PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 14749369-0 2004 Activation of H-Ras in the endoplasmic reticulum by the RasGRF family guanine nucleotide exchange factors. Guanine Nucleotides 70-88 HRas proto-oncogene, GTPase Homo sapiens 14-19 14979728-2 2004 NO has been shown to promote guanine nucleotide exchange on the critical cellular signaling protein p21Ras (Ras) by S-nitrosylation of a redox-active thiol group (Cys(118)). Guanine Nucleotides 29-47 HRas proto-oncogene, GTPase Homo sapiens 100-106 9722985-5 1998 This mutation causes striking sequence similarity with the guanine nucleotide binding domain of c-H-ras. Guanine Nucleotides 59-77 HRas proto-oncogene, GTPase Homo sapiens 96-103 11948427-2 2002 We searched for novel guanine nucleotide exchange factors of HRas and isolated small G-protein dissociation stimulator (smgGDS), a guanine nucleotide exchange factor known to act on numerous Ras and Rho family GTPases. Guanine Nucleotides 22-40 HRas proto-oncogene, GTPase Homo sapiens 61-65 11075717-10 2000 Along this line, microinjection of anti-Shc antibody inhibited insulin-induced mitogenesis, and the guanine nucleotide exchange activity for p21ras is tightly associated with Shc, but not with IRS. Guanine Nucleotides 100-118 HRas proto-oncogene, GTPase Homo sapiens 141-147 10498616-7 1999 An S27N mutant of M-Ras, like the analogous H-Ras S17N mutant, was a dominant inhibitor of activation of the c-fos promoter by constitutively active Src Y527F, suggesting that M-Ras and p21 Ras shared guanine nucleotide exchange factors and are likely to be activated in parallel. Guanine Nucleotides 201-219 HRas proto-oncogene, GTPase Homo sapiens 186-193 10049745-1 1999 We demonstrate that stimulation of primary cultures of endothelial cells with vascular endothelial cell growth factor (VEGF) results in a rapid increase in labeled guanine nucleotide bound to p21ras. Guanine Nucleotides 164-182 HRas proto-oncogene, GTPase Homo sapiens 192-198 9434775-5 1997 Triggering of the T cell receptor (TCR) perturbs the guanine nucleotide binding cycle of p21ras and in turn induces phosphorylation and activation of mitogen-activated protein kinases (MAPK). Guanine Nucleotides 53-71 HRas proto-oncogene, GTPase Homo sapiens 89-95 7608150-1 1995 Activation of p21ras by receptor tyrosine kinases is thought to result from recruitment of guanine nucleotide exchange factors such as Son-of-sevenless (Sos) to plasma membrane receptor substrates via adaptor proteins such as Grb2. Guanine Nucleotides 91-109 HRas proto-oncogene, GTPase Homo sapiens 14-20 9115849-8 1996 This inhibition results in reduced guanine nucleotide exchange in p21ras. Guanine Nucleotides 35-53 HRas proto-oncogene, GTPase Homo sapiens 66-72 8636102-7 1996 As long as the cellular localizations of the different proteins and their biological functions are not clarified, these biochemical data seem to indicate that Ral-guanine nucleotide exchange factors is an effector molecule of Rap1A rather than of H-Ras. Guanine Nucleotides 163-181 HRas proto-oncogene, GTPase Homo sapiens 247-252 7487952-13 1995 The effects described appear to be unique for c-di-GMP and, taken together, raise the possibility that an irreversible binding of this guanine nucleotide to the growth-promoting p21ras protein results in a fixed active conformation of this protein affecting DNA synthesis. Guanine Nucleotides 135-153 HRas proto-oncogene, GTPase Homo sapiens 178-184 7673152-7 1995 Finally, using recombinant p21ras in vitro, we found that redox modulators directly promoted guanine nucleotide exchange on p21ras. Guanine Nucleotides 93-111 HRas proto-oncogene, GTPase Homo sapiens 27-33 8950985-4 1996 In addition, the sensitivity of H-Ras to GRF was abolished when residues 130-139 were replaced by proline-aspartic acid-glutamine, whereas substitution of the entire loop 8 (residues 123-130 replaced by leucine-isoleucine-arginine) had no effect on the stimulation of guanine nucleotide release by GRF. Guanine Nucleotides 268-286 HRas proto-oncogene, GTPase Homo sapiens 32-37 8524141-0 1995 Analysis of intrinsic and CDC25-stimulated guanine nucleotide exchange of p21ras-nucleotide complexes by fluorescence measurements. Guanine Nucleotides 43-61 HRas proto-oncogene, GTPase Homo sapiens 74-80 7706235-0 1995 Nitric oxide-stimulated guanine nucleotide exchange on p21ras. Guanine Nucleotides 24-42 HRas proto-oncogene, GTPase Homo sapiens 55-61 7706235-8 1995 These studies identify p21ras as a target of NO in T cells and suggest that NO activates p21ras by an action which mimics that of guanine nucleotide exchange factors. Guanine Nucleotides 130-148 HRas proto-oncogene, GTPase Homo sapiens 23-29 7718090-3 1995 Here, Manolo Izquierdo Pastor, Karin Reif and Doreen Cantrell review the numerous recent advances in understanding how the p21ras guanine nucleotide binding protein couples the TCR to the T-cell signalling cascade. Guanine Nucleotides 130-148 HRas proto-oncogene, GTPase Homo sapiens 123-129 7809086-0 1994 Identification of the guanine nucleotide dissociation stimulator for Ral as a putative effector molecule of R-ras, H-ras, K-ras, and Rap. Guanine Nucleotides 22-40 HRas proto-oncogene, GTPase Homo sapiens 115-120 7988425-2 1994 As both growth factors have been shown to stimulate guanine nucleotide exchange on p21Ras in permeabilized cells, we examined their effects on total cellular guanine nucleotide exchange factor (GEF) activity in a direct assay, using the rate of dissociation of [3H]GDP from p21Ras as a measure of GEF activity. Guanine Nucleotides 52-70 HRas proto-oncogene, GTPase Homo sapiens 83-89 7972015-2 1994 The H-Ras protein was found to interact with a guanine nucleotide dissociation stimulator (GDS) that has been previously shown to regulate guanine nucleotide exchange on another member of the Ras protein family, Ral. Guanine Nucleotides 47-65 HRas proto-oncogene, GTPase Homo sapiens 4-9 7972015-2 1994 The H-Ras protein was found to interact with a guanine nucleotide dissociation stimulator (GDS) that has been previously shown to regulate guanine nucleotide exchange on another member of the Ras protein family, Ral. Guanine Nucleotides 139-157 HRas proto-oncogene, GTPase Homo sapiens 4-9 8142894-1 1994 We have utilized Raman difference spectroscopy to investigate hydrogen bonding interactions of the guanine moiety in guanine nucleotides with the binding site of two G proteins, EF-Tu (elongation factor Tu from Escherichia coli) and the c-Harvey ras protein, p21 (the gene product of the human c-H-ras proto-oncogene). Guanine Nucleotides 117-136 HRas proto-oncogene, GTPase Homo sapiens 294-301 7917105-1 1994 The guanine nucleotide binding proteins p21ras are activated by the T-cell antigen receptor and play a critical role in transducing signals from the T-cell receptor to the cell nucleus. Guanine Nucleotides 4-22 HRas proto-oncogene, GTPase Homo sapiens 40-46 8196614-10 1994 We show that both H-rasAsn-17 and H-rasTyr-57, compared with wild-type H-ras, are defective in their guanine nucleotide-dependent release from human cdc25 and that this defect is more severe for the H-rasTyr-57 mutant. Guanine Nucleotides 101-119 HRas proto-oncogene, GTPase Homo sapiens 18-23 8260648-7 1993 The present review focuses on TCR and IL-2R regulation of two common intracellular signalling pathways: the regulation of a PtdIns-3-kinase and the activation of the guanine nucleotide binding proteins p21ras. Guanine Nucleotides 166-184 HRas proto-oncogene, GTPase Homo sapiens 202-208 8361768-7 1993 The mutations at A66 show for the first time that helix alpha 2 of p21ras is involved in the stimulation of guanine nucleotide exchange by exchange factors. Guanine Nucleotides 108-126 HRas proto-oncogene, GTPase Homo sapiens 67-73 8386636-1 1993 Proton-NMR signals in the downfield region (below approximately 10 ppm) have been shown to provide a useful spectroscopic window to monitor the binding of guanine nucleotides to the active site of GTP/GDP-binding proteins via H-bonds, as specified here by the 21-kDa product of the c-H-ras gene (p21). Guanine Nucleotides 155-174 HRas proto-oncogene, GTPase Homo sapiens 282-289 8496156-7 1993 This utilizes the increase of fluorescence anisotropy upon binding of GAP to p21ras complexed with 2"(3")-O-(N-methylanthraniloyl) (mant) derivatives of guanine nucleotides. Guanine Nucleotides 153-172 HRas proto-oncogene, GTPase Homo sapiens 77-83 2038322-5 1991 Biochemical analysis of the proteins encoded by v-rasH(S39C) and c-rasH(S39C) demonstrated that the encoded p21ras proteins were stable and bound guanine nucleotides in vivo at permissive and nonpermissive temperatures. Guanine Nucleotides 146-165 HRas proto-oncogene, GTPase Homo sapiens 108-114 8299426-2 1993 The structure of the guanine nucleotide-binding domain of H-Ras (or p21H-ras) in the triphosphate conformation was determined at very high resolution (1.4 A). Guanine Nucleotides 21-39 HRas proto-oncogene, GTPase Homo sapiens 58-63 8417322-0 1993 Ras activation by insulin and epidermal growth factor through enhanced exchange of guanine nucleotides on p21ras. Guanine Nucleotides 83-102 HRas proto-oncogene, GTPase Homo sapiens 106-112 8417322-2 1993 This accumulation could be caused either by an increase in guanine nucleotide exchange on p21ras or by a decrease in the GTPase activity of p21ras. Guanine Nucleotides 59-77 HRas proto-oncogene, GTPase Homo sapiens 90-96 1532814-2 1992 Here we show that the guanine nucleotide-binding proteins p21ras may be involved in IL-2 signal transduction pathways. Guanine Nucleotides 22-40 HRas proto-oncogene, GTPase Homo sapiens 58-64 1395932-2 1992 In T cells recent studies have indicated that activation of the guanine nucleotide-binding proteins p21ras is mediated by PKC, which suggests that the p21ras proteins may regulate intracellular signalling events downstream of PKC. Guanine Nucleotides 64-82 HRas proto-oncogene, GTPase Homo sapiens 100-106 1395932-2 1992 In T cells recent studies have indicated that activation of the guanine nucleotide-binding proteins p21ras is mediated by PKC, which suggests that the p21ras proteins may regulate intracellular signalling events downstream of PKC. Guanine Nucleotides 64-82 HRas proto-oncogene, GTPase Homo sapiens 151-157 1741165-7 1992 In vivo guanine nucleotide binding to p21ras in the revertant cell lines demonstrated binding of both GTP and GDP, indicating that reversion to the non-transformed phenotype was not due to inability of p21ras to bind GTP. Guanine Nucleotides 8-26 HRas proto-oncogene, GTPase Homo sapiens 38-44 1785141-4 1991 The p21ras structure is similar to that of the G-domain of elongation factor Tu (EF-Tu) from Escherichia coli, suggesting that p21ras can serve as a good model for other guanine nucleotide binding proteins. Guanine Nucleotides 170-188 HRas proto-oncogene, GTPase Homo sapiens 4-10 1785141-4 1991 The p21ras structure is similar to that of the G-domain of elongation factor Tu (EF-Tu) from Escherichia coli, suggesting that p21ras can serve as a good model for other guanine nucleotide binding proteins. Guanine Nucleotides 170-188 HRas proto-oncogene, GTPase Homo sapiens 127-133 1674518-0 1991 CD2 antigen mediated activation of the guanine nucleotide binding proteins p21ras in human T lymphocytes. Guanine Nucleotides 39-57 HRas proto-oncogene, GTPase Homo sapiens 75-81 1674518-1 1991 T cell stimulation via the TCR complex (TCR/CD3 complex) results in activation of the guanine nucleotide binding proteins encoded by the ras protooncogenes (p21ras). Guanine Nucleotides 86-104 HRas proto-oncogene, GTPase Homo sapiens 157-163 1903516-1 1991 More than thirty small guanine nucleotide-binding proteins related to the ras-encoded oncoprotein, termed Ras or p21ras, are known. Guanine Nucleotides 23-41 HRas proto-oncogene, GTPase Homo sapiens 113-119 1633420-2 1992 Regulation of p21ras is achieved by GTPase activating proteins, which control the rate of hydrolysis of GTP to GDP, and also by GDP dissociation stimulators, which catalyze the exchange of guanine nucleotides. Guanine Nucleotides 189-208 HRas proto-oncogene, GTPase Homo sapiens 14-20 2120590-1 1990 Cellular ras genes encode a family of membrane-associated proteins (p21ras) that bind guanine nucleotide and possess a low intrinsic GTPase activity. Guanine Nucleotides 86-104 HRas proto-oncogene, GTPase Homo sapiens 68-74 2121270-4 1990 High-affinity guanine nucleotide binding is associated with a polypeptide migrating identically with H-ras on SDS-PAGE. Guanine Nucleotides 14-32 HRas proto-oncogene, GTPase Homo sapiens 101-106 2199064-1 1990 The X-ray structures of the guanine nucleotide binding domains (amino acids 1-166) of five mutants of the H-ras oncogene product p21 were determined. Guanine Nucleotides 28-46 HRas proto-oncogene, GTPase Homo sapiens 106-111 2116014-2 1990 A protein that stimulates the rate of exchange of guanine nucleotide on p21ras has been identified and characterized in cytoplasmic extracts of human placenta. Guanine Nucleotides 50-68 HRas proto-oncogene, GTPase Homo sapiens 72-78 2491843-1 1989 The protein products of the mammalian ras genes, p21ras, are regulatory guanine nucleotide binding proteins that are involved in the control of cell proliferation, though the exact biochemical processes regulated are unknown. Guanine Nucleotides 72-90 HRas proto-oncogene, GTPase Homo sapiens 49-55 35324017-0 2022 Conformations and binding pockets of HRas and its guanine nucleotide exchange factors complexes in the guanosine triphosphate exchange process. Guanine Nucleotides 50-68 HRas proto-oncogene, GTPase Homo sapiens 37-41 2494654-1 1989 A structural model of guanine nucleotide-binding regulatory protein alpha subunits (G alpha subunits) is proposed based on the crystal structure of the catalytic domain of the human HRAS protein (p21ras). Guanine Nucleotides 22-40 HRas proto-oncogene, GTPase Homo sapiens 182-186 2494654-1 1989 A structural model of guanine nucleotide-binding regulatory protein alpha subunits (G alpha subunits) is proposed based on the crystal structure of the catalytic domain of the human HRAS protein (p21ras). Guanine Nucleotides 22-40 HRas proto-oncogene, GTPase Homo sapiens 196-202 3487832-1 1986 Single amino acid changes were introduced into normal (non-oncogenic) and activated forms of the human H-ras protein at a position (residue 116) proposed on structural grounds to represent a contact site with guanine nucleotides. Guanine Nucleotides 209-228 HRas proto-oncogene, GTPase Homo sapiens 103-108 28139825-7 2017 Functional studies revealed that amino acid change p.Gly60Val impairs HRAS binding to effectors PIK3CA, phospholipase C1, and RAL guanine nucleotide dissociation stimulator. Guanine Nucleotides 130-148 HRas proto-oncogene, GTPase Homo sapiens 70-74 3915772-0 1985 Antibody of predetermined specificity to a carboxy-terminal region of H-ras gene products inhibits their guanine nucleotide-binding function. Guanine Nucleotides 105-123 HRas proto-oncogene, GTPase Homo sapiens 70-75 3891097-1 1985 In these experiments we demonstrate that purified RAS proteins, whether derived from the yeast RAS1 or RAS2 or the human H-ras genes, activate yeast adenylate cyclase in the presence of guanine nucleotides. Guanine Nucleotides 186-205 HRas proto-oncogene, GTPase Homo sapiens 121-126 25946318-3 2015 Here we show that H-Ras, N-Ras, and K-Ras are coexpressed with their activators (guanine nucleotide exchange factors) in neurofibromin-null malignant peripheral nerve sheath tumor (MPNST) cells, and that all 3 Ras proteins are activated. Guanine Nucleotides 81-99 HRas proto-oncogene, GTPase Homo sapiens 18-23 20018863-7 2010 Guanine nucleotide exchange factor-catalyzed nucleotide exchange for both H-Ras and RhoA was inhibited by mant-substituted nucleotides, and the degree of inhibition depends highly on the GTPase and whether the assay measures association of mantGTP with, or dissociation of mantGDP from the GTPase. Guanine Nucleotides 0-18 HRas proto-oncogene, GTPase Homo sapiens 74-79 23335589-7 2013 Indeed, we identified strongly augmented active HRAS(E63_D69dup) that co-precipitated with effectors RAF1, RAL guanine nucleotide dissociation stimulator and phospholipase C1. Guanine Nucleotides 111-129 HRas proto-oncogene, GTPase Homo sapiens 48-52 18790720-4 2008 The results from limited proteinase degradation show that Ca(2+) protects the fragments of H-Ras from being further degraded by trypsin and by proteinase K. HPLC studies together with fluorescence spectroscopic measurements indicate that binding of Ca(2+) to the H-Ras.GDP.Mg(2+) complex remarkably promotes guanine nucleotide exchange on H-Ras under emulated physiological Ca(2+) concentration conditions. Guanine Nucleotides 308-326 HRas proto-oncogene, GTPase Homo sapiens 91-96 18790720-5 2008 Addition of high concentrations of either of two macromolecular crowding agents, Ficoll 70 and dextran 70, dramatically enhances H-Ras guanine nucleotide exchange extent in the presence of Ca(2+) at emulated physiological concentrations, and the nucleotide exchange extent increases significantly with the concentrations of crowding agents. Guanine Nucleotides 135-153 HRas proto-oncogene, GTPase Homo sapiens 129-134 18790720-6 2008 Together, these results indicate that binding of calcium ions to H-Ras remarkably promotes H-Ras guanine nucleotide exchange under emulated physiological conditions. Guanine Nucleotides 97-115 HRas proto-oncogene, GTPase Homo sapiens 65-70 18790720-6 2008 Together, these results indicate that binding of calcium ions to H-Ras remarkably promotes H-Ras guanine nucleotide exchange under emulated physiological conditions. Guanine Nucleotides 97-115 HRas proto-oncogene, GTPase Homo sapiens 91-96 16415107-6 2006 S-glutathiolation also promoted guanine nucleotide exchange of recombinant p21ras. Guanine Nucleotides 32-50 HRas proto-oncogene, GTPase Homo sapiens 75-81 16841939-1 2006 P21ras, the translation product of the most commonly mutated oncogene, is a small guanine nucleotide exchange protein. Guanine Nucleotides 82-100 HRas proto-oncogene, GTPase Homo sapiens 0-6