PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
15322091-12	2004	We provide evidence that p22phox directly interacts with Nox1 and Nox4, to form an superoxide-generating NADPH oxidase and demonstrate that mutation of the potential heme binding site in the Nox proteins disrupts the complex formation of Nox1 and Nox4 with p22phox.	Heme	166-170	cytochrome b-245 alpha chain	Homo sapiens	25-32	
24573492-2	2014	The C242T polymorphism at the p22PHOX gene affects binding of p22PHOX to heme, leading to variants of NADPH oxidase that produce different levels of reactive oxygen species (ROS).	Heme	73-77	cytochrome b-245 alpha chain	Homo sapiens	30-37	
24573492-2	2014	The C242T polymorphism at the p22PHOX gene affects binding of p22PHOX to heme, leading to variants of NADPH oxidase that produce different levels of reactive oxygen species (ROS).	Heme	73-77	cytochrome b-245 alpha chain	Homo sapiens	62-69	
19567155-3	2009	The p22phox subunit is polymorphic with a C242T variant that changes histidine-72 for a tyrosine in the potential heme binding site.	Heme	114-118	cytochrome b-245 alpha chain	Homo sapiens	4-11	
19251588-5	2009	Incubating HAECs with LPS also significantly increased cellular iron and heme levels and mRNA and protein levels of p22phox, a heme-containing, catalytic subunit of NADPH oxidase.	Heme	127-131	cytochrome b-245 alpha chain	Homo sapiens	116-123	
15322091-12	2004	We provide evidence that p22phox directly interacts with Nox1 and Nox4, to form an superoxide-generating NADPH oxidase and demonstrate that mutation of the potential heme binding site in the Nox proteins disrupts the complex formation of Nox1 and Nox4 with p22phox.	Heme	166-170	cytochrome b-245 alpha chain	Homo sapiens	257-264	
10440830-3	1999	The C242T polymorphism, located in the potential heme-binding site of the p22phox gene, has recently been reported to confer a protective effect on CAD risk in a Japanese study population.	Heme	49-53	cytochrome b-245 alpha chain	Homo sapiens	74-81