PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7982492-5	1994	The SSAT-induced changes in cellular polyamine content resulted in a compensatory increase in the activities of ornithine decarboxylase and S-adenosylmethionine decarboxylase, i.e. the enzymes catalyzing the rate-limiting steps in polyamine biosynthesis.	Polyamines	37-46	spermidine/spermine N1-acetyltransferase 1	Homo sapiens	4-8	
7982492-5	1994	The SSAT-induced changes in cellular polyamine content resulted in a compensatory increase in the activities of ornithine decarboxylase and S-adenosylmethionine decarboxylase, i.e. the enzymes catalyzing the rate-limiting steps in polyamine biosynthesis.	Polyamines	231-240	spermidine/spermine N1-acetyltransferase 1	Homo sapiens	4-8	
7982492-6	1994	This is the first demonstration that a primary increase in SSAT activity will induce an interconversion-like change in the polyamine levels and the physiological role of SSAT is most likely to protect cells against too high concentrations of spermidine and spermine.	Polyamines	123-132	spermidine/spermine N1-acetyltransferase 1	Homo sapiens	59-63