PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10727784-1	2000	Hypoxia may increase GABA levels in neurons by ATP depletion-induced activation of glutamate decarboxylase and by inhibiting GABA transaminase.	Adenosine Triphosphate	47-50	glutamate-ammonia ligase	Rattus norvegicus	83-106	
16530878-1	2006	BACKGROUND/AIMS: It has been proposed that, in acute liver failure, skeletal muscle adapts to become the principle organ responsible for removal of blood-borne ammonia by increasing glutamine synthesis, a reaction that is catalyzed by the cytosolic ATP-dependent enzyme glutamine synthetase.	Adenosine Triphosphate	249-252	glutamate-ammonia ligase	Rattus norvegicus	270-290	
12742096-3	2003	This reaction is catalyzed by glutamine synthetase and consumes ATP.	Adenosine Triphosphate	64-67	glutamate-ammonia ligase	Rattus norvegicus	30-50	
11882516-7	2002	The notion that increased cytoplasmic ATP levels can suppress GAD activity in beta-cells, and hence GABA production and release, is compatible with previous findings on ATP suppression of brain GAD activity.	Adenosine Triphosphate	38-41	glutamate-ammonia ligase	Rattus norvegicus	62-65	
11882516-7	2002	The notion that increased cytoplasmic ATP levels can suppress GAD activity in beta-cells, and hence GABA production and release, is compatible with previous findings on ATP suppression of brain GAD activity.	Adenosine Triphosphate	38-41	glutamate-ammonia ligase	Rattus norvegicus	194-197	
11882516-7	2002	The notion that increased cytoplasmic ATP levels can suppress GAD activity in beta-cells, and hence GABA production and release, is compatible with previous findings on ATP suppression of brain GAD activity.	Adenosine Triphosphate	169-172	glutamate-ammonia ligase	Rattus norvegicus	194-197	
20557426-1	2010	Glutamine synthetase (GS) forms glutamine by catalyzing the ATP-dependent amidation of glutamate.	Adenosine Triphosphate	60-63	glutamate-ammonia ligase	Rattus norvegicus	0-20	
15114044-1	2004	BACKGROUND/AIMS: Glutamine synthetase is a key enzyme necessary for ammonia detoxification in the brain, but excessive activation of this enzyme can be cytotoxic to neural cells as a consequence of excessive consumption of ATP and glutamate.	Adenosine Triphosphate	223-226	glutamate-ammonia ligase	Rattus norvegicus	17-37	
9752723-1	1998	Glutamine synthetase, the enzyme that catalyzes the ATP-dependent conversion of glutamate and ammonia into glutamine, is expressed in a tissue-specific and developmentally controlled manner.	Adenosine Triphosphate	52-55	glutamate-ammonia ligase	Rattus norvegicus	0-20	
2434618-6	1987	They suggest that Ca2+ and the Na+, K+ pump may serve a role in regulating the activity of ATP-dependent glutamine synthetase, a key enzyme of the glutamate-glutamine cycle, located in the astrocytes.	Adenosine Triphosphate	91-94	glutamate-ammonia ligase	Rattus norvegicus	105-125	
7487913-5	1995	A linear increase of 1/v with 1/s permitted estimation of the in vivo glutamine synthetase (GS) activity at a physiological blood ammonia concentration to be 0.4-2.1 mumol/h per g. The observed ammonia-dependence strongly suggests that, under physiological conditions, in vivo GS activity is kinetically limited by sub-optimal in situ concentrations of ammonia as well as glutamate and ATP.	Adenosine Triphosphate	386-389	glutamate-ammonia ligase	Rattus norvegicus	70-90	
1363168-1	1992	Glutamine synthetase (L-glutamate:ammonia ligase; EC 6.3.1.2), an enzyme catalysing the ATP-dependent formation of glutamine from glutamate and ammonia, was detected immunocytochemically only in glial (interstitial) cells of the superficial pineal gland of the rat.	Adenosine Triphosphate	88-91	glutamate-ammonia ligase	Rattus norvegicus	0-20	
7882063-2	1994	The enzyme activators, chlorides and adenosine triphosphate influenced in varying measures the GAD activity in renal homogenates of both controlled and acidotic animals.	Adenosine Triphosphate	37-59	glutamate-ammonia ligase	Rattus norvegicus	95-98	
5472154-2	1970	A radiochemical assay for glutamine synthetase has been developed in which an ATP-regenerating system is incorporated to prevent accumulation of inhibitory amounts of ADP.	Adenosine Triphosphate	78-81	glutamate-ammonia ligase	Rattus norvegicus	26-46