PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 1429539-2 1992 The model is based on analogies to the known structures of the MgATP site on adenylate kinase and the guanine nucleotide sites on elongation factor Tu (Ef-Tu) and the ras p21 protein. Guanine Nucleotides 102-120 H3 histone pseudogene 16 Homo sapiens 171-174 1932015-0 1991 An isotope edited classical Raman difference spectroscopic study of the interactions of guanine nucleotides with elongation factor Tu and H-ras p21. Guanine Nucleotides 88-107 H3 histone pseudogene 16 Homo sapiens 144-147 1351293-1 1992 Current knowledge of the structure of H-ras p21 is reviewed with particular emphasis on the interaction between guanine nucleotides and the active site of the protein. Guanine Nucleotides 112-131 H3 histone pseudogene 16 Homo sapiens 44-47 1351296-1 1992 Guanine nucleotides modified by acetylation of the ribose moiety with the small fluorophore N-methylanthranilic acid(mant) have been shown to bind to p21 ras with similar equilibrium and kinetic rate constants as the parent nucleotides. Guanine Nucleotides 0-19 H3 histone pseudogene 16 Homo sapiens 150-153 1533366-6 1992 The results of this analysis have indicated two distinct interactive regions in p21, one associated with the guanine-nucleotide-binding site, whilst the second is proposed to be associated with a binding site for an activator protein. Guanine Nucleotides 109-127 H3 histone pseudogene 16 Homo sapiens 80-83 1533366-7 1992 These studies indicate that the p21 protein, besides the ability to function as a plasma-membrane-associated guanine-nucleotide-binding regulatory protein and bind free guanine nucleotides in the cytoplasm, has the structural ability to bind guanine incorporated in DNA. Guanine Nucleotides 169-188 H3 histone pseudogene 16 Homo sapiens 32-35 1740128-2 1992 The influence of the ionic environment on the intrinsic GTPase activity and the guanine-nucleotide interaction of Ha-ras protein p21 were studied in various experimental conditions and compared with the behaviour of elongation factor (EF) Tu. Guanine Nucleotides 80-98 H3 histone pseudogene 16 Homo sapiens 129-132 1932015-1 1991 We have measured the Raman spectrum of GDP bound to the elongation factor protein, EF-Tu, and the c-Harvey-ras protein, p21, two proteins of the guanine nucleotide binding family. Guanine Nucleotides 145-163 H3 histone pseudogene 16 Homo sapiens 120-123 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 H3 histone pseudogene 16 Homo sapiens 129-132 2180382-1 1990 The ras oncogene product, ras p21, is structurally homologous to guanine nucleotide-binding proteins, which play an important role in transmembrane signaling systems. Guanine Nucleotides 65-83 H3 histone pseudogene 16 Homo sapiens 30-33 2476675-0 1989 Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation. Guanine Nucleotides 17-35 H3 histone pseudogene 16 Homo sapiens 82-85 2476675-1 1989 The crystal structure of the guanine-nucleotide-binding domain of p21 (amino acids 1-166) complexed to the guanosine triphosphate analogue guanosine-5"-(beta, gamma-imido)triphosphate (GppNp) has been determined at a resolution of 2.6 A. Guanine Nucleotides 29-47 H3 histone pseudogene 16 Homo sapiens 66-69 2668035-0 1989 Conformational changes occurring in N-ras p21 in response to binding of guanine nucleotide and metal ions probed by proteolysis performed under controlled conditions. Guanine Nucleotides 72-90 H3 histone pseudogene 16 Homo sapiens 42-45 2668035-4 1989 Some capacity to bind guanine nucleotide is also retained by p21 treated with 7 M urea, as evidenced by increased resistance to proteolytic degradation, but the ability to bind divalent cations is irreversibly lost following denaturation. Guanine Nucleotides 22-40 H3 histone pseudogene 16 Homo sapiens 61-64 2439901-0 1987 Neutralizing monoclonal antibody against ras oncogene product p21 which impairs guanine nucleotide exchange. Guanine Nucleotides 80-98 H3 histone pseudogene 16 Homo sapiens 62-65 3140742-1 1988 The ras oncogene product ras p21 is structurally homologous to guanine nucleotide-binding proteins and plays an important role in transducing signals elicited by membrane receptors into intracellular metabolism. Guanine Nucleotides 63-81 H3 histone pseudogene 16 Homo sapiens 29-32 3328019-3 1987 Furthermore, it has been shown that residues 16, 116 and 119 in p21 played critical roles in the guanine nucleotide binding and, consequently, the ability of the protein to induce changes characteristic of cellular transformation. Guanine Nucleotides 97-115 H3 histone pseudogene 16 Homo sapiens 64-67 3554231-2 1987 The G domain, whose primary structure shares homology with the eukaryotic protein p21, is capable of supporting the basic activities of the intact molecule (guanine nucleotide binding in 1:1 molar ratio and GTPase activity). Guanine Nucleotides 157-175 H3 histone pseudogene 16 Homo sapiens 82-85 3540608-0 1986 Activation of ras p21 transforming properties associated with an increase in the release rate of bound guanine nucleotide. Guanine Nucleotides 103-121 H3 histone pseudogene 16 Homo sapiens 18-21 3898366-7 1985 The model makes it possible to visualize how oncogenic mutations of p21 affect interaction with guanine nucleotides. Guanine Nucleotides 96-115 H3 histone pseudogene 16 Homo sapiens 68-71 3333361-3 1986 The ras gene family encodes a group of closely related 21,000 dalton (p21) proteins with special affinity for guanine nucleotides. Guanine Nucleotides 110-129 H3 histone pseudogene 16 Homo sapiens 70-73 3012529-1 1986 Recent studies have shown that the 21-kilodalton protein (p21) Ha-ras gene product shares sequence homology with and may exhibit biochemical properties similar to the mammalian guanine nucleotide-binding proteins. Guanine Nucleotides 177-195 H3 histone pseudogene 16 Homo sapiens 58-61 3012529-8 1986 These data support the hypothesis that both the normal and mutated Ha-ras p21s are related to guanine nucleotide-binding proteins. Guanine Nucleotides 94-112 H3 histone pseudogene 16 Homo sapiens 74-77 3537694-2 1986 The ability of the encoded p21"s to autophosphorylate, bind guanine nucleotides, and hydrolyze GTP was assessed. Guanine Nucleotides 60-79 H3 histone pseudogene 16 Homo sapiens 27-30 3321304-4 1986 Its binding to p21 is completely blocked by guanine nucleotides, even though the region of p21 to which it binds does not seem to be part of the guanine nucleotide-binding site. Guanine Nucleotides 44-63 H3 histone pseudogene 16 Homo sapiens 15-18 3321304-4 1986 Its binding to p21 is completely blocked by guanine nucleotides, even though the region of p21 to which it binds does not seem to be part of the guanine nucleotide-binding site. Guanine Nucleotides 44-63 H3 histone pseudogene 16 Homo sapiens 91-94 3321304-4 1986 Its binding to p21 is completely blocked by guanine nucleotides, even though the region of p21 to which it binds does not seem to be part of the guanine nucleotide-binding site. Guanine Nucleotides 44-62 H3 histone pseudogene 16 Homo sapiens 15-18 3321304-4 1986 Its binding to p21 is completely blocked by guanine nucleotides, even though the region of p21 to which it binds does not seem to be part of the guanine nucleotide-binding site. Guanine Nucleotides 44-62 H3 histone pseudogene 16 Homo sapiens 91-94 3321304-6 1986 Another interesting region of p21 includes amino acids 116 and 119, which seem to confer, in part, the specificity of p21 for guanine nucleotides. Guanine Nucleotides 126-145 H3 histone pseudogene 16 Homo sapiens 30-33 3321304-6 1986 Another interesting region of p21 includes amino acids 116 and 119, which seem to confer, in part, the specificity of p21 for guanine nucleotides. Guanine Nucleotides 126-145 H3 histone pseudogene 16 Homo sapiens 118-121 3321304-8 1986 We were able to refine our model for guanine nucleotide interaction with p21 and to create mutant proteins with altered specificity for purine nucleotides. Guanine Nucleotides 37-55 H3 histone pseudogene 16 Homo sapiens 73-76 3915772-4 1985 This antibody was also shown to strikingly and specifically inhibit the guanine nucleotide-binding function of the p21 protein. Guanine Nucleotides 72-90 H3 histone pseudogene 16 Homo sapiens 115-118 3915772-5 1985 The inability of p21 protein to bind guanine nucleotides was associated with a lack of autophosphorylation or GTPase activities. Guanine Nucleotides 37-56 H3 histone pseudogene 16 Homo sapiens 17-20 3915772-6 1985 These studies suggest that a region toward its carboxy terminus is directly or indirectly involved in the guanine nucleotide-binding function of the p21 molecule. Guanine Nucleotides 106-124 H3 histone pseudogene 16 Homo sapiens 149-152 16323045-1 2005 We have previously computed the structures of three loops, residues 591-596, 654-675 and 742-751, in the ras-p21 protein-binding domain (residues 568-1044) of the guanine nucleotide-exchange-promoting SOS protein that were crystallographically undefined when one molecule of ras-p21 (unbound to nucleotide) binds to SOS. Guanine Nucleotides 163-181 H3 histone pseudogene 16 Homo sapiens 109-112 6392849-11 1984 Finally, we used anti-p21 monoclonal antibodies to detect a guanine nucleotide binding activity in yeast lysates. Guanine Nucleotides 60-78 H3 histone pseudogene 16 Homo sapiens 22-25 6147754-2 1984 In addition to the guanine nucleotide binding activity, normal p21 displays a GTPase activity which is selectively impaired by a mutation which activates its oncogenic potential. Guanine Nucleotides 19-37 H3 histone pseudogene 16 Homo sapiens 63-66 6610834-7 1984 We report here the evidence that epidermal growth factor enhances the guanine nucleotide binding activity of activated c-Ha-ras or v-Ha-ras p21, and phosphorylation of v-Ha-ras p21, suggesting that some mitogenic growth factors may regulate those activities. Guanine Nucleotides 70-88 H3 histone pseudogene 16 Homo sapiens 140-143 16323045-1 2005 We have previously computed the structures of three loops, residues 591-596, 654-675 and 742-751, in the ras-p21 protein-binding domain (residues 568-1044) of the guanine nucleotide-exchange-promoting SOS protein that were crystallographically undefined when one molecule of ras-p21 (unbound to nucleotide) binds to SOS. Guanine Nucleotides 163-181 H3 histone pseudogene 16 Homo sapiens 279-282 10839623-2 1999 The X-ray crystal structure of the ras oncogene-encoded p21 protein bound to SOS, the guanine nucleotide exchange-promoting protein, has been determined. Guanine Nucleotides 86-104 H3 histone pseudogene 16 Homo sapiens 56-59 16283548-1 2005 In previous studies, involving molecular modeling of wild-type and oncogenic forms of the ras-p21 protein bound to GTPase activating protein GAP and the ras-specific guanine nucleotide exchange-promoting protein, SOS, we identified specific domains of GAP and SOS proteins that differ in conformation when the computed average structures of the corresponding wild-type and oncogenic complexes are superimposed. Guanine Nucleotides 166-184 H3 histone pseudogene 16 Homo sapiens 94-97 15200053-1 2004 ras-p21 protein binds to the son-of-sevenless (SOS) guanine nucleotide-exchange promoter that allows it to exchange GDP for GTP. Guanine Nucleotides 52-70 H3 histone pseudogene 16 Homo sapiens 4-7 15200054-1 2004 In the accompanying paper, we found, using molecular dynamics calculations, four domains of the ras-specific SOS guanine nucleotide exchange protein (residues 589-601, 654-675, 746-761, and 980-989) that differ markedly in conformation when SOS is complexed with either oncogenic (Val 12-) ras-p21 or wild-type ras-p21. Guanine Nucleotides 113-131 H3 histone pseudogene 16 Homo sapiens 294-297 15200054-1 2004 In the accompanying paper, we found, using molecular dynamics calculations, four domains of the ras-specific SOS guanine nucleotide exchange protein (residues 589-601, 654-675, 746-761, and 980-989) that differ markedly in conformation when SOS is complexed with either oncogenic (Val 12-) ras-p21 or wild-type ras-p21. Guanine Nucleotides 113-131 H3 histone pseudogene 16 Homo sapiens 315-318 12740440-0 2003 Structural and biochemical studies of p21Ras S-nitrosylation and nitric oxide-mediated guanine nucleotide exchange. Guanine Nucleotides 87-105 H3 histone pseudogene 16 Homo sapiens 38-41 10661494-9 2000 Pearce, R. Levi, A. Novogrodsky, Nitric oxide-stimulated guanine nucleotide exchange on p21 ras, J. Biol. Guanine Nucleotides 57-75 H3 histone pseudogene 16 Homo sapiens 88-91 9020151-5 1997 NO-related species stimulated guanine nucleotide exchange on wild-type p21(ras), resulting in an active form, but not on p21(ras)C118S. Guanine Nucleotides 30-48 H3 histone pseudogene 16 Homo sapiens 71-74 10087060-6 1999 Estrogen produces a rapid, transient activation of src-family tyrosine kinases and tyrosine phosphorylation of p21(ras)-guanine nucleotide activating protein. Guanine Nucleotides 120-138 H3 histone pseudogene 16 Homo sapiens 111-114 9236898-2 1997 The ras family of genes consists of three functional genes which encode highly similar, guanine nucleotide-binding, proteins (p21) of 21kDa, with GTPase activity. Guanine Nucleotides 88-106 H3 histone pseudogene 16 Homo sapiens 126-129 9020151-7 1997 These data indicate that Cys118 is a critical site of redox regulation of p21(ras), and S-nitrosylation of this residue triggers guanine nucleotide exchange and downstream signaling. Guanine Nucleotides 129-147 H3 histone pseudogene 16 Homo sapiens 74-77 8887687-3 1996 p21(ras), a guanine nucleotide binding factor, mediates T-cell signal transduction through PKC-dependent and PKC-independent pathways. Guanine Nucleotides 12-30 H3 histone pseudogene 16 Homo sapiens 0-3 8663295-1 1996 Desensitization of p21(ras) after stimulation of cells by growth factors and phorbol 12-myristate 13-acetate (PMA) correlates with hyperphosphorylation of the guanine nucleotide exchange factor Son-of-sevenless (Sos) and its dissociation from the adaptor protein Grb2 (Cherniack, A., Klarlund, J. K., Conway, B. R., and Czech, M. P. (1995) J. Biol. Guanine Nucleotides 159-177 H3 histone pseudogene 16 Homo sapiens 19-22 8631299-5 1996 The p21 ras activation by Ang II is mediated by an increase in the guanine nucleotide exchange activity, but not by an inhibition of the GTPase-activating protein. Guanine Nucleotides 67-85 H3 histone pseudogene 16 Homo sapiens 4-7 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 H3 histone pseudogene 16 Homo sapiens 27-30 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 H3 histone pseudogene 16 Homo sapiens 23-26 15299413-1 1994 p21 is a small guanine nucleotide binding protein that is involved in intracellular signal transduction. Guanine Nucleotides 15-33 H3 histone pseudogene 16 Homo sapiens 0-3 8114695-7 1994 Furthermore, Shc immune complexes contained guanine nucleotide exchange activity toward p21ras in vitro. Guanine Nucleotides 44-62 H3 histone pseudogene 16 Homo sapiens 88-91 8810926-1 1996 As a molecular switch, the ras protein p21 undergoes structural changes that couple recognition sites on the protein surface to the guanine nucleotide-divalent metal ion binding site. Guanine Nucleotides 132-150 H3 histone pseudogene 16 Homo sapiens 39-42 8810926-4 1996 We report high frequency (139.5 GHz) EPR spectroscopy of p21.Mn(II) complexes of two guanine nucleotides that probes the link between threonine-35 and the divalent metal ion. Guanine Nucleotides 85-104 H3 histone pseudogene 16 Homo sapiens 57-60 7853016-2 1994 Like other guanine nucleotide-binding proteins p21ras is active when GTP bound and inactive when GDP bound. Guanine Nucleotides 11-29 H3 histone pseudogene 16 Homo sapiens 47-50 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 H3 histone pseudogene 16 Homo sapiens 259-262 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 H3 histone pseudogene 16 Homo sapiens 296-299 8419371-5 1993 All three mutations influence the dissociation constants and the association and dissociation rate constants of the interaction between guanine nucleotides and p21, but to a different degree. Guanine Nucleotides 136-155 H3 histone pseudogene 16 Homo sapiens 160-163 8419371-7 1993 31P NMR spectra of the GDP and Gpp(NH)p (guanosine-5"-(beta,gamma-imido)triphosphate) complexes of mutated p21 show a remarkable perturbation of the guanine nucleotide-binding site compared to wild-type protein. Guanine Nucleotides 149-167 H3 histone pseudogene 16 Homo sapiens 107-110