PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
18039331-5	2008	Kinetic analysis of the purified protein shows that RDH13 is catalytically active and recognizes retinoids as substrates.	Retinoids	97-106	retinol dehydrogenase 13	Homo sapiens	52-57
18039331-6	2008	Similar to the microsomal RDHs, RDH11, RDH12 and RDH14, RDH13 exhibits a much lower Km value for NADPH than for NADH and has a greater catalytic efficiency in the reductive than in the oxidative direction.	NADP	97-102	retinol dehydrogenase 13	Homo sapiens	56-61
18039331-6	2008	Similar to the microsomal RDHs, RDH11, RDH12 and RDH14, RDH13 exhibits a much lower Km value for NADPH than for NADH and has a greater catalytic efficiency in the reductive than in the oxidative direction.	NAD	112-116	retinol dehydrogenase 13	Homo sapiens	56-61
18039331-7	2008	The localization of RDH13 at the entrance to the mitochondrial matrix suggests that it may function to protect mitochondria against oxidative stress associated with the highly reactive retinaldehyde produced from dietary beta-carotene.	Retinaldehyde	185-198	retinol dehydrogenase 13	Homo sapiens	20-25
18039331-7	2008	The localization of RDH13 at the entrance to the mitochondrial matrix suggests that it may function to protect mitochondria against oxidative stress associated with the highly reactive retinaldehyde produced from dietary beta-carotene.	beta Carotene	221-234	retinol dehydrogenase 13	Homo sapiens	20-25
29656332-1	2019	Mitochondrion-localized retinol dehydrogenase 13 (Rdh13) is a short-chain dehydrogenase/reductase involved in vitamin A metabolism in both humans and mice.	Vitamin A	110-119	retinol dehydrogenase 13	Homo sapiens	24-48
29656332-1	2019	Mitochondrion-localized retinol dehydrogenase 13 (Rdh13) is a short-chain dehydrogenase/reductase involved in vitamin A metabolism in both humans and mice.	Vitamin A	110-119	retinol dehydrogenase 13	Homo sapiens	50-55