PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 11336789-6 2001 The relative amount of Ras2-GTP changes in a parallel way suggesting that there is a correlation with the cytosolic GTP/GDP ratio. Guanosine Diphosphate 120-123 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 23-27 11336789-7 2001 In addition "in vitro" mixed-nucleotide exchange experiments done on purified Ras2 protein demonstrated that the GTP and GDP concentrations influence the extent of Ras2-GTP loading giving further support to their possible regulatory role. Guanosine Diphosphate 121-124 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 78-82 11336789-7 2001 In addition "in vitro" mixed-nucleotide exchange experiments done on purified Ras2 protein demonstrated that the GTP and GDP concentrations influence the extent of Ras2-GTP loading giving further support to their possible regulatory role. Guanosine Diphosphate 121-124 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 164-168 8663268-1 1996 The interaction of Saccharomyces cerevisiae Ras2p with the catalytic domain of the GDP/GTP exchange factors (GEFs) mouse CDC25(Mm), yeast Cdc25p, and Sdc25p was analyzed by introducing the substitution R80D/N81D into Ras2p S24N, a mutant that is shown to interfere with the Ras2p wild type (wt)-GEF interaction by forming a stable complex. Guanosine Diphosphate 83-86 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 44-49 10747953-6 2000 These results indicate that in membrane-bound full-length GEF the N-terminal moiety regulates the interaction between catalytic domain and farnesylated Ras2p.GDP. Guanosine Diphosphate 158-161 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 152-157 9628870-4 1998 Deletion of the GTPase-activating proteins Ira1 and Ira2, or expression of the RAS2(val19) allele, causes an enhanced GTP/GDP basal ratio and abolishes the intracellular acidification-induced increase. Guanosine Diphosphate 122-125 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 79-83 8663268-4 1996 The affinity of Ras2p S24N/R80D/N81D for GDP and GTP was decreased 3 and 4 orders of magnitude, respectively, like that of Ras2p S24N, whereas the double mutant behaved as Ras2p wt. Guanosine Diphosphate 41-44 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 16-21 8663268-6 1996 Thus, the triple mutant and Ras2p S24N have opposite properties toward the binding to GEF but similarly modified behaviors toward GDP, GTP, and adenylyl cyclase. Guanosine Diphosphate 130-133 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 28-33 7818528-6 1995 Highly purified CDC25Mm 1005-1260, expressed in E. coli using the pMAL system, enhanced the GDP release from both H-ras p21 and S. cerevisiae Ras2p and its activity was nearly as high as that of CDC25Mm 974-1260. Guanosine Diphosphate 92-95 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 142-147 7577970-7 1995 The simultaneous presence of the catalytic domains of Ira2p and the yeast GDP/GTP exchange factor Cdc25p induced on Ras2p a multiple-round reaction of GTP hydrolysis and GDP/GTP exchange, showing that it is possible to reconstitute in vitro a S. cerevisiae system suitable for the study of the regulation of the Ras2p GDP/GTP cycle. Guanosine Diphosphate 74-77 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 116-121 7577970-7 1995 The simultaneous presence of the catalytic domains of Ira2p and the yeast GDP/GTP exchange factor Cdc25p induced on Ras2p a multiple-round reaction of GTP hydrolysis and GDP/GTP exchange, showing that it is possible to reconstitute in vitro a S. cerevisiae system suitable for the study of the regulation of the Ras2p GDP/GTP cycle. Guanosine Diphosphate 74-77 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 312-317 7577970-7 1995 The simultaneous presence of the catalytic domains of Ira2p and the yeast GDP/GTP exchange factor Cdc25p induced on Ras2p a multiple-round reaction of GTP hydrolysis and GDP/GTP exchange, showing that it is possible to reconstitute in vitro a S. cerevisiae system suitable for the study of the regulation of the Ras2p GDP/GTP cycle. Guanosine Diphosphate 170-173 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 116-121 7577970-7 1995 The simultaneous presence of the catalytic domains of Ira2p and the yeast GDP/GTP exchange factor Cdc25p induced on Ras2p a multiple-round reaction of GTP hydrolysis and GDP/GTP exchange, showing that it is possible to reconstitute in vitro a S. cerevisiae system suitable for the study of the regulation of the Ras2p GDP/GTP cycle. Guanosine Diphosphate 170-173 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 312-317 7851434-3 1995 The highly purified (greater than 95%) stable fusion protein, obtained by affinity chromatography, was very active in enhancing the dissociation rate or the GDP/GTP exchange of the GDP complex of Ras2p or human H-ras p21. Guanosine Diphosphate 157-160 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 196-201 7851434-3 1995 The highly purified (greater than 95%) stable fusion protein, obtained by affinity chromatography, was very active in enhancing the dissociation rate or the GDP/GTP exchange of the GDP complex of Ras2p or human H-ras p21. Guanosine Diphosphate 181-184 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 196-201 7851434-5 1995 The stimulation of the guanine nucleotide release by Sdc25p-C was stronger for Ras2p.GDP than Ras2p.GTP, an effect that was less pronounced in the case of the p21 complexes. Guanosine Diphosphate 85-88 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 79-84 7851434-6 1995 The association rate of the Ras2p.GDP (GTP) complex was also enhanced by Sdc25p-C. Monovalent and divalent salts inhibit the nucleotide-releasing activity of Sdc25p-C. Guanosine Diphosphate 34-37 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 28-33 7851434-10 1995 On gel filtration, truncated Sdc25p-C and nucleotide-free Ras2p (or p21) formed a stable 1:1 stoichiometric complex that was dissociated by increasing concentrations of GDP. Guanosine Diphosphate 169-172 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 58-63 7851434-12 1995 The complex with [S24N]Ras2p was greater than 100-fold less sensitive to the dissociating effect of GDP, whereas [R80D, N81D]Ras2p was unable to form a stable complex with truncated Sdc25p-C. Guanosine Diphosphate 100-103 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 23-28 1901951-8 1991 smg p21 GDS has low amino acid sequence homology with the yeast CDC25 and SCD25 proteins, which may regulate the GDP/GTP exchange reaction of the yeast RAS2 protein, but not with ras p21 GTPase-activating protein, the inhibitory GDP/GTP exchange proteins (GDP dissociation inhibitor) for smg p25A and rho p21s, and the beta gamma subunits of heterotrimeric GTP-binding proteins such as Gs and Gi. Guanosine Diphosphate 113-116 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 152-156 8206969-4 1994 Using Ras2p and a catalytic fragment of Cdc25p, both expressed in and purified from Escherichia coli, we determined that Cdc25p has a Km for Ras2p-GDP of 160 nM and a maximal rate of 0.20 s-1. Guanosine Diphosphate 147-150 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 141-146 8206969-5 1994 The Km of Cdc25p for Ras2p complexed to GTP is 3-fold greater than that for Ras2p complexed to GDP. Guanosine Diphosphate 95-98 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 21-26 8206969-5 1994 The Km of Cdc25p for Ras2p complexed to GTP is 3-fold greater than that for Ras2p complexed to GDP. Guanosine Diphosphate 95-98 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 76-81 8106517-3 1994 Characterization of their intrinsic GTPase and GDP dissociation as well as their ability to stimulate adenylate cyclase showed that these activities of RAS2-E99K mutant protein were similar to those of the wild type protein. Guanosine Diphosphate 47-50 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 152-156 8106517-4 1994 RAS2-E130K protein, on the other hand, differed from the wild type protein with a fast GDP dissociation rate and 2-fold higher activation of adenylate cyclase. Guanosine Diphosphate 87-90 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 0-4 8441380-5 1993 The CDC25 fusion protein catalyzed replacement of GDP-bound to Ras2 with GTP (activation) more efficiently than that of the reverse reaction of replacement of GTP for GDP (deactivation), consistent with prior genetic analysis of CDC25 which indicated a positive role in the activation of Ras. Guanosine Diphosphate 50-53 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 63-67 1447167-4 1992 We show that the product of a recently isolated mouse CDC25-like gene (CDC25Mm) can strongly enhance (more than 1000 times) the GDP release from both human c-Ha-ras p21 and yeast RAS2 in vitro. Guanosine Diphosphate 128-131 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 179-183 1639059-1 1992 We have previously shown that a conserved glycine at position 82 of the yeast RAS2 protein is involved in the conversion of RAS proteins from the GDP- to the GTP-bound form. Guanosine Diphosphate 146-149 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 78-82 1569942-6 1992 Cdc25 binds predominantly to the catalytically inactive GDP-bound form of Ras2, whereas a conformational change of Ras2 to its activated GTP-bound state results in its loss of binding affinity to Cdc25. Guanosine Diphosphate 56-59 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 74-78 1901951-8 1991 smg p21 GDS has low amino acid sequence homology with the yeast CDC25 and SCD25 proteins, which may regulate the GDP/GTP exchange reaction of the yeast RAS2 protein, but not with ras p21 GTPase-activating protein, the inhibitory GDP/GTP exchange proteins (GDP dissociation inhibitor) for smg p25A and rho p21s, and the beta gamma subunits of heterotrimeric GTP-binding proteins such as Gs and Gi. Guanosine Diphosphate 229-232 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 152-156 1901951-8 1991 smg p21 GDS has low amino acid sequence homology with the yeast CDC25 and SCD25 proteins, which may regulate the GDP/GTP exchange reaction of the yeast RAS2 protein, but not with ras p21 GTPase-activating protein, the inhibitory GDP/GTP exchange proteins (GDP dissociation inhibitor) for smg p25A and rho p21s, and the beta gamma subunits of heterotrimeric GTP-binding proteins such as Gs and Gi. Guanosine Diphosphate 229-232 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 152-156 2115118-8 1990 smg p25A GDI shares low amino acid sequence homology with the Saccharomyces cerevisiae CDC25-encoded protein, which has been suggested to serve as a factor that regulates the GDP-GTP exchange reaction of the yeast RAS2-encoded protein, but not with the beta gamma subunits of GTP-binding proteins having an alpha beta gamma subunit structure, such as Gs and Gi. Guanosine Diphosphate 175-178 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 214-218 2188363-4 1990 Partially purified preparations of the carboxy-terminal domain of the SCD25 gene product enhanced the exchange rate of guanosine diphosphate (GDP) to guanosine triphosphate (GTP) of pure RAS2 protein by stimulating the release of GDP. Guanosine Diphosphate 119-140 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 187-191 2188363-4 1990 Partially purified preparations of the carboxy-terminal domain of the SCD25 gene product enhanced the exchange rate of guanosine diphosphate (GDP) to guanosine triphosphate (GTP) of pure RAS2 protein by stimulating the release of GDP. Guanosine Diphosphate 142-145 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 187-191 2188363-4 1990 Partially purified preparations of the carboxy-terminal domain of the SCD25 gene product enhanced the exchange rate of guanosine diphosphate (GDP) to guanosine triphosphate (GTP) of pure RAS2 protein by stimulating the release of GDP. Guanosine Diphosphate 230-233 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 187-191 2104846-4 1990 By contrast, RAS2Ile152 shows a strong destabilization of the GDP complex (the dissociation rate constants of the RAS2Ile152.GDP complex is enhanced almost 50 times) and an increased GTPase activity. Guanosine Diphosphate 62-65 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 13-17 2104846-4 1990 By contrast, RAS2Ile152 shows a strong destabilization of the GDP complex (the dissociation rate constants of the RAS2Ile152.GDP complex is enhanced almost 50 times) and an increased GTPase activity. Guanosine Diphosphate 125-128 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 13-17 2104846-6 1990 Our kinetic results show that the functional modifications of RAS2 compensating for the CDC25 inactivation can not only be associated with the presence of a long-lived RAS2.GTP complex, but also with a rapid GDP to GTP exchange reaction. Guanosine Diphosphate 208-211 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 62-66 2104846-6 1990 Our kinetic results show that the functional modifications of RAS2 compensating for the CDC25 inactivation can not only be associated with the presence of a long-lived RAS2.GTP complex, but also with a rapid GDP to GTP exchange reaction. Guanosine Diphosphate 208-211 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 168-172 3038880-2 1987 Whereas S. cerevisiae RAS1 and RAS2 proteins were immunoprecipitated bound entirely to GDP, mammalian Harvey ras was isolated with GTP and GDP bound in near-equimolar proportions. Guanosine Diphosphate 87-90 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 31-35 3038880-3 1987 In a strain overexpressing a RAS2 variant where the RAS unique C-terminal domain was deleted, both GTP and GDP were detected in a ratio of 3:97. Guanosine Diphosphate 107-110 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 29-33 3299060-3 1987 The response of the enzyme to added RAS2 proteins bound with various guanine nucleotides and their analogs suggests that RAS2 proteins are active in their GTP-bound form and are virtually inactive in their GDP-bound form. Guanosine Diphosphate 206-209 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 36-40 3299060-3 1987 The response of the enzyme to added RAS2 proteins bound with various guanine nucleotides and their analogs suggests that RAS2 proteins are active in their GTP-bound form and are virtually inactive in their GDP-bound form. Guanosine Diphosphate 206-209 Ras family GTPase RAS2 Saccharomyces cerevisiae S288C 121-125