PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7646448-2	1995	It was found that glucose-6-phosphatase activity in histone II-A-pretreated liver microsomes was stimulated to the same extent as in detergent-permeabilized microsomes, and that the substrate specificity of the enzyme for glucose 6-phosphate was lost in histone II-A-pretreated microsomes, as [U-14C]glucose-6-phosphate hydrolysis was inhibited by mannose 6-phosphate and [U-14C]mannose 6-phosphate hydrolysis was increased.	mannose-6-phosphate	348-367	glucose-6-phosphatase catalytic subunit 1	Homo sapiens	18-39	
8611029-0	1996	Glucose 6-phosphate and mannose 6-phosphate are equally and more actively hydrolyzed by glucose 6-phosphatase during hysteretic transition within intact microsomal membrane than after detergent treatment.	mannose-6-phosphate	24-43	glucose-6-phosphatase catalytic subunit 1	Homo sapiens	88-109	
8611029-1	1996	We have studied the rapid kinetics of glucose-6-phosphatase (Glc6Pase) toward glucose 6-phosphate (Glc6P) and mannose 6-phosphate (Man6P) in intact and detergent-treated microsomes, using a radiometric assay based on the use of [U(-)14C]hexose 6-phosphates.	mannose-6-phosphate	110-129	glucose-6-phosphatase catalytic subunit 1	Homo sapiens	38-59	
8611029-1	1996	We have studied the rapid kinetics of glucose-6-phosphatase (Glc6Pase) toward glucose 6-phosphate (Glc6P) and mannose 6-phosphate (Man6P) in intact and detergent-treated microsomes, using a radiometric assay based on the use of [U(-)14C]hexose 6-phosphates.	mannose-6-phosphate	110-129	glucose-6-phosphatase catalytic subunit 1	Homo sapiens	61-69	
8611029-1	1996	We have studied the rapid kinetics of glucose-6-phosphatase (Glc6Pase) toward glucose 6-phosphate (Glc6P) and mannose 6-phosphate (Man6P) in intact and detergent-treated microsomes, using a radiometric assay based on the use of [U(-)14C]hexose 6-phosphates.	mannose-6-phosphate	131-136	glucose-6-phosphatase catalytic subunit 1	Homo sapiens	38-59	
8611029-1	1996	We have studied the rapid kinetics of glucose-6-phosphatase (Glc6Pase) toward glucose 6-phosphate (Glc6P) and mannose 6-phosphate (Man6P) in intact and detergent-treated microsomes, using a radiometric assay based on the use of [U(-)14C]hexose 6-phosphates.	mannose-6-phosphate	131-136	glucose-6-phosphatase catalytic subunit 1	Homo sapiens	61-69	
8611029-3	1996	During the hysteretic transition, preceding the steady-state rate of hydrolysis, Glc6Pase is able to hydrolyze both Glc6P and Man6P at very similar rates.	mannose-6-phosphate	126-131	glucose-6-phosphatase catalytic subunit 1	Homo sapiens	81-89	
7646448-2	1995	It was found that glucose-6-phosphatase activity in histone II-A-pretreated liver microsomes was stimulated to the same extent as in detergent-permeabilized microsomes, and that the substrate specificity of the enzyme for glucose 6-phosphate was lost in histone II-A-pretreated microsomes, as [U-14C]glucose-6-phosphate hydrolysis was inhibited by mannose 6-phosphate and [U-14C]mannose 6-phosphate hydrolysis was increased.	mannose-6-phosphate	379-398	glucose-6-phosphatase catalytic subunit 1	Homo sapiens	18-39	
7706226-2	1994	On the contrary, Glc6Pase of detergent-treated liver microsomes is able to hydrolyze both Glc6P and mannose-6-phosphate (Man6P) with the same affinities and rates (Km and Vmax) at pH 6.5 [Ajzannay, A., Minassian, C., Riou, J.P., and Mithieux, G. (1993) Eur.	mannose-6-phosphate	100-119	glucose-6-phosphatase catalytic subunit 1	Homo sapiens	17-25	
7706226-2	1994	On the contrary, Glc6Pase of detergent-treated liver microsomes is able to hydrolyze both Glc6P and mannose-6-phosphate (Man6P) with the same affinities and rates (Km and Vmax) at pH 6.5 [Ajzannay, A., Minassian, C., Riou, J.P., and Mithieux, G. (1993) Eur.	mannose-6-phosphate	121-126	glucose-6-phosphatase catalytic subunit 1	Homo sapiens	17-25	
7706226-8	1994	These data provide direct evidence that, in the presence of both Glc6P and Man6P, Glc6Pase is able to exhibit a specific, albeit limited, kinetic behavior towards the former after detergent treatment of the membrane.	mannose-6-phosphate	75-80	glucose-6-phosphatase catalytic subunit 1	Homo sapiens	82-90	
1318223-3	1992	It was found that the pre-incubation of intact microsomes with mannose-6-phosphate or glucose-6-phosphate (50 microM for 30 s) suppressed the burst in glucose-6-phosphatase activity, that the hysteretic transition was reversible and that mannose-6-phosphate inhibited glucose-6-phosphate hydrolysis during the first seconds of incubation, but not anymore after the burst.	mannose-6-phosphate	63-82	glucose-6-phosphatase catalytic subunit 1	Homo sapiens	151-172	
1319283-2	1992	In order to evaluate the degree of ER membrane integrity, glucose-6-phosphatase (G6P-A) was localized in light and electron microscopy using glucose-6-phosphate (G6P) and mannose-6-phosphate (M6P) as substrates.	mannose-6-phosphate	171-190	glucose-6-phosphatase catalytic subunit 1	Homo sapiens	58-79	
1319283-2	1992	In order to evaluate the degree of ER membrane integrity, glucose-6-phosphatase (G6P-A) was localized in light and electron microscopy using glucose-6-phosphate (G6P) and mannose-6-phosphate (M6P) as substrates.	mannose-6-phosphate	171-190	glucose-6-phosphatase catalytic subunit 1	Homo sapiens	81-86	
1319283-2	1992	In order to evaluate the degree of ER membrane integrity, glucose-6-phosphatase (G6P-A) was localized in light and electron microscopy using glucose-6-phosphate (G6P) and mannose-6-phosphate (M6P) as substrates.	mannose-6-phosphate	192-195	glucose-6-phosphatase catalytic subunit 1	Homo sapiens	58-79	
1319283-2	1992	In order to evaluate the degree of ER membrane integrity, glucose-6-phosphatase (G6P-A) was localized in light and electron microscopy using glucose-6-phosphate (G6P) and mannose-6-phosphate (M6P) as substrates.	mannose-6-phosphate	192-195	glucose-6-phosphatase catalytic subunit 1	Homo sapiens	81-86