PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
6240981-5	1984	The inhibition of glucokinase activity by alloxan was protected by the simultaneous presence of 15 mM hexose such as D-glucose, 3-O-methylglucose, or D-mannose.	Mannose	150-159	glucokinase	Rattus norvegicus	18-29	
3296598-7	1987	Glucokinase activity was protected from alloxan toxicity only by D-glucose and D-mannose; the alpha anomer of D-glucose provided significantly greater protection than the beta anomer.	Mannose	79-88	glucokinase	Rattus norvegicus	0-11	
3530846-4	1986	Inactivation of purified glucokinase was antagonized by glucose, mannose, and 2-deoxyglucose in order of decreasing potency but not by 3-O-methylglucose.	Mannose	65-72	glucokinase	Rattus norvegicus	25-36	
3530846-8	1986	The finding that glucokinase is inactivated by alloxan and protected by glucose with discrimination of its anomers similar to inhibition of glucose-stimulated insulin secretion by alloxan supports this hypothesis and appears to explain the mechanism for inhibition of hexose-stimulated insulin secretion by this agent and the unique role of glucose and mannose as protecting agents.	Mannose	353-360	glucokinase	Rattus norvegicus	17-28	
6317500-0	1983	Mannose phosphorylation by glucokinase from liver and transplantable insulinoma.	Mannose	0-7	glucokinase	Rattus norvegicus	27-38	
6317500-3	1983	Phosphorylation of alpha,beta-D-mannose by glucokinase occurred with cooperative rate dependence on mannose concentration (nH: 1.50).	Mannose	32-39	glucokinase	Rattus norvegicus	43-54	
6317500-8	1983	Islet glucokinase has previously been shown to be chromatographically and kinetically identical to glucokinase from insulinoma and liver; therefore, evidence that glucokinase from these two tissues phosphorylates mannose with cooperative rate dependence and differentiates mannose anomers supports the glucokinase-glucose sensor hypothesis.	Mannose	213-220	glucokinase	Rattus norvegicus	6-17	
6317500-8	1983	Islet glucokinase has previously been shown to be chromatographically and kinetically identical to glucokinase from insulinoma and liver; therefore, evidence that glucokinase from these two tissues phosphorylates mannose with cooperative rate dependence and differentiates mannose anomers supports the glucokinase-glucose sensor hypothesis.	Mannose	213-220	glucokinase	Rattus norvegicus	99-110	
6317500-8	1983	Islet glucokinase has previously been shown to be chromatographically and kinetically identical to glucokinase from insulinoma and liver; therefore, evidence that glucokinase from these two tissues phosphorylates mannose with cooperative rate dependence and differentiates mannose anomers supports the glucokinase-glucose sensor hypothesis.	Mannose	213-220	glucokinase	Rattus norvegicus	99-110	
6317500-8	1983	Islet glucokinase has previously been shown to be chromatographically and kinetically identical to glucokinase from insulinoma and liver; therefore, evidence that glucokinase from these two tissues phosphorylates mannose with cooperative rate dependence and differentiates mannose anomers supports the glucokinase-glucose sensor hypothesis.	Mannose	213-220	glucokinase	Rattus norvegicus	99-110	
6317500-8	1983	Islet glucokinase has previously been shown to be chromatographically and kinetically identical to glucokinase from insulinoma and liver; therefore, evidence that glucokinase from these two tissues phosphorylates mannose with cooperative rate dependence and differentiates mannose anomers supports the glucokinase-glucose sensor hypothesis.	Mannose	273-280	glucokinase	Rattus norvegicus	6-17	
8513967-2	1993	The inactivation of glucokinase by glyceraldehyde was blocked by the presence of its substrates such as glucose and mannose.	Mannose	116-123	glucokinase	Rattus norvegicus	20-31	
6385980-2	1983	This result may explain our previous findings of the alpha-anomeric preference in glucose- and mannose-stimulated insulin release, and therefore suggests to support the hypothesis that glucokinase in islets functions as a crucial hexose sensing enzyme for insulin release induced by glucose and mannose.	Mannose	95-102	glucokinase	Rattus norvegicus	185-196	
6385980-2	1983	This result may explain our previous findings of the alpha-anomeric preference in glucose- and mannose-stimulated insulin release, and therefore suggests to support the hypothesis that glucokinase in islets functions as a crucial hexose sensing enzyme for insulin release induced by glucose and mannose.	Mannose	295-302	glucokinase	Rattus norvegicus	185-196	
5944237-7	1966	Glucokinase catalyses the phosphorylation of glucose, mannose and 2-deoxyglucose.	Mannose	54-61	glucokinase	Rattus norvegicus	0-11	
9376178-8	1997	Mannose (20 mM), a substrate of GK, and sorbitol (1 mM), a stimulator of glucose phosphorylation by GK, induced the translocation of GK from the nucleus to the cytoplasm in the presence of 5 mM glucose.	Mannose	0-7	glucokinase	Rattus norvegicus	32-34