PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7814412-10	1995	Mammalian SSADH contains significant homology to bacterial NADP(+)-succinic semialdehyde dehydrogenase (EC 1.2.1.16) and conserved regions of general aldehyde dehydrogenases (EC 1.2.1.3), suggesting it is a member of the aldehyde dehydrogenase superfamily of proteins.	NADP	59-63	aldehyde dehydrogenase 5 family member A1	Homo sapiens	10-15	
20174634-5	2010	In the E. coli SSADH structure, electron density for the complete NADP+ cofactor in the binding sites is clearly evident; these data in particular revealing how the nicotinamide ring of the cofactor is positioned in each active site.	NADP	66-71	aldehyde dehydrogenase 5 family member A1	Homo sapiens	15-20	
20174634-6	2010	CONCLUSIONS/SIGNIFICANCE: Our structural data suggest that a deletion of three amino acids in E. coli SSADH permits this enzyme to use NADP+, whereas in contrast the human enzyme utilises NAD+.	NADP	135-140	aldehyde dehydrogenase 5 family member A1	Homo sapiens	102-107	
7814412-10	1995	Mammalian SSADH contains significant homology to bacterial NADP(+)-succinic semialdehyde dehydrogenase (EC 1.2.1.16) and conserved regions of general aldehyde dehydrogenases (EC 1.2.1.3), suggesting it is a member of the aldehyde dehydrogenase superfamily of proteins.	NADP	59-63	aldehyde dehydrogenase 5 family member A1	Homo sapiens	67-102