PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2663189-2	1989	The mutant grew normally in galactose medium, but in glucose medium, in which the promoter was repressed, it ceased growing after 12-15 h. The growth arrest was associated with a decrease in intracellular calmodulin levels: after 12 h, no intracellular calmodulin protein was detectable.	Glucose	53-60	calmodulin	Saccharomyces cerevisiae S288C	205-215	
9148755-0	1997	Glucose-independent inhibition of yeast plasma-membrane H+-ATPase by calmodulin antagonists.	Glucose	0-7	calmodulin	Saccharomyces cerevisiae S288C	69-79	
9148755-4	1997	The physiological role of a calmodulin-dependent protein kinase in glucose-induced activation was investigated by studying the effect of specific calmodulin antagonists on the glucose-induced ATPase kinetic changes in wild-type and two mutant strains affected in the glucose regulation of the enzyme.	Glucose	67-74	calmodulin	Saccharomyces cerevisiae S288C	28-38	
9148755-4	1997	The physiological role of a calmodulin-dependent protein kinase in glucose-induced activation was investigated by studying the effect of specific calmodulin antagonists on the glucose-induced ATPase kinetic changes in wild-type and two mutant strains affected in the glucose regulation of the enzyme.	Glucose	67-74	calmodulin	Saccharomyces cerevisiae S288C	146-156	
9148755-4	1997	The physiological role of a calmodulin-dependent protein kinase in glucose-induced activation was investigated by studying the effect of specific calmodulin antagonists on the glucose-induced ATPase kinetic changes in wild-type and two mutant strains affected in the glucose regulation of the enzyme.	Glucose	176-183	calmodulin	Saccharomyces cerevisiae S288C	28-38	
9148755-4	1997	The physiological role of a calmodulin-dependent protein kinase in glucose-induced activation was investigated by studying the effect of specific calmodulin antagonists on the glucose-induced ATPase kinetic changes in wild-type and two mutant strains affected in the glucose regulation of the enzyme.	Glucose	176-183	calmodulin	Saccharomyces cerevisiae S288C	146-156	
9148755-6	1997	In one mutant, pma1-T912A, the putative calmodulin-dependent protein kinase-phosphorylatable Thr-912 was eliminated, and in the other, pma1-P536L, H+-ATPase was constitutively activated, suggesting that the antagonistic effect was not mediated by a calmodulin-dependent protein kinase and not related to glucose regulation.	Glucose	304-311	calmodulin	Saccharomyces cerevisiae S288C	40-50	
2663189-2	1989	The mutant grew normally in galactose medium, but in glucose medium, in which the promoter was repressed, it ceased growing after 12-15 h. The growth arrest was associated with a decrease in intracellular calmodulin levels: after 12 h, no intracellular calmodulin protein was detectable.	Glucose	53-60	calmodulin	Saccharomyces cerevisiae S288C	253-263