Seeburg, P. H., & Goeddel, D. V. (1983) · Nature · doi:10.1038/302033a0 · Cited by 997 · 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
Blockade of the MAP kinase pathway suppresses growth of colon tumors in vivo
Sebolt, J. S., Dudley, D. T., Herrera, R., Becelaere, K. V., Wiland, A. M., Gowan, R. C., Tecle, H., Barrett, S. D., Bridges, A. J., Przybranowski, S. A., et al. (1999) · Nature Medicine · doi:10.1038/10533 · Cited by 972 · 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
Self-citationLi, 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
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
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
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
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
Reactive Oxygen Species-Induced Activation of the MAP Kinase Signaling Pathways
McCubrey, J. A., LaHair, M. M., & Franklin, R. A. (2006) · Antioxidants and Redox Signaling · doi:10.1089/ars.2006.8.1775 · Cited by 804 · 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
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
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
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
Reovirus Therapy of Tumors with Activated Ras Pathway
Coffey, M. C., Strong, J. E., Forsyth, P. A., & Lee, P. W. K. (1998) · Science · doi:10.1126/science.282.5392.1332 · Cited by 750 · see citing works
Cell-cycle control of c-myc but not c-ras expression is lost following chemical transformation
Campisi, J., Gray, H. E., Pardee, A. B., Dean, M. C., & Sonenshein, G. E. (1984) · Cell · doi:10.1016/0092-8674(84)90217-4 · Cited by 747 · see citing works
Bar-Sagi, D., & Feramisco, J. R. (1986) · Science · doi:10.1126/science.3090687 · Cited by 734 · 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
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
PKB/Akt: connecting phosphoinositide 3-kinase to cell survival and beyond
Marte, B. M. (1997) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(97)01097-9 · Cited by 696 · see citing works
Ras Proteins Induce Senescence by Altering the Intracellular Levels of Reactive Oxygen Species
Lee, A. C., Fenster, B. E., Ito, H., Takeda, K., Bae, N. S., Hirai, T., Yu, Z.-X., Ferrans, V. J., Howard, B. H., & Finkel, T. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.12.7936 · Cited by 691 · see citing works
Activation of Rac1, RhoA, and mitogen-activated protein kinases is required for Ras transformation
Khosravi-Far, R., Solski, P. A., Clark, G. J., Kinch, M. S., & Der, C. J. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.11.6443 · Cited by 683 · 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
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
Brannan, C. I., Perkins, A. S., Vogel, K. S., Ratner, N., Nordlund, M. L., Reid, S. W., Buchberg, A. M., Jenkins, N. A., Parada, L. F., & Copeland, N. G. (1994) · Genes & Development · doi:10.1101/gad.8.9.1019 · Cited by 641 · see citing works
Santos, E., Tronick, S. R., Aaronson, S. A., Pulciani, S., & Barbacid, M. (1982) · Nature · doi:10.1038/298343a0 · Cited by 624 · see citing works
Germline gain-of-function mutations in SOS1 cause Noonan syndrome
Roberts, A. E., Araki, T., Swanson, K. D., Montgomery, K. T., Schiripo, T. A., Joshi, V. A., Li, L., Yassin, Y., Tamburino, A. M., Neel, B. G., et al. (2007) · Nature Genetics · doi:10.1038/ng1926 · Cited by 605 · see citing works
NF1 Tumor Suppressor Gene Function
Cichowski, K. M., & Jacks, T. (2001) · Cell · doi:10.1016/s0092-8674(01)00245-8 · Cited by 603 · 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 · cited 1× · see citing works
“Moreover, although activated H-Ras is associated with both the Golgi apparatus and the endoplasmic reticulum (ER), only the ER-associated form can activate RAF1–ERK signallin”
Binding of Ras to Phosphoinositide 3-Kinase p110α Is Required for Ras- Driven Tumorigenesis in Mice
Gupta, S., Ramjaun, A. R., Haiko, P., Wang, Y., Warne, P. H., Nicke, B., Nye, E. L., Stamp, G., Alitalo, K. K., & Downward, J. (2007) · Cell · doi:10.1016/j.cell.2007.03.051 · Cited by 589 · 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
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 580 · see citing works
Germline Mutations in Genes Within the MAPK Pathway Cause Cardio-facio-cutaneous Syndrome
Rodriguez‐Viciana, P., Tetsu, O., Tidyman, W. E., Estep, A. L., Conger, B. A., Cruz, M. S., McCormick, F. P., & Rauen, K. A. (2006) · Science · doi:10.1126/science.1124642 · Cited by 571 · see citing works
Biological properties of human c-Ha-ras1 genes mutated at codon 12
Seeburg, P. H., Colby, W. W., Capon, D. J., Goeddel, D. V., & Levinson, A. D. (1984) · Nature · doi:10.1038/312071a0 · Cited by 567 · 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
The molecular basis of viral oncolysis: usurpation of the Ras signaling pathway by reovirus
Strong, J. E., Coffey, M. C., Tang, D., Sabinin, P., & Lee, P. W. K. (1998) · The EMBO Journal · doi:10.1093/emboj/17.12.3351 · Cited by 552 · 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
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
Kato, K., Cox, A. D., Hisaka, M. M., Graham, S. M., Buss, J. E., & Der, C. J. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.14.6403 · 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
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
Requirement of NF-κB Activation to Suppress p53-Independent Apoptosis Induced by Oncogenic Ras
Mayo, M. W., Wang, C.-Y., Cogswell, P. C., Rogers-Graham, K., Lowe, S. W., Der, C. J., & Baldwin, A. S. (1997) · Science · doi:10.1126/science.278.5344.1812 · 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
Activation of the mouse cellular Harvey-ras gene in chemically induced benign skin papillomas
Balmain, A., Ramsden, M., Bowden, G. T., & Smith, J. (1984) · Nature · doi:10.1038/307658a0 · Cited by 529 · see citing works
Structure and activation of the human N-ras gene
Taparowsky, E. J., Shimizu, K., Goldfarb, M. P., & Wigler, M. H. (1983) · Cell · doi:10.1016/0092-8674(83)90390-2 · Cited by 527 · see citing works
GTP-dependent segregation of H-ras from lipid rafts is required for biological activity
Prior, I. A., Harding, A. S., Yan, J., Sluimer, J. C., Parton, R. G., & Hancock, J. F. (2001) · Nature Cell Biology · doi:10.1038/35070050 · Cited by 513 · see citing works
Activation of extracellular signal‐regulated kinase, ERK2, by p21ras oncoprotein.
Leevers, S. J., & Marshall, C. J. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05088.x · Cited by 496 · see citing works
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
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
Mandai, K., Nakanishi, H., Satoh, A., Obaishi, H., Wada, M., Nishioka, H., Itoh, M., Mizoguchi, A., Aoki, T., Fujimoto, T., et al. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.139.2.517 · Cited by 476 · 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
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
PDGF induction of tyrosine phosphorylation of GTPase activating protein
Molloy, C. J., Bottaro, D. P., Fleming, T. P., Marshall, M. S., Gibbs, W. W., & Aaronson, S. A. (1989) · Nature · doi:10.1038/342711a0 · Cited by 454 · see citing works
Hall, A., Marshall, C. J., Spurr, N. K., & Weiss, R. A. (1983) · Nature · doi:10.1038/303396a0 · Cited by 438 · see citing works
Fibroblast immortality is a prerequisite for transformation by EJ c-Ha-ras oncogene
Newbold, R. F., & Overell, R. W. (1983) · Nature · doi:10.1038/304648a0 · Cited by 436 · 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
Self-citationBalmain, A., & Pragnell, I. B. (1983) · Nature · doi:10.1038/303072a0 · Cited by 424 · see citing works
Ras -Transformed Cells: Altered Levels of Phosphatidylinositol-4,5-Bisphosphate and Catabolites
Fleischman, L. F., Chahwala, S. B., & Cantley, L. C. (1986) · Science · doi:10.1126/science.3001936 · Cited by 422 · see citing works
Hagag, N. G., Halegoua, S., & Viola, M. V. (1986) · Nature · doi:10.1038/319680a0 · Cited by 419 · see citing works
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
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
Araki, T., Mohi, G., Ismat, F. A., Bronson, R. T., Williams, I. R., Kutok, J. L., Yang, W., Pao, L. I., Gilliland, D. G., Epstein, J. A., et al. (2004) · Nature Medicine · doi:10.1038/nm1084 · Cited by 415 · see citing works
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
cDNA cloning of the type 1 neurofibromatosis gene: Complete sequence of the NF1 gene product
Marchuk, D. A., Saulino, A. M., Tavakkol, R., Swaroop, M., Wallace, M. R., Andersen, L. B., Mitchell, A. L., Gutmann, D. H., Boguski, M. S., & Collins, F. S. (1991) · Genomics · doi:10.1016/0888-7543(91)90017-9 · Cited by 390 · 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
Mitogen‐activated protein kinase p38 defines the common senescence‐signalling pathway
Iwasa, H., Han, J., & Ishikawa, F. (2003) · Genes to Cells · doi:10.1046/j.1365-2443.2003.00620.x · Cited by 388 · 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
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
Krengel, U., Schlichting, I., Scherer, A., Schumann, R., Frech, M., John, J., Kabsch, W., Pai, E., & Wittinghofer, A. (1994) · Cell · doi:10.1016/0092-8674(90)90018-a · Cited by 374 · see citing works
GAPs galore! A survey of putative Ras superfamily GTPase activating proteins in man and Drosophila
Bernards, A. (2003) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(02)00082-3 · Cited by 362 · see citing works
Amino-acid substitutions at codon 13 of the N-ras oncogene in human acute myeloid leukaemia
Bos, J. L., Toksoz, D., Marshall, C. J., Vries, M. V., Veeneman, G. H., van der Eb, A. J., BOOM, J. H. V., Janssen, J. W. G., & Steenvoorden, A. C. M. (1985) · Nature · doi:10.1038/315726a0 · Cited by 362 · 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
NOONAN SYNDROME AND RELATED DISORDERS: Genetics and Pathogenesis
Tartaglia, M., & Gelb, B. D. (2005) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev.genom.6.080604.162305 · 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
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
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
Wright, L. P., & Philips, M. R. (2006) · Journal of Lipid Research · doi:10.1194/jlr.r600004-jlr200 · Cited by 343 · see citing works
Murray, M. J., Cunningham, J. M., Parada, L. F., Dautry, F., Lebowitz, P., & Weinberg, R. A. (1983) · Cell · doi:10.1016/0092-8674(83)90017-x · Cited by 337 · see citing works
Self-citationItoh, H., Kozasa, T., Nagata, S., Nakamura, S., Katada, T., Ui, M., Iwai, S., Ohtsuka, E., Kawasaki, H., & Suzuki, K. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.11.3776 · Cited by 337 · see citing works
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
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
PRAK Is Essential for ras-Induced Senescence and Tumor Suppression
Sun, P., Yoshizuka, N., New, L., Moser, B. A., Li, Y., Liao, R., Xie, C., Chen, J., Deng, Q., Yamout, M., et al. (2007) · Cell · doi:10.1016/j.cell.2006.11.050 · Cited by 321 · see citing works
Ashar, H. R., James, L. J., Gray, K., Carr, D. M., Black, S., Armstrong, L., Bishop, W. R., & Kirschmeier, P. T. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003469200 · Cited by 321 · 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
Wolfman, A., & Macara, I. G. (1987) · Nature · doi:10.1038/325359a0 · Cited by 319 · see citing works
Ras‐activated endocytosis is mediated by the Rab5 guanine nucleotide exchange activity of RIN1
Tall, G. G., Barbieri, M. A., Stahl, P. D., & Horazdovsky, B. F. (2001) · Developmental Cell · doi:10.1016/s1534-5807(01)00008-9 · Cited by 308 · see citing works
DeFeo, D., Gonda, M. A., Young, H. A., Chang, E. H., Lowy, D. R., Scolnick, E. M., & Ellis, R. W. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.6.3328 · Cited by 301 · see citing works
Diverse Biochemical Properties of Shp2 Mutants
Keilhack, H., David, F. S., McGregor, M. J., Cantley, L. C., & Neel, B. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504699200 · Cited by 299 · see citing works
Novel source of 1,2-diacylglycerol elevated in cells transformed by Ha-ras oncogene
Lacal, J. C., Moscat, J., & Aaronson, S. A. (1987) · Nature · doi:10.1038/330269a0 · Cited by 299 · see citing works
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
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
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
Expression of p21 proteins in Escherichia coli and stereochemistry of the nucleotide‐binding site.
Tucker, J., Sczakiel, G., Feuerstein, J., John, J., Goody, R. S., & Wittinghofer, A. (1986) · The EMBO Journal · doi:10.1002/j.1460-2075.1986.tb04366.x · Cited by 285 · see citing works
Identification of effector residues and a neutralizing epitope of Ha-ras-encoded p21.
Sigal, I. S., Gibbs, W. W., D'Alonzo, J., & Scolnick, E. M. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.13.4725 · Cited by 285 · see citing works
The role of Shp2 (PTPN11) in cancer
Mohi, G., & Neel, B. G. (2007) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2006.12.011 · Cited by 277 · see citing works
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 cardiofaciocutaneous syndrome
Roberts, A., Allanson, J., Jadico, S. K., Kavamura, M. I., Noonan, J., Opitz, J. M., Young, T., & Neri, G. (2006) · Journal of Medical Genetics · doi:10.1136/jmg.2006.042796 · Cited by 271 · see citing works
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
Purification of ras GTPase activating protein from bovine brain.
Gibbs, W. W., Schaber, M. D., Allard, W. J., Sigal, I. S., & Scolnick, E. M. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.14.5026 · Cited by 245 · see citing works
White, M. A., Vale, T., Camonis, J., SCHAEFER, E. M., & Wigler, M. H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.28.16439 · Cited by 240 · see citing works
The murine N-ras gene is not essential for growth and development.
Umanoff, H., Edelmann, W., Pellicer, À., & Kucherlapati, R. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.5.1709 · Cited by 234 · see citing works
CDC25 : a Component of the RAS -Adenylate Cyclase Pathway in Saccharomyces cerevisiae
Robinson, L. C., Gibbs, W. W., Marshall, M. S., Sigal, I. S., & Tatchell, K. (1987) · Science · doi:10.1126/science.3547648 · Cited by 234 · see citing works
Hrycyna, C. A., Sapperstein, S. K., Clarke, S. G., & Michaelis, S. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07694.x · Cited by 234 · see citing works
Sun, J., Qian, Y., Hamilton, A. D., & Sebti, S. M. (1995) · PubMed · Cited by 227 · see citing works
Polyisoprenylation of Ras in vitro by a farnesyl-protein transferase.
Schaber, M. D., O'Hara, M. B., Garsky, V. M., Mosser, S. D., Bergstrom, J. D., Moores, S. L., Marshall, M. S., Friedman, P. A., Dixon, R., & Gibbs, W. W. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)77164-0 · Cited by 227 · see citing works
A Cytosolic Protein Catalyzes the Release of GDP from p21 ras
Wolfman, A., & Macara, I. G. (1990) · Science · doi:10.1126/science.2181667 · Cited by 223 · see citing works
Differential Expression of the ras Gene Family in Mice
León, J., Guerrero, I., & Pellicer, À. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.4.1535 · Cited by 222 · see citing works
Ras p21 as a Potential Mediator of Insulin Action in Xenopus Oocytes
Korn, L. J., Siebel, C. W., McCormick, F. P., & Roth, R. A. (1987) · Science · doi:10.1126/science.3554510 · Cited by 221 · see citing works
Hand, P. H., Thor, A. D., Wunderlich, D. A., Muraro, R., Caruso, A., & Schlom, J. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.16.5227 · Cited by 220 · see citing works
Differential modification of Ras proteins by ubiquitination.
Jura, N., Scotto–Lavino, E., Sobczyk, A., & Bar-Sagi, D. (2006) · Molecules and Cells · doi:10.1016/j.molcel.2006.02.011 · Cited by 219 · see citing works
Farnesyltransferase Inhibitors Alter the Prenylation and Growth-stimulating Function of RhoB
Lebowitz, P. F., Casey, P. J., Prendergast, G. C., & Thissen, J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.25.15591 · Cited by 216 · see citing works
Neoplastic Transformation of Human Epidermal Keratinocytes by AD12-SV40 and Kirsten Sarcoma Viruses
Rhim, J. S., Jay, G., Arnstein, P., Price, F. M., Sanford, K. K., & Aaronson, S. A. (1985) · Science · doi:10.1126/science.2579430 · Cited by 216 · see citing works
Tumor Susceptibility of Rassf1a Knockout Mice
Tommasi, S., Dammann, R., Zhang, Z., Wang, Y., Liu, L., Tsark, W. M. K., Wilczynski, S. P., Li, J., You, M., & Pfeifer, G. P. (2005) · Cancer Research · doi:10.1158/0008-5472.92.65.1 · Cited by 214 · see citing works
Identification of Nore1 as a Potential Ras Effector
Vavvas, D. G., Li, X., Avruch, J., & Zhang, X. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.10.5439 · Cited by 208 · see citing works
Identification of AF-6 and Canoe as Putative Targets for Ras
Kuriyama, M., Harada, N., Kuroda, S., Yamamoto, T. G., Nakafuku, M., Iwamatsu, A., Yamamoto, D., Prasad, R., Croce, C. M., Canaani, E., et al. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.2.607 · Cited by 208 · see citing works
Crucial Role of Phospholipase Cε in Chemical Carcinogen-Induced Skin Tumor Development
Bai, Y., Edamatsu, H., Maeda, S., Saito, H., 昇, 鈴., Satoh, T., & Kataoka, T. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-3143 · Cited by 206 · see citing works
A novel family ofras-binding domains
Ponting, C. P., & Benjamin, D. R. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)30038-8 · Cited by 205 · see citing works
RAL GTPases are linchpin modulators of human tumour‐cell proliferation and survival
Chien, Y., & White, M. A. (2003) · EMBO Reports · doi:10.1038/sj.embor.embor899 · Cited by 195 · see citing works
The tumor-suppressive functions of the human INK4A locus
Voorhoeve, P. M., & Agami, R. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00223-x · Cited by 194 · see citing works
Kamata, T., & Feramisco, J. R. (1984) · Nature · doi:10.1038/310147a0 · Cited by 194 · see citing works
RAS mutations and clonality analysis in children with juvenile myelomonocytic leukemia (JMML)
Flotho, C., Valcamonica, S., Mach‐Pascual, S., Schmahl, G. E., Corral, L., Ritterbach, J., Hasle, H., Aricò, M., Biondi, A., & Niemeyer, C. M. (1999) · Leukemia · doi:10.1038/sj.leu.2401240 · Cited by 194 · see citing works
Transformation of Human Bronchial Epithelial Cells Transfected by Harvey ras Oncogene
Yoakum, G. H., Lechner, J. F., Gabrielson, E. W., Korba, B. E., Malan-Shibley, L. B., Willey, J. C., Valerio, M. G., Shamsuddin, A. M., Trump, B. F., & Harris, C. C. (1985) · Science · doi:10.1126/science.3975607 · Cited by 191 · see citing works
Specific inhibition of K-ras expression and tumorigenicity of lung cancer cells by antisense RNA
Cavender, A. C. (1991) · Lung Cancer · doi:10.1016/0169-5002(91)90412-y · Cited by 189 · see citing works
A molecular approach to leukemogenesis: mouse lymphomas contain an activated c-ras oncogene.
Guerrero, I., Calzada, P., Mayer, A. J., & Pellicer, À. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.1.202 · Cited by 188 · see citing works
RASSF2 Is a Novel K-Ras-specific Effector and Potential Tumor Suppressor
Vos, M. D., Ellis, C. A., Elam, C. A., Ülkü, A. S., Taylor, B. J., & Clark, G. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300554200 · Cited by 184 · see citing works
Geyer, M., & Wittinghofer, A. (1997) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(97)80147-9 · Cited by 182 · see citing works
RalGDS is required for tumor formation in a model of skin carcinogenesis
González-Garcı́a, A., Pritchard, C. A., Paterson, H. F., Mavria, G., Stamp, G., & Marshall, C. J. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.01.029 · Cited by 181 · see citing works
Ha-ras oncogenes are activated by somatic alterations in human urinary tract tumours
Fujita, J., Yoshida, O., Yuasa, Y., Rhim, J. S., Hatanaka, M., & Aaronson, S. A. (1984) · Nature · doi:10.1038/309464a0 · Cited by 181 · see citing works
Inactivation of Icmt inhibits transformation by oncogenic K-Ras and B-Raf
Bergö, M. O., Gavino, B. J., Hong, C., Beigneux, A. P., McMahon, M., Casey, P. J., & Young, S. G. (2004) · Journal of Clinical Investigation · doi:10.1172/jci18829 · Cited by 180 · see citing works
Inactivation of Icmt inhibits transformation by oncogenic K-Ras and B-Raf
Bergo, M. O., Gavino, B. J., Hong, C., Beigneux, A. P., McMahon, M., Casey, P. J., & Young, S. G. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200418829 · Cited by 180 · see citing works
Winter-Vann, A. M., Baron, R. A., Wong, W., dela Cruz, J., York, J. D., Gooden, D. M., Bergo, M. O., Young, S. G., Toone, E. J., & Casey, P. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408107102 · Cited by 178 · see citing works
Activation of a c-K- ras Oncogene by Somatic Mutation in Mouse Lymphomas Induced by Gamma Radiation
Guerrero, I., Villasanté, A., Corces, V. G., & Pellicer, À. (1984) · Science · doi:10.1126/science.6474169 · Cited by 175 · see citing works
Schafer, W. R., Trueblood, C. E., Yang, C.-C., Mayer, M. P., Rosenberg, S., Poulter, C. D., Kim, S., & Rine, J. (1990) · Science · doi:10.1126/science.2204115 · Cited by 172 · see citing works
Han, L., & Colicelli, J. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.3.1318 · Cited by 170 · see citing works
N-myc can cooperate with ras to transform normal cells in culture.
Yancopoulos, G. D., Nisen, P. D., Tesfaye, A., Kohl, N. E., Goldfarb, M. P., & Alt, F. W. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.16.5455 · Cited by 167 · see citing works
Basso, A. D., Mirza, A., Liu, G., Long, B. J., Bishop, W. R., & Kirschmeier, P. T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503763200 · Cited by 162 · see citing works
Liu, A., Du, W., Liu, J.-P., Jessell, T. M., & Prendergast, G. C. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.16.6105-6113.2000 · Cited by 160 · see citing works
Chan, R. J., Leedy, M. B., Munugalavadla, V., Voorhorst, C. S., Li, Y., Yu, M., & Kapur, R. (2005) · Blood · doi:10.1182/blood-2004-10-4002 · Cited by 156 · see citing works
Shih, T. Y., Weeks, M. O., Gruss, P., Dhar, R., Oroszlan, S., & Scolnick, E. M. (1982) · Journal of Virology · doi:10.1128/jvi.42.1.253-261.1982 · Cited by 149 · see citing works
Winter-Vann, A. M., Kamen, B. A., Bergö, M. O., Young, S. G., Melnyk, S., James, S. J., & Casey, P. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1135239100 · Cited by 146 · see citing works
Mangues, R., Corral, T., Kohl, N. E., Symmans, W. F., Lü, S., Malumbres, M., Gibbs, W. W., Oliff, A. I., & Pellicer, À. (1998) · PubMed · Cited by 146 · see citing works
Identification of a nucleotide exchange-promoting activity for p21ras.
Downward, J., Riehl, R., Wu, L., & Weinberg, R. A. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.15.5998 · Cited by 142 · see citing works
Self-citationAbsence of the CAAX Endoprotease Rce1: Effects on Cell Growth and Transformation
Bergö, M. O., Ambroziak, P., Gregory, C., George, A. M., Otto, J. C., Kim, E. J.-H., Nagase, H., Casey, P. J., Balmain, A., & Young, S. G. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.1.171-181.2002 · Cited by 142 · see citing works
Nakano, H., Yamamoto, F., Neville, C., Evans, D., Mizuno, T., & Perucho, M. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.1.71 · Cited by 133 · see citing works
Matallanas, D., Sanz-Moreno, V., Arozarena, I., Calvo, F., Agudo-Ibáñez, L., Santos, E., Berciano, M., & Crespo, P. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.1.100-116.2006 · Cited by 130 · see citing works
Potenza, N., Vecchione, C., Notte, A., Rienzo, A. D., Rosica, A., Bauer, L., Affuso, A., Felice, M. D., Russo, T., Poulet, R., et al. (2005) · EMBO Reports · doi:10.1038/sj.embor.7400397 · Cited by 126 · see citing works
The Pro-apoptotic Ras Effector Nore1 May Serve as a Ras-regulated Tumor Suppressor in the Lung
Vos, M. D., Martı́nez, A., Ellis, C. A., Vallecorsa, T., & Clark, G. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211019200 · Cited by 122 · see citing works
Structural differences between a ras oncogene protein and the normal protein
Tong, L., de Vos, A. M., Milburn, M. V., Jancarik, J., Noguchi, S., Nishimura, S., Miura, K., Ohtsuka, E., & Kim, S. (1989) · Nature · doi:10.1038/337090a0 · Cited by 122 · see citing works
Rapid Stimulation of Diacylglycerol Production in Xenopus Oocytes by Microinjection of H- ras p21
Lacal, J. C., de la Peña, P., Moscat, J., Garcia-Barreno, P., Anderson, P. S., & Aaronson, S. A. (1987) · Science · doi:10.1126/science.2821623 · Cited by 121 · see citing works
Involvement of Functional Protein Kinase C in the Mitogenic Response to the H-ras Oncogene Product
Lacal, J. C., Fleming, T. P., Warren, B. S., Blumberg, P. M., & Aaronson, S. A. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.11.4146 · Cited by 117 · see citing works
Brünger, A. T., Milburn, M. V., Tong, L., Devos, A. M., Jancarik, J., Yamaizumi, Z., Nishimura, S., Ohtsuka, E., & Kim, S. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.12.4849 · Cited by 115 · see citing works
A novel membrane factor stimulates guanine nucleotide exchange reaction of ras proteins
West, M., Kung, H., & Kamata, T. (1990) · FEBS Letters · doi:10.1016/0014-5793(90)80019-f · Cited by 114 · see citing works
Antibody to phosphatidylinositol 4,5-bisphosphate inhibits oncogene-induced mitogenesis.
Fukami, K., Matsuoka, K., Nakanishi, O., Yamakawa, A., Kawai, S., & Takenawa, T. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.23.9057 · Cited by 109 · see citing works
Normal Human Fibroblasts Are Resistant to RAS-Induced Senescence
Benanti, J. A., & Galloway, D. A. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.7.2842-2852.2004 · Cited by 103 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Activation and function of the MAPKs and their substrates, the MAPK-activated protein kinases
Cargnello, M., & Roux, P. P. (2011) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00031-10 · Cited by 3,274 · see citing works
Panitumumab–FOLFOX4 Treatment and <i>RAS</i> Mutations in Colorectal Cancer
Douillard, J.-Y., Oliner, K. S., Siena, S., Tabernero, J., Burkes, R., Barugel, M., Humblet, Y., Bodoky, G., Cunningham, D., Jassem, J., et al. (2013) · New England Journal of Medicine · doi:10.1056/nejmoa1305275 · Cited by 2,263 · see citing works
RAS oncogenes: weaving a tumorigenic web
Pylayeva-Gupta, Y., Grabocka, E., & Bar-Sagi, D. (2011) · Nature Reviews Cancer · doi:10.1038/nrc3106 · Cited by 1,789 · see citing works
Oncogene ablation-resistant pancreatic cancer cells depend on mitochondrial function
Viale, A., Pettazzoni, P., Lyssiotis, C. A., Ying, H., Sánchez, N., Marchesini, M., Carugo, A., Green, T., Seth, S., Giuliani, V., et al. (2014) · Nature · doi:10.1038/nature13611 · Cited by 1,259 · 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
Exploring treatment options in cancer: tumor treatment strategies
Liu, B., Zhou, H., Tan, L., Siu, K. T. H., & Guan, X.-Y. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01856-7 · Cited by 1,201 · see citing works
KRAS Mutation: From Undruggable to Druggable in Cancer
Huang, L., Guo, Z., Wang, F., & Fu, L. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00780-4 · Cited by 1,127 · see citing works
Signaling cross-talk between TGF-β/BMP and other pathways
Guo, X., & Wang, X. (2008) · Cell Research · doi:10.1038/cr.2008.302 · Cited by 1,027 · 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
The Roles of Autophagy in Cancer
Yun, C. W., & Lee, S. H. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19113466 · Cited by 965 · see citing works
Recent progresses in small-molecule enzymatic fluorescent probes for cancer imaging
Liu, H.-W., Chen, L., Xu, C., Li, Z., Zhang, H., Zhang, X.-B., & Tan, W. (2018) · Chemical Society Reviews · doi:10.1039/c7cs00862g · Cited by 948 · 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
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
Stephen, A. G., Esposito, D., Bagni, R. K., & McCormick, F. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.02.017 · Cited by 795 · see citing works
Tumor biomarkers for diagnosis, prognosis and targeted therapy
Zhou, Y., Tao, L., Qiu, J., Xu, J., Yang, X., Zhang, Y., Tian, X., Guan, X., Cen, X., & Zhao, Y. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01823-2 · Cited by 772 · see citing works
Ras history: The saga continues
Cox, A. D., & Der, C. J. (2010) · Small GTPases · doi:10.4161/sgtp.1.1.12178 · Cited by 706 · see citing works
Dynamic modularity in protein interaction networks predicts breast cancer outcome
Taylor, I. W., Linding, R., Warde-Farley, D., Liu, Y., Pesquita, C., Faria, D., Bull, S. B., Pawson, T. J., Morris, Q., & Wrana, J. L. (2009) · Nature Biotechnology · doi:10.1038/nbt.1522 · Cited by 690 · 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
MEK1 and MEK2 inhibitors and cancer therapy: the long and winding road
Caunt, C. J., Sale, M. J., Smith, P. D., & Cook, S. J. (2015) · Nature Reviews Cancer · doi:10.1038/nrc4000 · Cited by 606 · see citing works
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
Gavine, P. R., Mooney, L. M., Kilgour, E., Thomas, A. P., Al-Kadhimi, K. J., Beck, S., Rooney, C., Coleman, T., Baker, D., Mellor, M. J., et al. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-3034 · Cited by 507 · see citing works
Implementing Genome-Driven Oncology
Hyman, D. M., Taylor, B. S., & Baselga, J. M. (2017) · Cell · doi:10.1016/j.cell.2016.12.015 · Cited by 505 · see citing works
Facilitative glucose transporters: Implications for cancer detection, prognosis and treatment
Barron, C. C., Bilan, P. J., Tsakiridis, T. K., & Tsiani, E. (2015) · Metabolism · doi:10.1016/j.metabol.2015.10.007 · Cited by 441 · see citing works
Hedgehog beyond medulloblastoma and basal cell carcinoma
Teglund, S., & Toftgård, R. (2010) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2010.01.003 · Cited by 426 · see citing works
Papke, B., & Der, C. J. (2017) · Science · doi:10.1126/science.aam7622 · Cited by 399 · see citing works
Roles for KRAS in Pancreatic Tumor Development and Progression
di Magliano, M. P., & Logsdon, C. D. (2013) · Gastroenterology · doi:10.1053/j.gastro.2013.01.071 · Cited by 397 · see citing works
Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials
Xie, X., Yu, T., Li, X., Zhang, N., Foster, L. J., Peng, C., Huang, W., & He, G. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01589-z · Cited by 396 · 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 385 · see citing works
Cook, D. R., Rossman, K. L., & Der, C. J. (2014) · Oncogene · doi:10.1038/onc.2013.362 · Cited by 378 · see citing works
The Ras protein superfamily: Evolutionary tree and role of conserved amino acids
Rojas, A. M., Fuentes, G., Rausell, A., & Valencia, A. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201103008 · Cited by 378 · see citing works
Molecular biology of lung cancer.
Cooper, W. A., Lam, D. C.-L., O'Toole, S. A., & Minna, J. D. (2013) · Europe PMC (PubMed Central) · doi:10.3978/j.issn.2072-1439.2013.08.03 · Cited by 365 · see citing works
Characterization of the interface between normal and transformed epithelial cells
Hogan, C., Dupré‐Crochet, S., Norman, M., Kajita, M., Zimmermann, C., Pelling, A. E., Piddini, E., Baena-López, L. A., Vincent, J., Itoh, Y., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1853 · Cited by 362 · see citing works
Frequency and type of KRAS mutations in routine diagnostic analysis of metastatic colorectal cancer.
Neumann, J., Zeindl-Eberhart, E., Kirchner, T., & Jung, A. (2009) · Pathology - Research and Practice · doi:10.1016/j.prp.2009.07.010 · Cited by 361 · see citing works
Singhal, A., Li, B. T., & O'Reilly, E. M. (2024) · Nature Medicine · doi:10.1038/s41591-024-02903-0 · Cited by 358 · 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
Role and regulation of autophagy in cancer
Chen, N., & Karantza‐Wadsworth, V. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.12.013 · Cited by 355 · see citing works
Therapeutic Strategies for Targeting Ras Proteins
Gysin, S., Salt, M. B., Young, A. E., & McCormick, F. (2011) · Genes & Cancer · doi:10.1177/1947601911412376 · Cited by 321 · see citing works
A Novel Role for Copper in Ras/Mitogen-Activated Protein Kinase Signaling
Turski, M. L., Brady, D. C., Kim, H. J., Kim, B.-E., Nose, Y., Counter, C. M., Winge, D. R., & Thiele, D. J. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.05722-11 · Cited by 318 · 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
Fuxe, J., Vincent, C. T., & de Herreros, A. G. (2010) · Cell Cycle · doi:10.4161/cc.9.12.12050 · Cited by 311 · 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 306 · see citing works
Blasco, R. B., Francoz, S., Santamaría, D., Cañamero, M., Dubus, P., Charron, J., Baccarini, M., & Barbacid, M. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.04.002 · Cited by 302 · see citing works
Shima, F., Yoshikawa, Y., Ye, M., Araki, M., Matsumoto, S., Liao, J., Hu, L., Sugimoto, T., Ijiri, Y., Takeda, A., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1217730110 · Cited by 293 · 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
Modeling High-Grade Serous Ovarian Carcinogenesis from the Fallopian Tube
Karst, A. M., Levanon, K., & Drapkin, R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1017300108 · Cited by 280 · see citing works
Rho GTPase signaling in cancer progression and dissemination
Crosas‐Molist, E., Samain, R., Kohlhammer, L., Orgaz, J. L., George, S. L., Maiques, Ó., Barcelo, J., & Sanz‐Moreno, V. (2021) · Physiological Reviews · doi:10.1152/physrev.00045.2020 · Cited by 277 · 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
Functional Specificity of Ras Isoforms: So Similar but So Different
Castellano, E., & Santos, E. (2011) · Genes & Cancer · doi:10.1177/1947601911408081 · Cited by 273 · see citing works
Multivalent Small-Molecule Pan-RAS Inhibitors
Welsch, M., Kaplan, A. R., Chambers, J. M., Stokes, M. E., Bos, P. H., Zask, A., Zhang, Y., Sánchez-Martín, M., Badgley, M. A., Huang, C., et al. (2017) · Cell · doi:10.1016/j.cell.2017.02.006 · Cited by 273 · see citing works
The Mitochondrial Chaperone TRAP1 Promotes Neoplastic Growth by Inhibiting Succinate Dehydrogenase
Sciacovelli, M., Guzzo, G., Morello, V., Frezza, C., Zheng, L., Nannini, N., Calabrese, F., Laudiero, G., Esposito, F., Landriscina, M., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.04.019 · Cited by 269 · see citing works
The chemokine MCP-1 (CCL2) in the host interaction with cancer: a foe or ally?
Yoshimura, T. (2018) · Cellular and Molecular Immunology · doi:10.1038/cmi.2017.135 · Cited by 269 · see citing works
ERK1/2 Phosphorylate Raptor to Promote Ras-dependent Activation of mTOR Complex 1 (mTORC1)
Carriere, A., Romeo, Y., Acosta-Jaquez, H. A., Moreau, J., Bonneil, E., Thibault, P., Fingar, D. C., & Roux, P. P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.159046 · Cited by 268 · see citing works
K-ras Mutation Subtypes in NSCLC and Associated Co-occuring Mutations in Other Oncogenic Pathways
Scheffler, M., Ihle, M. A., Hein, R., Merkelbach-Bruse, S., Scheel, A. H., Siemanowski, J., Brägelmann, J., Kron, A., Abedpour, N., Ueckeroth, F., et al. (2019) · Journal of Thoracic Oncology · doi:10.1016/j.jtho.2018.12.013 · Cited by 264 · see citing works
The current state of molecular testing in the treatment of patients with solid tumors, 2019
El‐Deiry, W. S., Goldberg, R. M., Lenz, H., Shields, A. F., Gibney, G. T., Tan, A. R., Brown, J., Eisenberg, B., Heath, E. I., Phuphanich, S., et al. (2019) · CA: A Cancer Journal for Clinicians · doi:10.3322/caac.21560 · Cited by 264 · see citing works
Yeung, M. L., Houzet, L., Yedavalli, V. S. R. K., & Jeang, K. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.010033 · Cited by 263 · see citing works
Martinelli, S., De Luca, A., Stellacci, E., Rossi, C., Checquolo, S., Lepri, F., Caputo, V., Silvano, M., Buscherini, F., Consoli, F., et al. (2010) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2010.06.015 · Cited by 259 · see citing works
Maltese, W. A., & Overmeyer, J. H. (2014) · American Journal Of Pathology · doi:10.1016/j.ajpath.2014.02.028 · Cited by 254 · see citing works
A Comparative Analysis of Individual RAS Mutations in Cancer Biology
Muñoz-Maldonado, C., Zimmer, Y., & Medová, M. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.01088 · Cited by 250 · see citing works
Imamura, Y., Morikawa, T., Liao, X., Lochhead, P. J., Kuchiba, A., Yamauchi, M., Qian, Z. R., Nishihara, R., Meyerhardt, J. A., Haigis, K. M., et al. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-11-3210 · Cited by 249 · see citing works
Molecular Biology of Lung Cancer: Clinical Implications
Larsen, J. E., & Minna, J. D. (2011) · Clinics in Chest Medicine · doi:10.1016/j.ccm.2011.08.003 · Cited by 247 · see citing works
Oxidative phosphorylation in cancer cells
Solaini, G., Sgarbi, G., & Baracca, A. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2010.09.003 · Cited by 231 · see citing works
Large conformational changes in proteins: signaling and other functions
Grant, B. J., Gorfe, A. A., & McCammon, J. A. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2009.12.004 · Cited by 228 · see citing works
Involvement of Autophagy in Oncogenic K-Ras-induced Malignant Cell Transformation
Kim, M. J., Woo, S.-J., Yoon, C., Lee, J., An, S., Choi, Y. H., Hwang, S., Yoon, G., & Lee, S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.138958 · Cited by 225 · see citing works
Phosphorylation by Cdk2 is required for Myc to repress Ras-induced senescence in cotransformation
Hydbring, P., Bahram, F., Su, Y., Tronnersjö, S., Högstrand, K., von der Lehr, N., Sharifi, H. R., Lilischkis, R., Hein, N., Wu, S., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900121106 · Cited by 224 · see citing works
ERK1/2 Regulation of CD44 Modulates Oral Cancer Aggressiveness
Judd, N. P., Winkler, A. E., Murillo, O., Brotman, J. J., Law, J. H., Lewis, J. S., Dunn, G. P., Bui, J. D., Sunwoo, J. B., & Uppaluri, R. (2011) · Cancer Research · doi:10.1158/0008-5472.can-11-1831 · Cited by 223 · see citing works
Suda, K., Tomizawa, K., & Mitsudomi, T. (2010) · Cancer and Metastasis Reviews · doi:10.1007/s10555-010-9209-4 · Cited by 220 · see citing works
Eke, I., Deuse, Y., Hehlgans, S., Gurtner, K., Krause, M., Baumann, M. A., Shevchenko, A., Sandfort, V., & Cordes, N. (2012) · Journal of Clinical Investigation · doi:10.1172/jci61350 · Cited by 220 · see citing works
Young, A., Lou, D., & McCormick, F. (2013) · Cancer Discovery · doi:10.1158/2159-8290.cd-12-0231 · Cited by 211 · see citing works
Little, A. S., Balmanno, K., Sale, M. J., Newman, S., Dry, J. R., Hampson, M., Edwards, P. A., Smith, P. D., & Cook, S. J. (2011) · Science Signaling · doi:10.1126/scisignal.2001752 · Cited by 211 · see citing works
Molecular biology of lung cancer: Clinical implications
Fong, K. M., & Minna, J. D. (2002) · Clinics in Chest Medicine · doi:10.1016/s0272-5231(03)00062-5 · Cited by 210 · see citing works
ERKs in Cancer: Friends or Foes?
Deschênes‐Simard, X., Kottakis, F., Meloche, S., & Ferbeyre, G. (2014) · Cancer Research · doi:10.1158/0008-5472.can-13-2381 · Cited by 210 · see citing works
GTP-Dependent K-Ras Dimerization
Muratcioglu, S., Chavan, T. S., Freed, B. C., Jang, H., Khavrutskii, L., Freed, R. N., Dyba, M. A., Stefanisko, K., Tarasov, S. G., Gursoy, A., et al. (2015) · Structure · doi:10.1016/j.str.2015.04.019 · Cited by 202 · see citing works
Tartaglia, M., & Gelb, B. D. (2010) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2010.05790.x · Cited by 198 · see citing works
The secret life of kinases: functions beyond catalysis
Rauch, J., Volinsky, N., Romano, D., & Kölch, W. (2011) · Cell Communication and Signaling · doi:10.1186/1478-811x-9-23 · Cited by 198 · see citing works
Tumor Suppression and Promotion by Autophagy
Ávalos, Y., Canales, J., Bravo, R., Criollo, A., Lavandero, S., & Quest, A. F. G. (2014) · BioMed Research International · doi:10.1155/2014/603980 · Cited by 197 · see citing works
K-Ras promotes tumorigenicity through suppression of non-canonical Wnt signaling
Wang, M.-T., Holderfield, M., Galeas, J., Delrosario, R., To, M. D., Balmain, A., & McCormick, F. (2015) · Cell · doi:10.1016/j.cell.2015.10.041 · Cited by 196 · see citing works
Warburg effect revisited: an epigenetic link between glycolysis and gastric carcinogenesis
Liu, X., Wang, X., Zhang, J., Lam, E. K. Y., Shin, V. Y., Cheng, A. S. L., Yu, J. Q., Chan, F. K. L., Sung, J. J. �., & Jin, H. (2009) · Oncogene · doi:10.1038/onc.2009.332 · Cited by 195 · see citing works
When ubiquitination meets phosphorylation: a systems biology perspective of EGFR/MAPK signalling
Nguyen, L. K., Kölch, W., & Kholodenko, B. Ν. (2013) · Cell Communication and Signaling · doi:10.1186/1478-811x-11-52 · Cited by 192 · see citing works
Precision Oncology: The Road Ahead
Senft, D., Leiserson, M. D. M., Ruppin, E., & Ronai, Z. A. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.08.003 · Cited by 192 · see citing works
Cooperative Activation of PI3K by Ras and Rho Family Small GTPases
Yang, H. W., Shin, M., Lee, S., Kim, J., Park, W. S., Cho, K., Meyer, T., & Heo, W. D. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.007 · Cited by 191 · 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
Gaedcke, J., Grade, M., Jung, K., Camps, J., Jo, P., Emons, G., Gehoff, A., Sax, U., Schirmer, M., Becker, H., et al. (2010) · Genes Chromosomes and Cancer · doi:10.1002/gcc.20811 · Cited by 187 · 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
Danese, A., Patergnani, S., Bonora, M., Wieckowski, M. R., Previati, M., Giorgi, C., & Pinton, P. (2017) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2017.01.003 · Cited by 184 · see citing works
Grant, B. J., Gorfe, A. A., & McCammon, J. A. (2009) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000325 · Cited by 182 · see citing works
Ubiquitination of K-Ras Enhances Activation and Facilitates Binding to Select Downstream Effectors
Sasaki, A. T., Carracedo, A., Locasale, J. W., Anastasiou, D., Takeuchi, K., Kahoud, E. R., Haviv, S., Asara, J. M., Pandolfi, P. P., & Cantley, L. C. (2011) · Science Signaling · doi:10.1126/scisignal.2001518 · Cited by 182 · see citing works
RAS-mediated oncogenic signaling pathways in human malignancies
Khan, A. Q., Kuttikrishnan, S., Siveen, K. S., Prabhu, K. S., Shanmugakonar, M., Al‐Naemi, H. A., Haris, M., Dermime, S., & Shahab Uddin, M. S. (2018) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2018.03.001 · Cited by 179 · see citing works
Novel Allosteric Sites on Ras for Lead Generation
Grant, B. J., Lukman, S., Hocker, H. J., Sayyah, J., Brown, J. H., McCammon, J. A., & Gorfe, A. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025711 · Cited by 178 · see citing works
Survival of pancreatic cancer cells lacking KRAS function
Muzumdar, M. D., Chen, P.-Y., Dorans, K. J., Chung, K. M., Bhutkar, A., Hong, E., Noll, E. M., Sprick, M. R., Trumpp, A., & Jacks, T. (2017) · Nature Communications · doi:10.1038/s41467-017-00942-5 · Cited by 177 · see citing works
Kaiser, C. E., Ert, N. A. V., Agrawal, P., Chawla, R., Yang, D., & Hurley, L. H. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b02046 · Cited by 176 · see citing works
Metabolic Heterogeneity of Cancer Cells: An Interplay between HIF-1, GLUTs, and AMPK
Moldogazieva, N. T., Mokhosoev, I. M., & Terentiev, A. A. (2020) · Cancers · doi:10.3390/cancers12040862 · Cited by 176 · see citing works
The Transcription Factor FOXM1 (Forkhead box M1)
Wierstra, I. (2013) · Advances in cancer research · doi:10.1016/b978-0-12-407173-5.00004-2 · Cited by 174 · see citing works
Biomarkers That Currently Affect Clinical Practice in Lung Cancer: EGFR, ALK, MET, ROS-1, and KRAS
Korpanty, G. J., Graham, D. M., Vincent, M. D., & Leighl, N. B. (2014) · Frontiers in Oncology · doi:10.3389/fonc.2014.00204 · Cited by 174 · see citing works
Targeting apoptotic and autophagic pathways for cancer therapeutics
Liu, J., Mou, L., Yu, J., Liu, B., & Bao, J. (2010) · Cancer Letters · doi:10.1016/j.canlet.2010.10.001 · Cited by 171 · see citing works
An expanding role for RAS GTPase activating proteins (RAS GAPs) in cancer
Maertens, O., & Cichowski, K. M. (2014) · Advances in Biological Regulation · doi:10.1016/j.jbior.2014.04.002 · Cited by 170 · see citing works
Organization, dynamics, and segregation of Ras nanoclusters in membrane domains
Janosi, L., Li, Z., Hancock, J. F., & Gorfe, A. A. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1200773109 · Cited by 170 · see citing works
Targeting KRAS in metastatic colorectal cancer: current strategies and emerging opportunities
Porru, M., Pompili, L., Caruso, C., Biroccio, A., & Leonetti, C. (2018) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-018-0719-1 · Cited by 170 · see citing works
Big Signals from Small Particles: Regulation of Cell Signaling Pathways by Nanoparticles
Rauch, J., Kölch, W., Laurent, S., & Mahmoudi, M. (2013) · Chemical Reviews · doi:10.1021/cr3002627 · Cited by 169 · see citing works
Jones, R. P., Sutton, P. A., Evans, J. P., Clifford, R., McAvoy, A., Lewis, J., Rousseau, A., Mountford, R., McWhirter, D., & Malik, H. Z. (2017) · British Journal of Cancer · doi:10.1038/bjc.2017.37 · Cited by 166 · see citing works
A KRAS-directed transcriptional silencing pathway that mediates the CpG island methylator phenotype
Serra, R. W., Fang, M., Park, S. M., Hutchinson, L., & Green, M. R. (2014) · eLife · doi:10.7554/elife.02313 · Cited by 166 · see citing works
- Authors
- Karnoub, A. E., & Weinberg, R. A.
- Affiliations
- Whitehead Institute for Biomedical Research (US)
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2008-07
- Volume
- 9
- Issue
- 7
- Pages
- 517-531
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- PMC
- PMC3915522
- OpenAlex
- W2004774286
- Cited by
- 1,467
- References
- 234
- Citations by year
- 2026: 28 · 2025: 48 · 2024: 58 · 2023: 60 · 2022: 67 · 2021: 89 · 2020: 74 · 2019: 87 · 2018: 93 · 2017: 95 · 2016: 103 · 2015: 118 · 2014: 100 · 2013: 108 · 2012: 94
- FWCI
- 6.15
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Cancer Institute (P01 CA08111, U54 CA12515, P01CA080111, P50CA089393)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- oncogenic Ras, carcinogenesis, developmental disorders, downstream effectors, cell physiology, Ras proteins
- MeSH terms
- Amino Acid Sequence, Animals, Cell Transformation, Neoplastic, DNA-Binding Proteins, Enzyme Activation, Gene Expression Regulation, Humans, Models, Molecular, Molecular Sequence Data, Phylogeny, Protein Conformation, Protein Processing, Post-Translational, Genes, ras, Transcription Factors, Signal Transduction, Sequence Alignment, ras Proteins, Phosphatidylinositol 3-Kinases, GTPase-Activating Proteins, Mitogen-Activated Protein Kinases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review