PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8286335-0	1994	Thiophene derivatives as new mechanism-based inhibitors of cytochromes P-450: inactivation of yeast-expressed human liver cytochrome P-450 2C9 by tienilic acid.	Thiophenes	0-9	cytochrome P450 family 2 subfamily C member 9	Homo sapiens	122-142	
8286335-0	1994	Thiophene derivatives as new mechanism-based inhibitors of cytochromes P-450: inactivation of yeast-expressed human liver cytochrome P-450 2C9 by tienilic acid.	Ticrynafen	146-159	cytochrome P450 family 2 subfamily C member 9	Homo sapiens	122-142	
8286335-1	1994	Oxidation of tienilic acid (TA) by microsomes of yeast expressing two closely related human liver cytochrome P-450s (P450), P450 2C9 and 2C10, led to catalysis-dependent loss of activity of these P450s.	Ticrynafen	13-26	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	117-121	
8286335-1	1994	Oxidation of tienilic acid (TA) by microsomes of yeast expressing two closely related human liver cytochrome P-450s (P450), P450 2C9 and 2C10, led to catalysis-dependent loss of activity of these P450s.	Ticrynafen	13-26	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	124-128	
8286335-1	1994	Oxidation of tienilic acid (TA) by microsomes of yeast expressing two closely related human liver cytochrome P-450s (P450), P450 2C9 and 2C10, led to catalysis-dependent loss of activity of these P450s.	Ticrynafen	28-30	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	117-121	
8286335-1	1994	Oxidation of tienilic acid (TA) by microsomes of yeast expressing two closely related human liver cytochrome P-450s (P450), P450 2C9 and 2C10, led to catalysis-dependent loss of activity of these P450s.	Ticrynafen	28-30	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	124-128	
8286335-3	1994	The loss of P450 activity during TA oxidation was concomitant with product (5-hydroxytienilic acid, 5-OHTA) formation, showed pseudo-first-order and saturation kinetics, and was inhibited by an alternative substrate, tolbutamide.	5-hydroxythienilic acid	76-98	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	12-16	
8286335-3	1994	The loss of P450 activity during TA oxidation was concomitant with product (5-hydroxytienilic acid, 5-OHTA) formation, showed pseudo-first-order and saturation kinetics, and was inhibited by an alternative substrate, tolbutamide.	5-ohta	100-106	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	12-16	
8286335-3	1994	The loss of P450 activity during TA oxidation was concomitant with product (5-hydroxytienilic acid, 5-OHTA) formation, showed pseudo-first-order and saturation kinetics, and was inhibited by an alternative substrate, tolbutamide.	Tolbutamide	217-228	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	12-16	
8286335-8	1994	Moreover, a specific covalent binding of 0.9 mol of TA metabolite per mole of P450 2C10 was found to occur before the complete loss of enzyme activity (in incubations performed in the presence of glutathione).	Glutathione	196-207	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	78-82	
8286335-10	1994	It involves the intermediate formation of an electrophilic thiophene sulfoxide, which may react at position 5 of its thiophene ring either with H2O to give 5-OHTA or with a nucleophilic group of an amino acid residue of the P450 active site, which results in its covalent binding to P450 protein.	thiophene sulfoxide	59-78	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	224-228	
8286335-10	1994	It involves the intermediate formation of an electrophilic thiophene sulfoxide, which may react at position 5 of its thiophene ring either with H2O to give 5-OHTA or with a nucleophilic group of an amino acid residue of the P450 active site, which results in its covalent binding to P450 protein.	thiophene sulfoxide	59-78	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	283-287	
8286335-10	1994	It involves the intermediate formation of an electrophilic thiophene sulfoxide, which may react at position 5 of its thiophene ring either with H2O to give 5-OHTA or with a nucleophilic group of an amino acid residue of the P450 active site, which results in its covalent binding to P450 protein.	Thiophenes	59-68	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	224-228	
8286335-10	1994	It involves the intermediate formation of an electrophilic thiophene sulfoxide, which may react at position 5 of its thiophene ring either with H2O to give 5-OHTA or with a nucleophilic group of an amino acid residue of the P450 active site, which results in its covalent binding to P450 protein.	Thiophenes	59-68	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	283-287	
8286335-10	1994	It involves the intermediate formation of an electrophilic thiophene sulfoxide, which may react at position 5 of its thiophene ring either with H2O to give 5-OHTA or with a nucleophilic group of an amino acid residue of the P450 active site, which results in its covalent binding to P450 protein.	Water	144-147	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	224-228	
8286335-10	1994	It involves the intermediate formation of an electrophilic thiophene sulfoxide, which may react at position 5 of its thiophene ring either with H2O to give 5-OHTA or with a nucleophilic group of an amino acid residue of the P450 active site, which results in its covalent binding to P450 protein.	Water	144-147	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	283-287	
8286335-10	1994	It involves the intermediate formation of an electrophilic thiophene sulfoxide, which may react at position 5 of its thiophene ring either with H2O to give 5-OHTA or with a nucleophilic group of an amino acid residue of the P450 active site, which results in its covalent binding to P450 protein.	5-ohta	156-162	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	224-228	
8286335-10	1994	It involves the intermediate formation of an electrophilic thiophene sulfoxide, which may react at position 5 of its thiophene ring either with H2O to give 5-OHTA or with a nucleophilic group of an amino acid residue of the P450 active site, which results in its covalent binding to P450 protein.	5-ohta	156-162	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	283-287