PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
6260797-15	1981	The factors responsible for the biphasic kinetics of oxidation by intact mitochondria and biphasic binding of sterol substrates by partially purified preparations of cytochrome P-450scc are still unknown.	Sterols	110-116	cholesterol side-chain cleavage enzyme, mitochondrial	Bos taurus	166-185	
7213622-7	1981	The presence of these sterols as native constituents of cytochrome P-450scc supports their role as enzyme-bound intermediates in the biosynthesis of pregnenolone from cholesterol.	Sterols	22-29	cholesterol side-chain cleavage enzyme, mitochondrial	Bos taurus	56-75	
25130438-12	2014	The previously reported biological activity of pL and the presence of CYP11A1 in skin suggest that this pathway may serve to produce biologically active products from L3, emphasizing a novel role of CYP11A1 in sterol metabolism.	Sterols	210-216	cholesterol side-chain cleavage enzyme, mitochondrial	Bos taurus	70-77	
25130438-12	2014	The previously reported biological activity of pL and the presence of CYP11A1 in skin suggest that this pathway may serve to produce biologically active products from L3, emphasizing a novel role of CYP11A1 in sterol metabolism.	Sterols	210-216	cholesterol side-chain cleavage enzyme, mitochondrial	Bos taurus	199-206	
23124253-1	2013	Docking simulations and experimental data indicate that 22-(N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)amino)-23,24-bisnor-5-cholen-3beta-ol (22-NBD-cholesterol), a common fluorescent sterol analog, binds into active sites of bovine cytochrome P450scc and microbial cholesterol dehydrogenases (CHDHs) and then undergoes regiospecific oxidations by these enzymes.	Sterols	148-154	cholesterol side-chain cleavage enzyme, mitochondrial	Bos taurus	227-245