PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
2475503-7	1989	These data suggest that the detrimental deficiency of this one patient results from a structurally altered UMP synthase that is probably present in low steady-state amounts due to proteolysis and that this labile protein can be stabilized against heat denaturation and proteolytic degradation by 6-aza-UMP.	6-azauridine-5'-monophosphate	296-305	uridine monophosphate synthetase	Homo sapiens	107-119	
497352-0	1979	Theoretical drug design: 6-azauridine-5"-phosphate--its X-ray crystal structure, potential energy maps, and mechanism of inhibition of orotidine-5"-phosphate decarboxylase.	6-azauridine-5'-monophosphate	25-50	uridine monophosphate synthetase	Homo sapiens	135-171	
3680222-7	1987	Preliminary characterization of the human placental UMP synthase showed it to be similar to UMP synthase from the Ehrlich ascites carcinoma in subunit molecular weight, native molecular weight, isozyme pattern (although not absolute pI values), pH optima of enzymatic activities, and kinetic constants for orotidine 5"-monophosphate (Km) and 6-azauridine 5"-monophosphate (Ki) at the decarboxylase site.	6-azauridine-5'-monophosphate	342-371	uridine monophosphate synthetase	Homo sapiens	52-64	
7006681-0	1980	Inhibition of orotidine-5"-phosphate decarboxylase by 1-(5"-phospho-beta-d-ribofuranosyl)barbituric acid, 6-azauridine 5"-phosphate, and uridine 5"-phosphate.	6-azauridine-5'-monophosphate	106-131	uridine monophosphate synthetase	Homo sapiens	14-50