PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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+.	NAD	188-192	aldehyde dehydrogenase 5 family member A1	Homo sapiens	102-107	
18588919-5	2008	This recombinant cattle tick protein has potent NAD(+)-dependent SSADH activity, but possesses also marked enzymatic activity on other aliphatic and aromatic aldehyde substrates.	NAD	48-54	aldehyde dehydrogenase 5 family member A1	Homo sapiens	65-70	
33203024-3	2020	Here, we present a patient with a severe phenotype of SSADHD caused by a novel genetic variant c.728T > C that leads to an exchange of leucine to proline at residue 243, located within the highly conserved nicotinamide adenine dinucleotide (NAD)+ binding domain of SSADH.	NAD	206-239	aldehyde dehydrogenase 5 family member A1	Homo sapiens	54-59	
33203024-3	2020	Here, we present a patient with a severe phenotype of SSADHD caused by a novel genetic variant c.728T > C that leads to an exchange of leucine to proline at residue 243, located within the highly conserved nicotinamide adenine dinucleotide (NAD)+ binding domain of SSADH.	NAD	241-244	aldehyde dehydrogenase 5 family member A1	Homo sapiens	54-59