PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15051535-6	2004	Ratios of individual metabolite levels to total metabolite levels provided evidence of competitive inhibition of CYP 2E1 enzymes leading to increased production of phenol, catechol, and phenylmercapturic acid at the expense of hydroquinone, trihydroxybenzene, and muconic acid.	Phloroglucinol	241-258	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	113-120	
27637483-6	2016	Catechol and trihydroxybenzene (activated by CYP2E1) induced micronuclei most strongly at 6h/18h, whereas somewhat longer exposures were optimal for hydroquinone, another compound activated by CYP2E1.	Phloroglucinol	13-30	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	45-51	
27637483-6	2016	Catechol and trihydroxybenzene (activated by CYP2E1) induced micronuclei most strongly at 6h/18h, whereas somewhat longer exposures were optimal for hydroquinone, another compound activated by CYP2E1.	Phloroglucinol	13-30	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	193-199	
25771868-9	2014	These results suggest that in addition to activating benzene and phenol, human CYP2E1 may further convert hydroquinone, catechol and trihydroxybenzene to more genotoxic metabolites, and sulfo-conjugation of the multi-hydroxylated metabolites of benzene by human SULT1A1 may represent an important detoxifying pathway.	Phloroglucinol	133-150	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	79-85