PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
3978151-1	1985	The role of tyrosine residues of cytochrome P-450scc in the interaction with adrenodoxin and cholesterol was investigated, using chemical modifications with tetranitromethane.	Tetranitromethane	157-174	cytochrome P450 family 11 subfamily A member 1	Homo sapiens	33-52	
3978151-4	1985	Both high spin effectors, i.e., substrate and adrenodoxin, prevent cytochrome P-450scc from the inactivation caused by tetranitromethane.	Tetranitromethane	119-136	cytochrome P450 family 11 subfamily A member 1	Homo sapiens	67-86	
6487639-0	1984	Chemical modification of adrenocortical cytochrome P-450scc with tetranitromethane.	Tetranitromethane	65-82	cytochrome P450 family 11 subfamily A member 1	Homo sapiens	40-59	
6487639-1	1984	Selective chemical modification of adrenocortical cytochrome P-450scc, responsible for key stages of steroid biogenesis, with tetranitromethane has been carried out.	Tetranitromethane	126-143	cytochrome P450 family 11 subfamily A member 1	Homo sapiens	50-69	
6487639-3	1984	Analysis of the cytochrome P-450scc inactivation kinetics indicates that there are several pools of tyrosine residues, differing in their accessibility to tetranitromethane.	Tetranitromethane	155-172	cytochrome P450 family 11 subfamily A member 1	Homo sapiens	16-35	
6487639-5	1984	Cholesterol and adrenodoxin (high-spin effectors) prevent the inactivation of cytochrome P-450scc with tetranitromethane, i.e., protect the essential tyrosine residue(s) from modification.	Tetranitromethane	103-120	cytochrome P450 family 11 subfamily A member 1	Homo sapiens	78-97