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

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

Neurofibromatosis type 1 as a model system to study molecular mechanisms of autism spectrum disorder symptoms

Molosh, A. I., & Shekhar, A. (2018) · Progress in brain research · doi:10.1016/bs.pbr.2018.09.014 · Cited by 24

Small GTP binding proteins and bacterial virulence

Boquet, P. (2000) · Microbes and Infection · doi:10.1016/s1286-4579(00)90369-1 · Cited by 22

The ras superfamily of molecular switches

Macara, I. G. (1991) · Cellular Signalling · doi:10.1016/0898-6568(91)90043-t · Cited by 22

A GTPase-activating protein for rhoB p20, a ras p21-like GTP-binding protein — partial purification, characterization and subcellular distribution in rat brain

Yamamoto, J., Kikuchi, A., Ueda, T., Ohga, N., & Takai, Y. (1990) · Molecular Brain Research · doi:10.1016/0169-328x(90)90054-h · Cited by 22

Analysis of mutations of neurofibromatosis type 1 gene and N‐ ras gene in acute myelogenous leukemia

Lee, Y. Y., Kim, W. S., Jung, T. J., Choi, I. Y., Kim, W. S., Bang, Y., Jung, C. W., Park, S., Kim, B. K., Kim, N. K., et al. (1995) · Stem Cells · doi:10.1002/stem.5530130514 · Cited by 22

Modulation of maturation and ribosomal protein S6 phosphorylation in Xenopus oocytes by microinjection of oncogenic ras protein and protein kinase C.

Kamata, T., & Kung, H. F. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.3.880 · Cited by 22

A mutation in the putative Mg(2+)-binding site of Gs alpha prevents its activation by receptors.

Hildebrandt, J. D., Day, R., Farnsworth, C. L., & Feig, L. A. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.10.4830 · Cited by 22

Human T lymphocytes

Reinherz, E. L. (1986) · Springer eBooks · Cited by 22

SH3 domain regulation of RhoGAP activity: Crosstalk between p120RasGAP and DLC1 RhoGAP

Chau, J. E., Vish, K. J., Boggon, T. J., & Stiegler, A. L. (2022) · Nature Communications · doi:10.1038/s41467-022-32541-4 · Cited by 21

A novel RASA1 mutation causing capillary malformation–arteriovenous malformation (CM–AVM) presenting during pregnancy

Durrington, H. J., Firth, H. V., Patient, C. J., Belham, M., Jayne, D. R. W., Burrows, N., Morrell, N. W., & Chilvers, E. R. (2013) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.35935 · Cited by 21

Detection of functional protein domains by unbiased genome-wide forward genetic screening

Herzog, M., Puddu, F., Coates, J., Geisler, N. J., Forment, J. V., & Jackson, S. P. (2018) · Scientific Reports · doi:10.1038/s41598-018-24400-4 · Cited by 22

Neurofibromin: Protein Domains and Functional Characteristics

Scheffzek, K., & Welti, S. (2012) · Springer eBooks · doi:10.1007/978-3-642-32864-0_20 · Cited by 21

P120-GAP associated with syndecan-2 to function as an active switch signal for Src upon transformation with oncogenic ras

Huang, J., Chen, C.-L., & Chuang, N. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.02.045 · Cited by 21

The Ultraviolet Fingerprint Dominates the Mutational Spectrum of the p53 and Ha-ras Genes in Psoralen + Ultraviolet A Keratoses from Psoriasis Patients

Wolf, P., Kreimer-Erlacher, H., Seidl, H., Bäck, B., Soyer, H. P., & Kerl, H. (2004) · Journal of Investigative Dermatology · doi:10.1046/j.0022-202x.2004.22118.x · Cited by 21

Wild-type and Ras-transformed fibroblasts display differential mitogenic responses to transient sodium arsenite exposure

Trouba, K. J., Glanzer, J. G., & Vorce, R. L. (1999) · Toxicological Sciences · doi:10.1093/toxsci/50.1.72 · Cited by 21

The ras family of oncogenes

Der, C. J. (1989) · Cancer treatment and research · doi:10.1007/978-1-4613-1599-5_4 · Cited by 20

Modification of the function of pertussis toxin substrate GTP-binding protein by cholera toxin-catalyzed ADP-ribosylation.

Iiri, T., Ohoka, Y., Ui, M., & Katada, T. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48389-5 · Cited by 21

Activation of Raf-1 in Human Pancreatic Adenocarcinoma

Berger, D. H., Jardines, L. A., Chang, H., & Ruggeri, B. (1997) · Journal of Surgical Research · doi:10.1006/jsre.1997.5022 · Cited by 21

RNA aptamers that specifically bind to the Ras‐binding domain of Raf‐1

Kimoto, M., Sakamoto, K., Shirouzu, M., Hirao, I., & Yokoyama, S. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01572-5 · Cited by 21

Characterization of human platelet GTPase activating protein for the Ral GTP-binding protein

Bhullar, R. P., & Seneviratne, H. D. (1996) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(96)00002-x · Cited by 21

The current state of oncogenes and cancer: Experimental approaches for analyzing oncogenetic events in human cancer

Chiao, P. J., Bischoff, F. Z., Strong, L. C., & Tainsky, M. A. (1990) · Cancer and Metastasis Reviews · doi:10.1007/bf00047589 · Cited by 22

H- ras Mutants Lacking the Epitope for the Neutralizing Monoclonal Antibody Y13-259 Show Decreased Biological Activity and Are Deficient in GTPase-Activating Protein Interaction

Srivastava, S. K., Donato, A. D., & Lacal, J. C. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.4.1779-1783.1989 · Cited by 21

rho GAP of 28 kDa (GAP2), but not of 190 kDa (p190), requires Asp65 and Asp67 of rho GTPase for its activation.

Morii, N., Kumagai, N., Nur-e-Kamal, M. S. A., Narumiya, S., & Maruta, H. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74231-8 · Cited by 21

Regulation of Tetradecanoyl Phorbol Acetate-Induced Responses in NIH 3T3 Cells by GAP, the GTPase-Activating Protein Associated with p21c-ras

Nori, M., L’Allemain, G., & Weber, M. J. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.3.936-945.1992 · Cited by 21

Treatment of KRAS-Mutated Pancreatic Cancer: New Hope for the Patients?

Krupa, K., Fudalej, M. M., Włoszek, E., Miski, H., Badowska-Kozakiewicz, A. M., Mękal, D., Budzik, M. P., Czerw, A. I., & Deptała, A. (2025) · Cancers · doi:10.3390/cancers17152453 · Cited by 21

A brief history of RAS and the RAS Initiative

McCormick, F. P. (2022) · Advances in cancer research · doi:10.1016/bs.acr.2021.07.003 · Cited by 20

Classic Ras Proteins Promote Proliferation and Survival via Distinct Phosphoproteome Alterations in Neurofibromin-Null Malignant Peripheral Nerve Sheath Tumor Cells

Brossier, N. M., Prechtl, A. M., Longo, J. F., Barnes, S., Wilson, L. S., Byer, S. J., Brosius, S. N., & Carroll, S. L. (2015) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000201 · Cited by 20

Genetic Aspects of Cancer

Goddard, A. D., & Solomon, E. (1993) · Springer eBooks · doi:10.1007/978-1-4615-3010-7_4 · Cited by 22

Purification, characterization, and cellular localization of the 100-kDa human placental GTPase-activating protein.

Zhang, Y., Zhang, G., Mollat, P., Carles, C., Riva, M., Frobert, Y., Malassiné, A., Rostène, W. H., Thang, D. C., & Beltchev, B. G. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)46708-1 · Cited by 20

Mechanisms for the activation/electron transfer of neutrophil NADPH-oxidase complex and molecular pathology of chronic granulomatous disease

Umeki, S. (1994) · Annals of Hematology · doi:10.1007/bf01695032 · Cited by 20

Tyrosine phosphorylation of Ras GTPase-activating protein stabilizes its association with p62 at membranes of v-Src transformed cells.

Park, S., & Jove, R. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74450-0 · Cited by 20

Identification of p125, a component of a group of 120-kDa proteins that are phosphorylated on tyrosine residues in response to bradykinin and bombesin stimulation, in anti-ras-GTPase-activating protein immunoprecipitates of Swiss 3T3 cells.

Leeb-Lundberg, L. M. F., & Song, X. H. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53074-x · Cited by 20

Inhibition of v-src-Induced Transformation by a GTPase-Activating Protein

Nori, M., Vogel, U. S., Gibbs, W. W., & Weber, M. J. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.5.2812-2818.1991 · Cited by 20

It took a long, long time: Ras and the race to cure cancer

Weinberg, R. A. (2024) · Cell · doi:10.1016/j.cell.2024.02.042 · Cited by 19

New insights into RAS biology reinvigorate interest in mathematical modeling of RAS signaling

Erickson, K. E., Rukhlenko, O. S., Posner, R. G., Hlavacek, W. S., & Kholodenko, B. Ν. (2018) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2018.02.008 · Cited by 21

GAPs

Kahn, R. (2011) · Cellular Logistics · doi:10.4161/cl.1.2.15153 · Cited by 19

The β-Subunit of the Signal Recognition Particle Receptor Is a Novel GTP-binding Protein without Intrinsic GTPase Activity

Legate, K. R., & Andrews, D. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302158200 · Cited by 19

Limited Proteolysis and Amino Acid Replacements in the Effector Region ofThermus thermophilusElongation Factor Tu

Zeidler, W., Schirmer, N. K., Egle, C., Ribeiro, S., Kreutzer, R., & Sprinzl, M. (1996) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1996.0265u.x · Cited by 19

Regulation of the GTPase activity of the ras-related rap2 protein

Janoueix‐Lerosey, I., Polakis, P. G., Tavitian, A., & de Gunzburg, J. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)91580-j · Cited by 19

A novel human RasGAP‐like gene that maps within the prostate cancer susceptibility locus at chromosome 1q25

Noto, S., Maeda, T., Hattori, S., Inazawa, J., Imamura, M., Asaka, M., & Hatakeyama, M. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01530-0 · Cited by 19

Agonist-induced association of the p21rasGTPase-activating protein with phosphatidylinositol 3-kinase

Sjölander, A., & Lapetina, E. G. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)90245-g · Cited by 19

Comparison of the computed three-dimensional structures of oncogenic forms (bound to GDP) of theras-Gene-Encoded p21 protein with the structure of the normal (non-transforming) wild-type protein

Monaco, R. R., Chen, J., Chung, D. L., Brandt‐Rauf, P. W., & Pincus, M. R. (1995) · Journal of Protein Chemistry · doi:10.1007/bf01888140 · Cited by 19

A Dominant Activating Mutation in the Effector Region of RAS Abolishes IRA2 Sensitivity

Tanaka, K., Wood, D. R., Lin, B. K., Khalil, M., Tamanoi, F., & Cannon, J. F. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.2.631 · Cited by 19

Evidence for Multiple, ras-like, Guanine Nucleotide-binding Proteins in Swiss 3T3 Plasma Membranes

Wolfman, A., Moscucci, A., & Macara, I. G. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)81694-5 · Cited by 19

Platelet Activation and Inhibition

Peterson, S. N., & Lapetina, E. G. (1994) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1994.tb12030.x · Cited by 19

Quantitative analysis of SH2 domain binding. Evidence for specificity and competition.

Wood, E. R., McDonald, O. B., & Sahyoun, N. E. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49689-0 · Cited by 19

Genetic Definition of ras Effector Elements

Stone, J. C., & Blanchard, R. A. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.12.6158 · Cited by 19

A G-protein signaling network mediated by an RGS proteinPreprint

Guan, K., & Han, M. (1999) · Genes & Development · doi:10.1101/gad.13.14.1763 · Cited by 19

Closing the GAP in a signal transduction pathway

Parsons, J. T. (1990) · Trends in Genetics · doi:10.1016/0168-9525(90)90155-y · Cited by 19

The Bovine Papillomavirus E5 Oncogene Can Cooperate with ras: Identification of p21 Amino Acids Critical for Transformation by c-ras H but Not v-ras H

Willumsen, B. M., Vass, W. C., Velu, T. J., Papageorge, A. G., Schiller, J. T., & Lowy, D. R. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.12.6026-6033.1991 · Cited by 19

Mutation profiling in chinese patients with metastatic colorectal cancer and its correlation with clinicopathological features and anti-EGFR treatment response

Li, Z.-Z., Wang, F., Zhang, Z.-C., Wang, F., Zhao, Q., Zhang, D.-S., Wang, F.-H., Wang, D., Luo, H., He, M.-M., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.8541 · Cited by 18

Mechanistic insights from animal models of neurofibromatosis type 1 cognitive impairment

Miller, A. H., & Halloran, M. C. (2022) · Disease Models & Mechanisms · doi:10.1242/dmm.049422 · Cited by 18

No evidence of oncogenic KRAS mutations in squamous cell carcinomas of the anogenital tract and head and neck region independent of human papillomavirus and p16INK4a status

Prigge, E., Urban, K., Stiegler, S., Müller, M., Kloor, M., Mai, S., Ottstadt, M., Lohr, F., Wenz, F. K., Wagner, S., et al. (2014) · Human Pathology · doi:10.1016/j.humpath.2014.08.001 · Cited by 18

Oncogenes and Tumor Suppressor Genes: New Biochemical Tests

Diamandis, E. P. (1992) · Critical Reviews in Clinical Laboratory Sciences · doi:10.3109/10408369209114603 · Cited by 18

HRAS T81C polymorphism modulates risk of urinary bladder cancer and predicts advanced tumors in ethnic Kashmiri population

Pandith, A. A., Shah, Z. A., Khan, N. P., Baba, K. M., Wani, M. S., & Siddiqi, M. A. (2011) · Urologic Oncology Seminars and Original Investigations · doi:10.1016/j.urolonc.2011.03.004 · Cited by 18

The CCS1 gene from Saccharomyces cerevisiae which is involved in mitochondrial functions is identified as IRA2 an attenuator of RAS1 and RAS2 gene products

Bussereau, F., Dupont, C.-H., Boy‐Marcotte, E., Mallet, L., & Jacquet, M. (1992) · Current Genetics · doi:10.1007/bf00351690 · Cited by 18

Ras mutations in human leukemia and related disorders

Greenberger, J. S. (1989) · The International Journal Of Cell Cloning · doi:10.1002/stem.5530070603 · Cited by 18

Development of Keratoacanthomas and Squamous Cell Carcinomas in Transgenic Rabbits with Targeted Expression of EJras. Oncogene in Epidermis

Peng, X., Griffith, J. W., Han, R., Lang, C., & Kreider, J. W. (1999) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65125-5 · Cited by 18

Clostridial ADP-ribosyltransferases ? Modification of low molecular weight GTP-binding proteins and of actin by clostridial toxins

Aktories, K. (1990) · Medical Microbiology and Immunology · doi:10.1007/bf00202390 · Cited by 18

Detection of Ki- ras and p53 gene mutations in tissue and pancreatic juice from pancreatic adenocarcinomas

Kondoh, S., Kaino, M., Okita, S., Ryozawa, S., Akiyama, T., & Okita, K. (1998) · Journal of Gastroenterology · doi:10.1007/s005350050101 · Cited by 18

A1H-15N NM R study of human c-Ha-ras protein: Biosynthetic incorporation of15N-labeled amino acids

Yamasaki, K., Muto, Y., Ito, Y., Walchli, M. R., Miyazawa, T., Nishimura, S., & Yokoyama, S. (1992) · Journal of Biomolecular NMR · doi:10.1007/bf02192801 · Cited by 18

Structural effects of the binding of GTP to the wild-type and oncogenic forms of theras-gene-encoded p21 proteins

Monaco, R. R., Chen, J., Friedman, F. K., Brandt‐Rauf, P. W., Chung, D. L., & Pincus, M. R. (1995) · Journal of Protein Chemistry · doi:10.1007/bf01886911 · Cited by 18

The induction of Egr-1 expression by v-Fps is via a protein kinase C-independent intracellular signal that is sequentially dependent upon HaRas and Raf-1.

Alexandropoulos, K., Qureshi, S. A., Bruder, J. T., Rapp, U. R., & Foster, D. A. (1992) · PubMed · Cited by 18

Aphanin, a triterpenoid from Amoora rohituka inhibits K-Ras mutant activity and STAT3 in pancreatic carcinoma cells

Rabi, T., & Catapano, C. V. (2016) · Tumor Biology · doi:10.1007/s13277-016-5102-2 · Cited by 17

Specific Regulation of Point-Mutated K- ras -Immortalized Cell Proliferation by a Photodynamic Antisense Strategy

Higuchi, M., Yamayoshi, A., Kato, K., Kobori, A., Wake, N., & Murakami, A. (2009) · Oligonucleotides · doi:10.1089/oli.2008.0173 · Cited by 17

Activation of extracellular signal-regulated kinase in lung tissues of mice treated with carcinogen

Yano, T., Yano, Y., Nagashima, Y., Yuasa, M., Yajima, S., Horikawa, S., Hagiwara, K., Kishimoto, M., Ichikawa, T., & Otani, S. (1998) · Life Sciences · doi:10.1016/s0024-3205(98)00558-x · Cited by 17

Differential and dose-dependent regulation of gene expression at the mid-hindbrain boundary by Ras–MAP kinase signaling

Vennemann, A., Agoston, Z., & Schulte, D. (2008) · Brain Research · doi:10.1016/j.brainres.2008.01.100 · Cited by 17

A novel isoform of the neurofibromatosis type-1 mRNA and a switch of isoforms during murine cell differentiation and proliferation

萬谷, 昭., Wakasugi, S., Yokota, Y., Abe, K., Yukitaka, U., & Yamamura, K. (1994) · Gene · doi:10.1016/0378-1119(94)90695-5 · Cited by 17

A Universal Expression–Purification System Based on the Coiled–Coil Interaction of Myosin Heavy Chain

Wolber, V., Maéda, K., Schumann, R., Brandmeier, B., Wiesmüller, L., & Wittinghofer, A. (1992) · Nature Biotechnology · doi:10.1038/nbt0892-900 · Cited by 17

Deletions within the Amino-Terminal Half of the c-src Gene Product That Alter the Functional Activity of the Protein

Nemeth, S. P., Fox, L., DeMarco, M. J., & Brugge, J. S. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.3.1109-1119.1989 · Cited by 17

The Saccharomyces cerevisiae SDC25 C-Domain Gene Product Overcomes the Dominant Inhibitory Activity of Ha-Ras Asn-17

Schweighoffer, F., Cai, H., Chevallier‐Multon, M., Fath, I., Cooper, G. M., & Tocqué, B. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.1.39-43.1993 · Cited by 17

Kinetic analysis of the binding of guanine nucleotides to bovine brainrhoB p20, a ras p21-like GTP-binding protein

Kuroda, S., Kikuchi, A., & Takai, Y. (1989) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(89)92276-6 · Cited by 17

Scrape-loaded p21ras down-regulates agonist-stimulated inositol phosphate production by a mechanism involving protein kinase C

Price, B. D., Morris, J. D. H., Marshall, C., & Hall, A. (1989) · Biochemical Journal · doi:10.1042/bj2600157 · Cited by 17

Methylation of KRAS by SETD7 promotes KRAS degradation in non-small cell lung cancer

Chiang, C.-Y., Fan, S., Zheng, H., Guo, W., Zheng, Z., Sun, Y., Zhong, C., Zeng, J., Li, S., Zhang, M., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113003 · Cited by 16

An updated overview of K-RAS G12C inhibitors in advanced stage non-small cell lung cancer

Tenekeci, A. K., Unal, A. A., Ceylan, F., & Sendur, M. A. N. (2024) · Future Oncology · doi:10.1080/14796694.2024.2407280 · Cited by 16

A Gα-Stimulated RapGEF Is a Receptor-Proximal Regulator of Dictyostelium Chemotaxis

Liu, Y., Lacal, J., Veltman, D. M., Fusetti, F., Haastert, P. J. M. V., Firtel, R., & Kortholt, A. (2016) · Developmental Cell · doi:10.1016/j.devcel.2016.05.001 · Cited by 16

Water Distribution within Wild-Type NRas Protein and Q61 Mutants during Unrestrained QM/MM Dynamics

Tichauer, R. H., Favre, G., Cabantous, S., Landa, G., Hémeryck, A., & Brut, M. (2018) · Biophysical Journal · doi:10.1016/j.bpj.2018.07.042 · Cited by 16

Crystal structures of p120RasGAP N-terminal SH2 domain in its apo form and in complex with a p190RhoGAP phosphotyrosine peptide

Chehayeb, R. J., Stiegler, A. L., & Boggon, T. J. (2019) · PLoS ONE · doi:10.1371/journal.pone.0226113 · Cited by 15

The E5 gene product of rhesus papillomavirus is an activator of endogenous Ras and phosphatidylinositol-3′-kinase in NIH 3T3 cells

Ghai, J., Ostrow, R. S., Tolar, J., McGlennen, R. C., Lemke, T. D., Tobolt, D. K., Liu, Z., & Faras, A. J. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.23.12879 · Cited by 16

A Candida albicans homolog of CDC25 is functional in Saccharomyces cerevisiae

GOLDBERG, D., Marbach, I., Gross, E., Levitzki, A., & Simchen, G. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb17748.x · Cited by 16

Qβ-Phage Resistance by Deletion of the Coiled-coil Motif in Elongation Factor Ts

Karring, H., Mathu, S. G. J., DUIN, J. V., Clark, B. F. C., Kraal, B., & Knudsen, C. R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m306605200 · Cited by 16

Membrane‐anchoring domains of Cdc25p, a Saccharomyces cerevisiae ras exchange factor

Garreau, H., Geymonat, M., Renault, G., & Jacquet, M. (1996) · Biology of the Cell · doi:10.1016/0248-4900(96)84771-x · Cited by 16

Ras and Rho small G Proteins: Insights from the Schizophyllum commune genome sequence and comparisons to other fungi

Raudaskoski, M., Kothe, E., Fowler, T. J., Jung, E., & Horton, S. J. (2012) · Biotechnology and Genetic Engineering Reviews · doi:10.5661/bger-28-61 · Cited by 16

Molecular Dynamics of the H-rasGene-Encoded p21 Protein; Identification of Flexible Regions and Possible Effector Domains

Dykes, D. C., Friedman, F. K., Dykes, S. L., Murphy, R. B., Brandt‐Rauf, P. W., & Pincus, M. R. (1993) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.1993.10508009 · Cited by 16

Partial growth suppression of human prostate cancer cells by the Krev‐1 suppressor gene

Burney, T. L., Rockove, S., Eiseman, J. L., Jacobs, S. C., & Kyprianou, N. (1994) · The Prostate · doi:10.1002/pros.2990250403 · Cited by 16

Platelet-derived growth factor-induced p21ras-mediated signaling is independent of platelet-derived growth factor receptor interaction with GTPase-activating protein or phosphatidylinositol-3-kinase.

Burgering, B. M. T., Freed, E., van der Voorn, L., McCormick, F. P., & Bos, J. L. (1994) · PubMed · Cited by 16

Characterization of the Schizosaccharomyces pombe ral2 Gene Implicated in Activation of the ras1 Gene Product

Fukui, Y., Miyake, S., Satoh, M., & Yamamoto, M. P. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.12.5617-5622.1989 · Cited by 16

Co‐regulation of metastatic and transforming activity of normal and mutant ras genes

Egan, S. E., Broere, J. J., Jarolim, L., Wright, J. A., & Greenberg, A. H. (1989) · International Journal of Cancer · doi:10.1002/ijc.2910430317 · Cited by 16

Signaling Mismatch Repair: The Mechanics of an Adenosine-Nucleotide Molecular SwitchPreprint

Fishel, R. A., ACHARYA, S., Berardini, M. D., Bocker, T., Charbonneau, N., Cranston, A. N., Gradia, S., Guerrette, S., Heinen, C. D., MAZUREK, A., et al. (2000) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2000.65.217 · Cited by 16

R-Ras subfamily proteins elicit distinct physiologic effects and phosphoproteome alterations in neurofibromin-null MPNST cells

Weber, S. M., Brossier, N. M., Prechtl, A. M., Barnes, S., Wilson, L. S., Brosius, S. N., Longo, J. F., & Carroll, S. L. (2021) · Cell Communication and Signaling · doi:10.1186/s12964-021-00773-4 · Cited by 15

Tissue-specific functions of the Caenorhabditis elegans p120 Ras GTPase activating protein GAP-3

Steták, A., Gutierrez, P., & Hajnal, A. (2008) · Developmental Biology · doi:10.1016/j.ydbio.2008.08.026 · Cited by 15

N-terminal Sequences Contained in the Src Homology 2 and 3 Domains of p120 GTPase-activating Protein Are Required for Full Catalytic Activity Toward Ras

Bryant, S. S., Mitchell, A. L., Collins, F. S., Miao, W., Marshall, M. S., & Jove, R. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.9.5195 · Cited by 15

Formation of complexes involving RasGAP and p190 RhoGAP during morphogenetic events of the gastrulation in Xenopus

Dupont, H., & Blancq, M. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00689.x · Cited by 15

Site-directed mutagenesis of the GDP binding domain of bacterial elongation factor Tu

Hwang, Y., McCabe, P. G., Innis, M. A., & Miller, D. L. (1989) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(89)90452-9 · Cited by 15

Neurofibromatosis type 1 (NF1) gene: Implication in neuroectodermal differentiation and genesis of brain tumors

Nishi, T., & Saya, H. (1991) · Cancer and Metastasis Reviews · doi:10.1007/bf00554792 · Cited by 15

Hydrogen bond interactions of G proteins with the guanine ring moiety of guanine nucleotides

Weng, G., Chen, C. X., Balogh‐Nair, V., Callender, R. H., & Manor, D. (1994) · Protein Science · doi:10.1002/pro.5560030104 · Cited by 15

p120 GAP requirement in normal and malignant human hematopoiesis.

Skórski, T., Kanakaraj, P., Nieborowska-Skorska, M., Ratajczak, M. Z., Szczylik, C. A., Zon, G., Arlinghaus, R. B., Gewirtz, A. M., PERUSSIA, B., & Calabretta, B. (1993) · The Journal of Experimental Medicine · doi:10.1084/jem.178.6.1923 · Cited by 14

Saccharomyces cerevisiae cdc15 Mutants Arrested at a Late Stage in Anaphase Are Rescued by Xenopus cDNAs Encoding N -ras or a Protein with β-Transducin Repeats†

Spevak, W., Keiper, B. D., Stratowa, C., & Castañón, M. J. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.8.4953-4966.1993 · Cited by 15

Microinjection of a 19-kDa Guanine Nucleotide-binding Protein Inhibits Maturation of Xenopus Oocytes

Bahnson, T. D., Tsai, S. C., Adamik, R., Moss, J., & Vaughan, M. J. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63774-3 · Cited by 15

Cell Transformation by ras and Regulation of its Protein Product

Lowy, D. R., Johnson, M. R., DeClue, J. E., Cen, H., Zhang, K., Papageorge, A. G., Vass, W. C., Willumsen, B. M., Valentine, M. B., & Look, A. T. (2007) · Novartis Foundation symposium · doi:10.1002/9780470514450.ch5 · Cited by 15

Biochemical and Biological Properties of the Human N-ras p21 Protein

Trahey, M., Milley, R. J., Cole, G. E., Innis, M. A., Paterson, H., Marshall, C. J., Hall, A., & McCormick, F. P. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.1.541-544.1987 · Cited by 5

Molecular Biology of GAP and its Interaction with Oncogenic ras p21

Vogel, U. S., Diehl, R. E., Marshall, M. S., Schaber, M. D., Register, R. B., Hill, W. S., Ng, A. S., Scolnick, E. M., Dixon, R. A. F., Sigal, I. S., et al. (1989) · Springer eBooks · doi:10.1007/978-1-4757-1235-3_40

Kinetic and fluorescence studies of the interaction of p21(ras) with guanine nucleotides and the GTPase activating proteins, p120-GAP and Nfi-GAP

Moore, K. J. M. (1992) · UCL Discovery (University College London)

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

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