Cited by 1,211Protein Kinase Regulation and GTPase SignalingProtein Tyrosine PhosphatasesCellular transport and secretion

The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.

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

Trahey, Meg, McCormick, Frank·1987·Science

DOI 10.1126/science.2821624

Open this paper in CoChat — free account

Abstract

The role of guanine nucleotides in ras p21 function was determined by using the ability of p21 protein to induce maturation of Xenopus oocytes as a quantitative assay for biological activity. Two oncogenic mutant human N- ras p21 proteins, Asp12 and Val12, actively induced maturation, whereas normal Gly12 p21 was relatively inactive in this assay. Both mutant proteins were found to be associated with guanosine triphosphate (GTP) in vivo. In contrast, Gly12 p21 was predominantly guanosine diphosphate (GDP)-bound because of a dramatic stimulation of Gly12 p21-associated guanosine triphosphatase (GTPase) activity. A cytoplasmic protein was shown to be responsible for this increase in activity. This protein stimulated GTP hydrolysis by purified Gly12 p21 more than 200-fold in vitro, but had no effect on Asp12 or Val12 mutants. A similar factor could be detected in extracts from mammalian cells. It thus appears that, in Xenopus oocytes, this protein maintains normal p21 in a biologically inactive, GDP-bound state through its effect on GTPase activity. Furthermore, it appears that the major effect of position 12 mutations is to prevent this protein from stimulating p21 GTPase activity, thereby allowing these mutants to remain in the active GTP-bound state.

Integrity signals

Registry

Crossref · 10.1126/science.2821624

Cites

23 of 23 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

G proteins and dual control of adenylate cyclase
Gilman, A. G. (1984) · Cell · doi:10.1016/0092-8674(84)90336-2 · Cited by 1,772
Monoclonal antibodies to the p21 products of the transforming gene of Harvey murine sarcoma virus and of the cellular ras gene family
Furth, M. E., Davis, L. J., Fleurdelys, B. E., & Scolnick, E. M. (1982) · Journal of Virology · doi:10.1128/jvi.43.1.294-304.1982 · Cited by 800
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
Structure of the GDP Domain of EF-Tu and Location of the Amino Acids Homologous to ras Oncogene Proteins
JURNAK, F. A. (1985) · Science · doi:10.1126/science.3898365 · Cited by 621
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
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 536
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
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
Changes in protein phosphorylation accompanying maturation of Xenopus laevis oocytes
Maller, J. L., Wu, M. W., & Gerhart, J. C. (1977) · Developmental Biology · doi:10.1016/0012-1606(77)90093-8 · Cited by 276
Partial purification and characterization of the maturation-promoting factor from eggs of Xenopus laevis
Wu, M., & Gerhart, J. C. (1980) · Developmental Biology · doi:10.1016/0012-1606(80)90131-1 · Cited by 245

Flagged first, then by citations

Show all 23 references

Research works printed but not linked: 2

Gibbs, J. B., Proceedings of the National Academy of Sciences of the United States of America 81: 5704 (1984).
Manne, V., Proceedings of the National Academy of Sciences of the United States of America 81: 6953 (1984).

Sorted by citations

Items 101–200 of 999

Purification and characterization from bovine brain cytosol of a protein that inhibits the dissociation of GDP from and the subsequent binding of GTP to smg p25A, a ras p21-like GTP-binding protein.
Sasaki, T., Kikuchi, A., Araki, S., Hata, Y., Isomura, M., Kuroda, S., & Takai, Y. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39980-6 · Cited by 302
The ksr-1 gene encodes a novel protein kinase involved in Ras-mediated signaling in C. elegans
Kornfeld, K., Hom, D. B., & Horvitz, H. R. (1995) · Cell · doi:10.1016/0092-8674(95)90206-6 · Cited by 302
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
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
IRA2, a second gene of Saccharomyces cerevisiae that encodes a protein with a domain homologous to mammalian ras GTPase-activating protein.
Tanaka, K., Nakafuku, M., Tamanoi, F., Kaziro, Y., Matsumoto, K., & Toh‐e, A. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.8.4303 · Cited by 292
Mutational and Kinetic Analyses of the GTPase-Activating Protein (GAP)-p21 Interaction: The C-Terminal Domain of GAP Is Not Sufficient for Full Activity
Gideon, P., John, J., Frech, M., Lautwein, A., Clark, R., Scheffler, J. E., & Wittinghofer, A. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.5.2050 · Cited by 287
The Effect of GTPase Activating Protein Upon Ras Is Inhibited by Mitogenically Responsive Lipids
Tsai, M.-H., Yu, C., Wei, F.-S., & Stacey, D. W. (1989) · Science · doi:10.1126/science.2536192 · Cited by 284
RASA1: variable phenotype with capillary and arteriovenous malformations
Boon, L. M., Mulliken, J. B., & Vikkula, M. (2005) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2005.03.004 · Cited by 282
Insulin stimulation of gene expression mediated by p21ras activation.
Burgering, B. M. T., Medema, R. H., Maassen, J. A., van de Wetering, M., van der Eb, A. J., McCormick, F. P., & Bos, J. L. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb08050.x · Cited by 280
Self-citation
A putative Ras GTPase activating protein acts as a negative regulator of signaling by the Sevenless receptor tyrosine kinase
Gaul, U., Mardon, G., & Rubin, G. M. (1992) · Cell · doi:10.1016/0092-8674(92)90073-l · Cited by 278
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
Purification and characterization from bovine brain cytosol of a novel regulatory protein inhibiting the dissociation of GDP from and the subsequent binding of GTP to rhoB p20, a ras p21-like GTP-binding protein.
Ueda, T., Kikuchi, A., Ohga, N., Yamamoto, J., & Takai, Y. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)38859-3 · Cited by 276
Molecular mechanisms of resistance to the EGFR monoclonal antibody cetuximab
Brand, T. M., Iida, M., & Wheeler, D. L. (2011) · Cancer Biology & Therapy · doi:10.4161/cbt.11.9.15050 · Cited by 287
Tyrosine Kinase-Stimulated Guanine Nucleotide Exchange Activity of Vav in T Cell Activation
Gulbins, E., Coggeshall, K. M., Baier, G., Katzav, S., Burn, P., & Altman, A. (1993) · Science · doi:10.1126/science.8484124 · Cited by 273
The regulation of tyrosine kinase signalling pathways by growth factor and G-protein-coupled receptors
Malarkey, K., BELHAM, C. M., Paul, A., Graham, A. M., McLees, A., Scott, P., & Plevin, R. J. (1995) · Biochemical Journal · doi:10.1042/bj3090361 · Cited by 267
Kinetic and structural analysis of the Mg(2+)-binding site of the guanine nucleotide-binding protein p21H-ras.
John, J., Rensland, H., Schlichting, I., Vetter, I. R., Borasio, G. D., Goody, R. S., & Wittinghofer, A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54022-9 · Cited by 259
Protein-tyrosine kinases regulate the phosphorylation, protein interactions, subcellular distribution, and activity of p21ras GTPase-activating protein.
Moran, M. F., Polakis, P. G., McCormick, F. P., Pawson, T. J., & Ellis, C. A. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.4.1804 · Cited by 266
Self-citation
Yeast BUD5, encoding a putative GDP-GTP exchange factor, is necessary for bud site selection and interacts with bud formation gene BEM1
Chant, J., Corrado, K., Pringle, J. R., & Herskowitz, I. (1991) · Cell · doi:10.1016/0092-8674(91)90016-r · Cited by 265
Identification of a Novel Human Rho Protein with Unusual Properties: GTPase Deficiency and In Vivo Farnesylation
Foster, R., Hu, K., Lu, Y., Nolan, K. M., Thissen, J., & Settleman, J. E. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.6.2689 · Cited by 265
GTP Binding Is Essential to the Protein Kinase Activity of LRRK2, a Causative Gene Product for Familial Parkinson's Disease
Ito, G., Okai, T., Fujino, G., Takeda, K., Ichijo, H., Katada, T., & Iwatsubo, T. (2007) · Biochemistry · doi:10.1021/bi061960m · Cited by 263
Human cutaneous melanoma; a review of NRAS and BRAF mutation frequencies in relation to histogenetic subclass and body site
Platz, A., Egyházi, S., Ringborg, U. K., & Hansson, J. (2007) · Molecular Oncology · doi:10.1016/j.molonc.2007.12.003 · Cited by 277
Molecular cloning and nucleic acid binding properties of the GAP-associated tyrosine phosphoprotein p62
Wong, G. A., Müller, O., Clark, R., Conroy, L., Moran, M. F., Polakis, P. G., & McCormick, F. (1992) · Cell · doi:10.1016/0092-8674(92)90455-l · Cited by 258
Self-citation
Accumulation of p21ras.GTP in response to stimulation with epidermal growth factor and oncogene products with tyrosine kinase activity.
Satoh, T., Endo, M., Nakafuku, M., Akiyama, T., Yamamoto, T., & Kaziro, Y. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.20.7926 · Cited by 257
Targeting KRAS(G12C): From Inhibitory Mechanism to Modulation of Antitumor Effects in Patients
Kim, D., Xue, J. Y., & Lito, P. (2020) · Cell · doi:10.1016/j.cell.2020.09.044 · Cited by 239
Identification of distinct cytoplasmic targets for ras/R-ras and rho regulatory proteins
Garrett, M. D., Self, A. J., van Oers, C., & Hall, A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31215-2 · Cited by 252
Synthesis in Escherichia coli of GTPase-deficient mutants of Gsα
Graziano, M. P., & Gilman, A. G. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84854-8 · Cited by 251
Inhibition of GTPase Activating Protein Stimulation of Ras-p21 GTPase by the K rev -1 Gene Product
Frech, M., John, J., Pizon, V., Chardin, P., Tavitian, A., Clark, R., McCormick, F. P., & Wittinghofer, A. (1990) · Science · doi:10.1126/science.2164710 · Cited by 251
Self-citation
RAS pathways to cell cycle control and cell transformation
Pellicer, À. (1998) · Frontiers in bioscience · doi:10.2741/a331 · Cited by 251
Signal transduction by nerve growth factor and fibroblast growth factor in PC12 cells requires a sequence of src and ras actions.
Kremer, N. E., D’Arcangelo, G., Thomas, S. Μ., DeMarco, M., Brugge, J. S., & Halegoua, S. (1991) · The Journal of Cell Biology · doi:10.1083/jcb.115.3.809 · Cited by 246
IRA1, an inhibitory regulator of the RAS-cyclic AMP pathway in Saccharomyces cerevisiae.
Tanaka, K., Matsumoto, K., & Toh‐e, A. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.2.757 · Cited by 245
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
GAPs for rho-related GTPases
Lamarche, N., & Hall, A. (1994) · Trends in Genetics · doi:10.1016/0168-9525(94)90114-7 · Cited by 244
Cloning and characterization of CAP, the S. cerevisiae gene encoding the 70 kd adenylyl cyclase-associated protein
Field, J. M., Vojtek, A. B., Ballester, R., Bolger, G. B., Colicelli, J., Ferguson, K. M., Gerst, J. E., Kataoka, T., Michaeli, T., Powers, S., et al. (1990) · Cell · doi:10.1016/0092-8674(90)90812-s · Cited by 240
Association of a Ras-related protein with cytochrome b of human neutrophils
Quinn, M. T., Parkos, C. A., Walker, L. E., Orkin, S. H., Dinauer, M. C., & Jesaitis, A. J. (1989) · Nature · doi:10.1038/342198a0 · Cited by 242
ras oncogenes: their role in neoplasia
Barbacid, M. (1990) · European Journal of Clinical Investigation · doi:10.1111/j.1365-2362.1990.tb01848.x · Cited by 242
Probing Protein Structure and Function with an Expanded Genetic Code
Cornish, V. W., Mendel, D., & Schultz, P. G. (1995) · Angewandte Chemie International Edition in English · doi:10.1002/anie.199506211 · Cited by 244
rho family GTPase activating proteins p190, bcr and rhoGAP show distinct specificities in vitro and in vivo
Ridley, A. J., Self, A. J., Kasmi, F., Paterson, H. F., Hall, A., Marshall, C. J., & Ellis, C. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb06210.x · Cited by 238
Identification of a human rasGAP-related protein containing calmodulin-binding motifs.
Weissbach, L., Settleman, J. E., Kalady, M. F., Snijders, A. J., Murthy, A. E., Yan, Y. X., & Bernards, A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32023-9 · Cited by 235
ras p21 and GAP inhibit coupling of muscarinic receptors to atrial K+ channels
Yatani, A., Okabe, K., Polakis, P. G., Halenbeck, R., McCormick, F. P., & Brown, A. M. (1990) · Cell · doi:10.1016/0092-8674(90)90187-j · Cited by 230
Self-citation
KRAS Mutations in Lung Cancer
Karachaliou, N., Mayo, C., Costa, C., Magrí, I., Giménez-Capitán, A. A., Molina‐Vila, M. Á., & Rosell, R. (2012) · Clinical Lung Cancer · doi:10.1016/j.cllc.2012.09.007 · Cited by 241
Regulators of G-Protein Signaling and Their Gα Substrates: Promises and Challenges in Their Use as Drug Discovery Targets
Kimple, A. J., Bosch, D. E., Giguère, P. M., & Siderovski, D. P. (2011) · Pharmacological Reviews · doi:10.1124/pr.110.003038 · Cited by 238
The role of G proteins in transmembrane signalling
Taylor, C. W. (1990) · Biochemical Journal · doi:10.1042/bj2720001 · Cited by 227
Biological and clinical significance of KRAS mutations in lung cancer: an oncogenic driver that contrasts with EGFR mutation
Suda, K., Tomizawa, K., & Mitsudomi, T. (2010) · Cancer and Metastasis Reviews · doi:10.1007/s10555-010-9209-4 · Cited by 226
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
GTPase activating proteins: critical regulators of intracellular signaling
Donovan, S., Shannon, K., & Bollag, G. E. (2002) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/s0304-419x(01)00041-5 · Cited by 215
Identification and characterization of the neurofibromatosis type 1 protein product.
DeClue, J. E., Cohen, B. D., & Lowy, D. R. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.22.9914 · Cited by 215
Frequency and Spectrum of Mutations at Codons 12 and 13 of the C-K-ras Gene in Human Tumors
Capellá, G., Cronauer-Mitra, S., Pienado, M. A., & Perucho, M. (1991) · Environmental Health Perspectives · doi:10.1289/ehp.9193125 · Cited by 212
Relationship Among Guanine Nucleotide Exchange, GTP Hydrolysis, and Transforming Potential of Mutated ras Proteins
Feig, L. A., & Cooper, G. M. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.6.2472-2478.1988 · Cited by 213
The Function of Ras Genes in Saccharomyces Cerevisiae
Broach, J. R., & Deschenes, R. J. (1990) · Advances in cancer research · doi:10.1016/s0065-230x(08)60809-x · Cited by 213
Dominant inhibitory mutations in the Mg(2+)-binding site of RasH prevent its activation by GTP.
Farnsworth, C. L., & Feig, L. A. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.10.4822 · Cited by 211
Ras-catalyzed hydrolysis of GTP: a new perspective from model studies.
Maegley, K. A., Admiraal, S. J., & Herschlag, D. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.16.8160 · Cited by 208
Tyrosine-phosphorylated SOCS-3 inhibits STAT activation but binds to p120 RasGAP and activates Ras
Cacalano, N. A., Sanden, D., & Johnston, J. A. (2001) · Nature Cell Biology · doi:10.1038/35074525 · Cited by 210
Acylation of viral and eukaryotic proteins
Grand, R. J. A. (1989) · Biochemical Journal · doi:10.1042/bj2580625 · Cited by 209
Formation of a Transition-State Analog of the Ras GTPase Reaction by Ras·GDP, Tetrafluoroaluminate, and GTPase-Activating Proteins
Mittal, R., Ahmadian, M. R., Goody, R. S., & Wittinghofer, A. (1996) · Science · doi:10.1126/science.273.5271.115 · Cited by 202
p21ras activation via hemopoietin receptors and c-kit requires tyrosine kinase activity but not tyrosine phosphorylation of p21ras GTPase-activating protein.
Duronio, V., Welham, M. J., Abraham, S., Dryden, P., & Schrader, J. W. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.5.1587 · Cited by 205
The ras oncogene--an important regulatory element in lower eucaryotic organisms
Gibbs, W. W., & Marshall, M. S. (1989) · Microbiological Reviews · doi:10.1128/mr.53.2.171-185.1989 · Cited by 205
Mutations in the GTP-binding site of GSα alter stimulation of adenylyl cyclase
Masters, S. B., Miller, R. T., Chi, M. H., Chang, F. H., Beiderman, B., Lopez, N. G., & Bourne, H. R. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84853-6 · Cited by 202
The N‐terminal region of GAP regulates cytoskeletal structure and cell adhesion.
McGlade, J. C., Brunkhorst, B. A., Anderson, D. M., Mbamalu, G., Settleman, J. E., Dedhar, S., Rozakis-Adcock, M., Chen, L. B., & Pawson, T. J. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05976.x · Cited by 202
Prognostic importance of mutations in the ras proto-oncogenes in de novo acute myeloid leukemia
Neubauer, A., Dodge, R., George, S., Davey, F. R., Silver, R., Schiffer, C., Mayer, R. J., Ball, E., Wurster‐Hill, D. H., & Bloomfield, C. (1994) · Blood · doi:10.1182/blood.v83.6.1603.bloodjournal8361603 · Cited by 199
Raf-1 kinase is essential for early Xenopus development and mediates the induction of mesoderm by FGF
MacNicol, A. M., Muslin, A. J., & Williams, L. T. (1993) · Cell · doi:10.1016/0092-8674(93)90143-e · Cited by 197
Cross-linking of Fc gamma receptor I (Fc gamma RI) and receptor II (Fc gamma RII) on monocytic cells activates a signal transduction pathway common to both Fc receptors that involves the stimulation of p72 Syk protein tyrosine kinase.
Kiener, P. A., Rankin, B. M., Burkhardt, A. L., Schieven, G. L., Gilliland, L. K., Rowley, R. B., Bolen, J. B., & Ledbetter, J. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80545-6 · Cited by 196
Shc is the predominant signaling molecule coupling insulin receptors to activation of guanine nucleotide releasing factor and p21ras-GTP formation.
Sasaoka, T., Draznin, B., Leitner, J. W., Langlois, W. J., & Olefsky, J. M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34120-0 · Cited by 193
Ly-GDI, a GDP-dissociation inhibitor of the RhoA GTP-binding protein, is expressed preferentially in lymphocytes.
Scherle, P., Behrens, T., & Staudt, L. M. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.16.7568 · Cited by 195
Analysis of Activated GAPs and GEFs in Cell Lysates
García‐Mata, R., Wennerberg, K., Arthur, W. T., Hooten, N. N., Ellerbroek, S. M., & Burridge, K. (2006) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(06)06031-9 · Cited by 191
Homoleptic Phosphoraneiminato Complexes of Rare Earth Elements as Initiators for Ring-Opening Polymerization of Lactones
Gröb, T., Seybert, G., Massa, W., Weller, F., Palaniswami, R., Greiner, A., & Dehnicke, K. (2000) · Angewandte Chemie International Edition · doi:10.1002/1521-3773(20001201)39:23 · Cited by 33
Negative Feedback Regulation and Desensitization of Insulin- and Epidermal Growth Factor-stimulated p21ras Activation
Langlois, W. J., Sasaoka, T., Saltiel, A. R., & Olefsky, J. M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.43.25320 · Cited by 187
Structural requirements for the interaction of p21ras with GAP, exchange factors, and its biological effector target
Polakis, P. G., & McCormick, F. P. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98325-0 · Cited by 186
Self-citation
Regulation of DNA Methylation by the Ras Signaling Pathway
MacLeod, A. R., Rouleau, J., & Moshe Szyf, A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.19.11327 · Cited by 185
Ras Activation by Insulin and Epidermal Growth Factor through Enhanced Exchange of Guanine Nucleotides on p21ras
Medema, R. H., de Vries-Smits, A. M. M., van der Zon, G. C. M., Maassen, J. A., & Bos, J. L. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.1.155-162.1993 · Cited by 183
The biochemistry of ras p21
Grand, R. J. A., & Owen, D. (1991) · Biochemical Journal · doi:10.1042/bj2790609 · Cited by 181
ras and GAP—Who's controlling whom?
Hall, A. (1990) · Cell · doi:10.1016/0092-8674(90)90054-i · Cited by 180
Mismatch repair, molecular switches, and signal transductionPreprint
Fishel, R. A. (1998) · Genes & Development · doi:10.1101/gad.12.14.2096 · Cited by 177
Structural analysis of the GAP‐related domain from neurofibromin and its implications
Scheffzek, K., Ahmadian, M. R., Wiesmüller, L., Kabsch, W., Stege, P., Schmitz, F., & Wittinghofer, A. (1998) · The EMBO Journal · doi:10.1093/emboj/17.15.4313 · Cited by 181
Purification and characterization of Rac 2. A cytosolic GTP-binding protein that regulates human neutrophil NADPH oxidase.
Knaus, U. G., Heyworth, P. G., Kinsella, B. T., Curnutte, J. T., & Bokoch, G. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35877-0 · Cited by 176
A novel small molecular weight GTP-binding protein with the same putative effector domain as the ras proteins in bovine brain membranes. Purification, determination of primary structure, and characterization.
Kawata, M., Matsui, Y., Kondo, J. D. M., HISHIDA, T., Teranishi, Y., & Takai, Y. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37376-9 · Cited by 176
The ras superfamily of small GTP-binding proteins
Downward, J. (1990) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(90)90300-z · Cited by 175
Perfect and Near-Perfect Adaptation in Cell Signaling
Ferrell, J. E. (2016) · Cell Systems · doi:10.1016/j.cels.2016.02.006 · Cited by 168
Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras
Scheffzek, K., Lautwein, A., Kabsch, W., Ahmadian, M. R., & Wittinghofer, A. (1996) · Nature · doi:10.1038/384591a0 · Cited by 173
Tumor suppressor genes: the p53 and retinoblastoma sensitivity genes and gene products
Levine, A. J. (1990) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/0304-419x(90)90015-s · Cited by 173
Direct Interaction between Ras and the Kinase Domain of Mitogen-activated Protein Kinase Kinase Kinase (MEKK1)
Russell, M., Lange, C. A., & Johnson, G. L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.20.11757 · Cited by 172
A Conserved Alternative Splice in the von Recklinghausen Neurofibromatosis ( NF1 ) Gene Produces Two Neurofibromin Isoforms, Both of Which Have GTPase-Activating Protein Activity
Andersen, L. B., Ballester, R., Marchuk, D. A., Chang, E. C., Gutmann, D. H., Saulino, A. M., Camonis, J., Wigler, M. H., & Collins, F. S. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.1.487-495.1993 · Cited by 172
Molecular Cloning and Expression of a G25K cDNA, the Human Homolog of the Yeast Cell Cycle Gene CDC42
Munemitsu, S. M., Innis, M. A., Clark, R., McCormick, F. P., Ullrich, A., & Polakis, P. G. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.11.5977 · Cited by 173
Self-citation
Identification of the catalytic domains and their functionally critical arginine residues of two yeast GTPase‐activating proteins specific for Ypt/Rab transport GTPases
Albert, Š., Will, E., & Gallwitz, D. (1999) · The EMBO Journal · doi:10.1093/emboj/18.19.5216 · Cited by 168
A yeast GTPase-activating protein that interacts specifically with a member of the Ypt/Rab family
Strom, M., Vollmer, P., Tan, T. J., & Gallwitz, D. (1993) · Nature · doi:10.1038/361736a0 · Cited by 168
The neurofibromatosis type 1 gene and its protein product, neurofibromin
Gutmann, D. H., & Collins, F. S. (1993) · Neuron · doi:10.1016/0896-6273(93)90324-k · Cited by 168
Detection of K-ras mutations in lung carcinomas: Relationship to prognosis
De Michele, M. A. A. (1996) · Lung Cancer · doi:10.1016/s0169-5002(96)80041-9 · Cited by 167
Relevance of ultraviolet-induced N-ras oncogene point mutations in development of primary human cutaneous melanoma.
van Elsas, A., Zerp, S. F., van der Flier, S., Krüse, K. M., Aarnoudse, C. A., Hayward, N. K., Ruiter, D. J., & Schrier, P. I. (1996) · Europe PMC (PubMed Central) · Cited by 160
Dominant Inhibitory Ras Mutants Selectively Inhibit the Activity of Either Cellular or Oncogenic Ras
Stacey, D. W., Feig, L. A., & Gibbs, W. W. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.8.4053 · Cited by 163
ERK1/2 inhibitors: New weapons to inhibit the RAS-regulated RAF-MEK1/2-ERK1/2 pathway
Kidger, A. M., Sipthorp, J., & Cook, S. J. (2018) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.02.007 · Cited by 166
RabGDI Displacement by DrrA from Legionella Is a Consequence of Its Guanine Nucleotide Exchange Activity
Schoebel, S., Oesterlin, L. K., Blankenfeldt, W., Goody, R. S., & Itzen, A. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.11.014 · Cited by 161
Role of Proto-Oncogene Activation in Carcinogenesis
Anderson, M. W., Reynolds, S. H., You, M., & Maronpot, R. M. (1992) · Environmental Health Perspectives · doi:10.1289/ehp.929813 · Cited by 161
Dominant yeast and mammalian RAS mutants that interfere with the CDC25-dependent activation of wild-type RAS in Saccharomyces cerevisiae.
Powers, S., O’Neill, K. E., & Wigler, M. H. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.2.390 · Cited by 161
p21ras couples the T cell antigen receptor to extracellular signal-regulated kinase 2 in T lymphocytes.
Izquierdo, M., Leevers, S. J., Marshall, C., & Cantrell, D. A. (1993) · The Journal of Experimental Medicine · doi:10.1084/jem.178.4.1199 · Cited by 161
Progress on Ras/MAPK Signaling Research and Targeting in Blood and Solid Cancers
Dillon, M., Lopez, A. R., Lin, E., Sales, D., Perets, R., & Jain, P. (2021) · Cancers · doi:10.3390/cancers13205059 · Cited by 175
A C‐terminal domain of GAP is sufficient to stimulate ras p21 GTPase activity.
Marshall, M. S., Hill, W. S., Ng, A. S., Vogel, U. S., Schaber, M. D., Scolnick, E. M., Dixon, R. A., Sigal, I. S., & Gibbs, W. W. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03480.x · Cited by 159
Drugging KRAS: Current perspectives and state-of-art review
Parikh, K., Banna, G., Liu, S. V., Friedlaender, A., Desai, A., Subbiah, V., & Addeo, A. (2022) · Journal of Hematology & Oncology · doi:10.1186/s13045-022-01375-4 · Cited by 164
KRAS(G12D) can be targeted by potent inhibitors via formation of salt bridge
Mao, Z., Xiao, H., Shen, P., Yang, Y., Xue, J., Yang, Y., Shang, Y., Zhang, L., Li, X., Zhang, Y., et al. (2022) · Cell Discovery · doi:10.1038/s41421-021-00368-w · Cited by 158
Molecular cloning and characterization of a novel type of regulatory protein (GDI) for smg p25A, a ras p21-like GTP-binding protein.
Matsui, Y., Kikuchi, A., Araki, S., Hata, Y., Kondo, J. D. M., Teranishi, Y., & Takai, Y. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.8.4116 · Cited by 157
Suppression of c-ras transformation by GTPase-activating protein
Zhang, K., DeClue, J. E., Vass, W. C., Papageorge, A. G., McCormick, F. P., & Lowy, D. R. (1990) · Nature · doi:10.1038/346754a0 · Cited by 157
Self-citation
Activation of the Cellular Proto-Oncogene Product p21Ras by Addition of a Myristylation Signal
Buss, J. E., Solski, P. A., Schaeffer, J., Macdonald, M. J., & Der, C. J. (1989) · Science · doi:10.1126/science.2648572 · Cited by 156

Authors: Trahey, M., & McCormick, F.
Affiliations: Department of Molecular Biology, Cetus Corporation, Emeryville, CA 94608.
ORCID: McCormick, Frank
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 1987-10-23
Volume: 238
Issue: 4826
Pages: 542-545
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.2821624
OpenAlex: W2058511768
Cited by: 1,211
References: 23
Citations by year: 2026: 12 · 2025: 19 · 2024: 19 · 2023: 12 · 2022: 12 · 2021: 19 · 2020: 14 · 2019: 9 · 2018: 17 · 2017: 18 · 2016: 20 · 2015: 17 · 2014: 10 · 2013: 9 · 2012: 18
FWCI: 32.07
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
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: GTPase activity, GDP-bound state, GTP hydrolysis, cytosolic proteins, guanine nucleotides
MeSH terms: Animals, Biological Assay, Cytoplasm, Female, Guanine Nucleotides, Guanosine Diphosphate, Guanosine Triphosphate, Guanylyl Imidodiphosphate, Hydrolysis, Immunosorbent Techniques, Mutation, Oocytes, Phosphoric Monoester Hydrolases, Proteins, Proto-Oncogene Proteins, Structure-Activity Relationship, Xenopus laevis, Proto-Oncogene Proteins p21(ras), GTP Phosphohydrolases

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

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

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks