PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28918898-5	2017	Increased ER glutathione import triggers H2O2-dependent Bip oxidation through Ero1 reductive activation, which inhibits glutathione import in a negative regulatory loop.	Hydrogen Peroxide	41-45	ER oxidoreductin	Saccharomyces cerevisiae S288C	78-82	
20486761-3	2010	To maintain an oxidized state, Ero1 couples disulfide transfer to PDI with reduction of molecular oxygen, forming hydrogen peroxide.	Hydrogen Peroxide	114-131	ER oxidoreductin	Saccharomyces cerevisiae S288C	31-35	
19129474-4	2009	Overexpression of the ER oxidoreductase Ero1p known to generate hydrogen peroxide in vitro, did not lead to increased superoxide levels in cells subjected to ER stress.	Hydrogen Peroxide	64-81	ER oxidoreductin	Saccharomyces cerevisiae S288C	40-45	
25651816-0	2015	ERO1: A protein disulfide oxidase and H2O2 producer.	Hydrogen Peroxide	38-42	ER oxidoreductin	Saccharomyces cerevisiae S288C	0-4	
25651816-2	2015	During this process, protein disulfide isomerase (PDI) chaperones oxidatively fold their client proteins before endoplasmic reticulum oxireductin 1 (ERO1) oxidase transfers electrons from the reduced PDI to the terminal acceptor, which is usually molecular oxygen and is subsequently reduced to H2O2.	Hydrogen Peroxide	295-299	ER oxidoreductin	Saccharomyces cerevisiae S288C	112-147	
25651816-2	2015	During this process, protein disulfide isomerase (PDI) chaperones oxidatively fold their client proteins before endoplasmic reticulum oxireductin 1 (ERO1) oxidase transfers electrons from the reduced PDI to the terminal acceptor, which is usually molecular oxygen and is subsequently reduced to H2O2.	Hydrogen Peroxide	295-299	ER oxidoreductin	Saccharomyces cerevisiae S288C	149-153	
25651816-6	2015	As the oxidative activity of ERO1 is related to the production of H2O2 and consequently burdens cells with potentially toxic reactive oxygen species, deregulated ERO1 activity is likely to impair cell fitness under certain conditions of severe ER stress and may therefore lead to a change from an adaptive to a maladaptive UPR.	Hydrogen Peroxide	66-70	ER oxidoreductin	Saccharomyces cerevisiae S288C	29-33	
25651816-6	2015	As the oxidative activity of ERO1 is related to the production of H2O2 and consequently burdens cells with potentially toxic reactive oxygen species, deregulated ERO1 activity is likely to impair cell fitness under certain conditions of severe ER stress and may therefore lead to a change from an adaptive to a maladaptive UPR.	Hydrogen Peroxide	66-70	ER oxidoreductin	Saccharomyces cerevisiae S288C	162-166	
25651816-7	2015	This review summarizes the evidence of the double-edged sword activity of ERO1 by highlighting its role as a protein disulfide oxidase and H2O2 producer.	Hydrogen Peroxide	139-143	ER oxidoreductin	Saccharomyces cerevisiae S288C	74-78	
21145486-8	2010	These observations implicate ER-localized PRDX4 in a previously unanticipated, parallel, ERO1-independent pathway that couples hydroperoxide production to oxidative protein folding in mammalian cells.	Hydrogen Peroxide	127-140	ER oxidoreductin	Saccharomyces cerevisiae S288C	89-93	
16407158-5	2006	Under aerobic conditions, reduction of molecular oxygen by Ero1p yielded stoichiometric hydrogen peroxide.	Hydrogen Peroxide	88-105	ER oxidoreductin	Saccharomyces cerevisiae S288C	59-64