PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15657-1	1977	A highly purified preparation of glutamine synthetase from chlorella grown on a medium containing nitrate as a sole source of nitrogen, was isolated and characterized by disc-electrophoresis and analytical ultracentrifugation.	Nitrates	98-105	glutamate-ammonia ligase	Homo sapiens	33-53	
170914-6	1975	The significance of the enzyme in conjunction with glutamine synthetase in the assimilation of nitrate by roots is discussed.	Nitrates	95-102	glutamate-ammonia ligase	Homo sapiens	51-71	
27009655-4	2012	Urease and glutamine synthetase (GS) activities varied with nitrogen source in a manner consistent with regulation by cellular nitrogen status via NtcA (rather than by external availability of nitrogen) in all three strains and indicated that each strain experienced some degree of nitrogen insufficiency during growth on nitrate.	Nitrates	322-329	glutamate-ammonia ligase	Homo sapiens	33-35	
5557824-0	1971	[Regulation of plant glutamine synthetase by ammonium and nitrate].	Nitrates	58-65	glutamate-ammonia ligase	Homo sapiens	21-41	
33460896-7	2021	Metagenomics analysis revealed that the preferred metabolic pathway of nitrogen was from ammonium to glutamate via glutamine, and the enzymes governing this transformation were glutamine synthetase and glutamate synthetase; while in nitrate based amendment, the conversion from nitrite to ammonium was restrained by the low abundance of nitrite reductase enzyme and therefore retarded the TPH degradation rate.	Nitrates	233-240	glutamate-ammonia ligase	Homo sapiens	177-197	
19449127-2	2010	Here, we report on the regulation of a cytosolic glutamine synthetase (CsGS) from Camellia sinensis (L.) O. Kuntze during developmental stages and light/dark conditions on the utilization of nitrate and ammonia.	Nitrates	191-198	glutamate-ammonia ligase	Homo sapiens	49-69	
22942686-1	2012	Glutamine synthetase (GS) is the key enzyme involved in the assimilation of ammonia derived either from nitrate reduction, N(2) fixation, photorespiration or asparagine breakdown.	Nitrates	104-111	glutamate-ammonia ligase	Homo sapiens	0-20	
16392746-0	2005	Regulation of glutamine synthetase and glutamate dehydrogenase in pea mutants rrrbrb, rrRbRb, and RRrbrb during nitrate nitrogen assimilation.	Nitrates	112-119	glutamate-ammonia ligase	Homo sapiens	14-34	
24276702-0	1981	Glutamine synthetase of Chlamydomonas: its role in the control of nitrate assimilation.	Nitrates	66-73	glutamate-ammonia ligase	Homo sapiens	0-20	
16662109-3	1981	Biosynthetic glutamine synthetase activity was 1.5 to 1.8 times greater in nitrogen-limited cells than cells grown at high levels of the three nitrogen sources.Conversely, glutamate dehydrogenase (both NADH- and NADPH-dependent activities) was greatest in cells grown at high levels of asparagine or ammonium, while nitrate-grown cells possessed little activity at all concentrations employed.	Nitrates	316-323	glutamate-ammonia ligase	Homo sapiens	13-33