PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
8730097-6	1996	We also show that the two genes are differentially regulated: SDC25 is not transcribed at a detectable level in growth conditions when glucose is the carbon source.	Glucose	135-142	SDC25	Saccharomyces cerevisiae S288C	62-67
10747953-2	2000	We have analyzed the function of this region and the effect of its farnesylation with respect to the action of the GDP/GTP exchange factors (GEFs) Cdc25p and Sdc25p and the target adenylyl cyclase.	Guanosine Diphosphate	115-118	SDC25	Saccharomyces cerevisiae S288C	158-164
10747953-2	2000	We have analyzed the function of this region and the effect of its farnesylation with respect to the action of the GDP/GTP exchange factors (GEFs) Cdc25p and Sdc25p and the target adenylyl cyclase.	Guanosine Triphosphate	119-122	SDC25	Saccharomyces cerevisiae S288C	158-164
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 Triphosphate	87-90	SDC25	Saccharomyces cerevisiae S288C	150-156
8730097-6	1996	We also show that the two genes are differentially regulated: SDC25 is not transcribed at a detectable level in growth conditions when glucose is the carbon source.	Carbon	150-156	SDC25	Saccharomyces cerevisiae S288C	62-67
7851434-0	1995	Properties of the catalytic domain of sdc25p, a yeast GDP/GTP exchange factor of Ras proteins.	Guanosine Triphosphate	58-61	SDC25	Saccharomyces cerevisiae S288C	38-44
7657656-1	1995	The Cdc25p and Sdc25p proteins were the first members of the family of guanine nucleotide exchange factors to be identified.	Guanine Nucleotides	71-89	SDC25	Saccharomyces cerevisiae S288C	15-21
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.	Guanine Nucleotides	23-41	SDC25	Saccharomyces cerevisiae S288C	53-59
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	SDC25	Saccharomyces cerevisiae S288C	53-59
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 Triphosphate	100-103	SDC25	Saccharomyces cerevisiae S288C	53-59
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	SDC25	Saccharomyces cerevisiae S288C	73-79
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	SDC25	Saccharomyces cerevisiae S288C	158-164
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 Triphosphate	39-42	SDC25	Saccharomyces cerevisiae S288C	73-79
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 Triphosphate	39-42	SDC25	Saccharomyces cerevisiae S288C	158-164
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	SDC25	Saccharomyces cerevisiae S288C	29-35
8325863-0	1993	Properties of the SDC25 C-domain, a GDP to GTP exchange factor of RAS proteins and in vitro modulation of adenylyl cyclase.	Guanosine Diphosphate	36-39	SDC25	Saccharomyces cerevisiae S288C	18-23
8325863-0	1993	Properties of the SDC25 C-domain, a GDP to GTP exchange factor of RAS proteins and in vitro modulation of adenylyl cyclase.	Guanosine Triphosphate	43-46	SDC25	Saccharomyces cerevisiae S288C	18-23
1429624-6	1992	Both CDC25 and a truncated SDC25 also restored p21H-ras-dependent guanyl nucleotide response in a strain isogenic to the one described above but containing a disrupted CDC25 locus instead of the temperature-sensitive allele.	guanyl nucleotide	66-83	SDC25	Saccharomyces cerevisiae S288C	27-32
8380225-0	1993	The Saccharomyces cerevisiae SDC25 C-domain gene product overcomes the dominant inhibitory activity of Ha-Ras Asn-17.	Asparagine	110-113	SDC25	Saccharomyces cerevisiae S288C	29-34
8380225-6	1993	On the other hand, transactivation of the Ras-responsive element of the Py tk promoter induced by SDC25 C domain is lost upon coexpression of increasing amounts of Ha-Ras Asn-17.	Asparagine	171-174	SDC25	Saccharomyces cerevisiae S288C	98-103
8380225-7	1993	In addition, coexpression of SDC25 C domain overcomes the inhibition of proliferation of NIH 3T3 cells caused by Ha-Ras Asn-17.	Asparagine	120-123	SDC25	Saccharomyces cerevisiae S288C	29-34
7999142-7	1993	We have demonstrated that the SDC25 C-terminus domain promotes GTP binding to Ras p21 in CHO cells.	Guanosine Triphosphate	63-66	SDC25	Saccharomyces cerevisiae S288C	30-35
22575457-2	2012	cAMP is produced by adenylate cyclase, which is activated both by Gpr1/Gpa2 system and Ras proteins, regulated by Cdc25/Sdc25 guanine exchange factors and Ira GTPase activator proteins.	Cyclic AMP	0-4	SDC25	Saccharomyces cerevisiae S288C	120-125
1569942-2	1992	We have been able to show for the first time that the guanine nucleotide exchange proteins Cdc25 and Sdc25 from Saccharomyces cerevisiae bind directly to their targets Ras1 and Ras2 in vivo.	Guanine Nucleotides	54-72	SDC25	Saccharomyces cerevisiae S288C	101-106
22575457-2	2012	cAMP is produced by adenylate cyclase, which is activated both by Gpr1/Gpa2 system and Ras proteins, regulated by Cdc25/Sdc25 guanine exchange factors and Ira GTPase activator proteins.	Guanine	126-133	SDC25	Saccharomyces cerevisiae S288C	120-125
22036786-2	2011	Ras proteins are regulated by Ira1/2 GTPase activating proteins (GAPs) and Cdc25/Sdc25 guanine nucleotide exchange factors (GEFs).	Guanine Nucleotides	87-105	SDC25	Saccharomyces cerevisiae S288C	81-86