PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9801064-3	1998	In the present study, we found the 28 kDa protein to have thiol-dependent antioxidant activity, thereby protecting radical-sensitive proteins such as glutamine synthetase and hemoglobin from oxidative modification caused by thiol-dependent metal ion-catalyzed oxidation system.	Sulfhydryl Compounds	58-63	glutamate-ammonia ligase	Rattus norvegicus	150-170	
9801064-3	1998	In the present study, we found the 28 kDa protein to have thiol-dependent antioxidant activity, thereby protecting radical-sensitive proteins such as glutamine synthetase and hemoglobin from oxidative modification caused by thiol-dependent metal ion-catalyzed oxidation system.	Sulfhydryl Compounds	224-229	glutamate-ammonia ligase	Rattus norvegicus	150-170	
8794470-4	1996	The results suggest that reaction of the iminium bond in the benzophenanthridine molecule with thiol groups of the enzyme participates in GAD inhibition.	Sulfhydryl Compounds	95-100	glutamate-ammonia ligase	Rattus norvegicus	138-141	
7488219-3	1995	The purified protein showed the thiol-specific antioxidant activity and protected glutamine synthetase from inactivation by a mixed metal-thiol oxidation.	Sulfhydryl Compounds	32-37	glutamate-ammonia ligase	Rattus norvegicus	82-102	
7488219-3	1995	The purified protein showed the thiol-specific antioxidant activity and protected glutamine synthetase from inactivation by a mixed metal-thiol oxidation.	Sulfhydryl Compounds	138-143	glutamate-ammonia ligase	Rattus norvegicus	82-102	
2999224-9	1985	These receptor alterations may be attributed to a disuse and/or a partial degeneration of nerve terminals due to peripheral neurotoxins (i.e., ammonia, mercaptans, short chain fatty acids) and the decrease of glutamate decarboxylase activity and of zinc levels in brain tissues seems to be respectively a direct and an indirect demonstration of this phenomenon.	Sulfhydryl Compounds	152-162	glutamate-ammonia ligase	Rattus norvegicus	209-232