PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
22511118-4	2012	Binding studies with purified CYP1B1 suggests that TMS interferes in the proximity of the heme region of CYP1B1 with high affinity.	Heme	90-94	cytochrome P450 family 1 subfamily B member 1	Homo sapiens	30-36	
22511118-4	2012	Binding studies with purified CYP1B1 suggests that TMS interferes in the proximity of the heme region of CYP1B1 with high affinity.	Heme	90-94	cytochrome P450 family 1 subfamily B member 1	Homo sapiens	105-111	
17159775-5	2006	RESULTS: The capabilities of the most efficient CYP enzymes oxidizing Sudan I, human and rat recombinant CYP1A1, as well as of human recombinant CYP1A2, 2A6 and 3A4 were significantly increased by b(5), while reactions catalyzed by human CYP1B1, 2C8, 2C9 and 2E1 were insensitive to this heme protein.	Heme	288-292	cytochrome P450 family 1 subfamily B member 1	Homo sapiens	238-244	
31746392-3	2020	As a heme-thiolate monooxygenase, cytochrome P450 family 1 subfamily B member 1 (CYP1B1) is able to metabolize arachidonic acid into hydroxyeicosatetraenoic acids, which are thought to serve a central function in the pathophysiology of the cardiovascular system.	Heme	5-18	cytochrome P450 family 1 subfamily B member 1	Homo sapiens	34-79	
31746392-3	2020	As a heme-thiolate monooxygenase, cytochrome P450 family 1 subfamily B member 1 (CYP1B1) is able to metabolize arachidonic acid into hydroxyeicosatetraenoic acids, which are thought to serve a central function in the pathophysiology of the cardiovascular system.	Heme	5-18	cytochrome P450 family 1 subfamily B member 1	Homo sapiens	81-87	
12732455-3	2003	In general, it appears that the CYP1B1 model is consistent with known substrate selectivity for the enzyme, and the sites of metabolism can be rationalized in terms of specific contacts with key amino acid residues within the CYP1B1 heme locus.	Heme	233-237	cytochrome P450 family 1 subfamily B member 1	Homo sapiens	32-38	
12732455-3	2003	In general, it appears that the CYP1B1 model is consistent with known substrate selectivity for the enzyme, and the sites of metabolism can be rationalized in terms of specific contacts with key amino acid residues within the CYP1B1 heme locus.	Heme	233-237	cytochrome P450 family 1 subfamily B member 1	Homo sapiens	226-232	
11854143-8	2002	These results indicate a post-transcriptional inhibitory effect of arsenite on the expression of CYP1A1 and CYP1B1 in T-47D cells, possibly resulting from reduced heme availability.	Heme	163-167	cytochrome P450 family 1 subfamily B member 1	Homo sapiens	108-114	
10781890-9	2000	The expression proved to be highly dependent upon this heme precursor, with levels of CYP1B1 increasing approximately 20-fold, to 920 nmol/l in the presence of up to 2.5 mM ALA.	Heme	55-59	cytochrome P450 family 1 subfamily B member 1	Homo sapiens	86-92	
10781890-11	2000	It could be shown that although heme synthesis was not limiting (CYP101 holoenzyme expression in the absence of ALA was four times higher than the ALA-supported CYP1B1 holoenzyme expression), it was necessary for optimal expression of CYP1B1.	Heme	32-36	cytochrome P450 family 1 subfamily B member 1	Homo sapiens	235-241	
10781890-12	2000	CYP1B1 protein synthesis appears to be coupled to heme precursor availability, as seen by SDS-PAGE, because in the absence of heme precursor apocytochrome P450 1B1 does not accumulate.	Heme	50-54	cytochrome P450 family 1 subfamily B member 1	Homo sapiens	0-6