PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
31172473-2	2019	DUOX activator proteins (DUOXA1 and DUOXA2), that form covalent complexes with DUOX; both chains together represent the mature catalytic unit that functions as a dedicated hydrogen peroxide-generating enzyme.	Hydrogen Peroxide	172-189	dual oxidase maturation factor 2	Homo sapiens	36-42	
31513783-0	2019	The Dual Oxidase Duox2 stabilized with DuoxA2 in an enzymatic complex at the surface of the cell produces extracellular H2O2 able to induce DNA damage in an inducible cellular model.	Hydrogen Peroxide	120-124	dual oxidase maturation factor 2	Homo sapiens	39-45	
31513783-6	2019	By normalizing H2O2 extracellular production by Duox or DuoxA membrane expression, we have demonstrated that the most active enzymatic complex is Duox2/DuoxA2, compared to Duox1/DuoxA1.	Hydrogen Peroxide	15-19	dual oxidase maturation factor 2	Homo sapiens	152-158	
31513783-10	2019	The present data demonstrate for the first time that H2O2 produced by the Duox2/DuoxA2 cell surface enzymatic complex could provoke potential mutagenic DNA damage in an inducible cellular model, and highlight the importance of the co-expressed partner in the activity and stability of Duox/DuoxA complexes.	Hydrogen Peroxide	53-57	dual oxidase maturation factor 2	Homo sapiens	80-86	
25675383-2	2015	Genetic defects in DUOXA2 lead to an impairment of the H2O2-generating system, in turn causing congenital hypothyroidism (CH) with goiter.	Hydrogen Peroxide	55-59	dual oxidase maturation factor 2	Homo sapiens	19-25	
29272487-1	2017	Background: DUOX2 and DUOXA2 form the predominant H2O2-producing system in human colorectal mucosa.	Hydrogen Peroxide	50-54	dual oxidase maturation factor 2	Homo sapiens	22-28	
25761904-3	2015	DUOX2 forms with its maturation factor, DUOX activator 2 (DUOXA2), a stable complex at the cell surface that is crucial for the H2O2-generating activity, but the nature of their interaction is unknown.	Hydrogen Peroxide	128-132	dual oxidase maturation factor 2	Homo sapiens	40-56	
25761904-3	2015	DUOX2 forms with its maturation factor, DUOX activator 2 (DUOXA2), a stable complex at the cell surface that is crucial for the H2O2-generating activity, but the nature of their interaction is unknown.	Hydrogen Peroxide	128-132	dual oxidase maturation factor 2	Homo sapiens	58-64	
25675383-8	2015	CONCLUSIONS: We identified a novel DUOXA2 mutation (I26M) causing CH with goiter, which affected H2O2 generation but did not alter the protein expression levels, further confirming the essential role of DUOXA2 in thyroid hormone synthesis.	Hydrogen Peroxide	97-101	dual oxidase maturation factor 2	Homo sapiens	35-41	
23404134-3	2013	The main enzymes composing the H2O2-generating system are the dual oxidase 2 (DUOX2) and the recently described DUOX maturation factor 2 (DUOXA2).	Hydrogen Peroxide	31-35	dual oxidase maturation factor 2	Homo sapiens	112-136	
24492313-4	2014	RESULTS: DUOX2 with maturation partner DUOXA2 forms the predominant system for H2O2 production in human colon and is upregulated in active colitis.	Hydrogen Peroxide	79-83	dual oxidase maturation factor 2	Homo sapiens	39-45	
23404134-3	2013	The main enzymes composing the H2O2-generating system are the dual oxidase 2 (DUOX2) and the recently described DUOX maturation factor 2 (DUOXA2).	Hydrogen Peroxide	31-35	dual oxidase maturation factor 2	Homo sapiens	138-144	
21321110-4	2011	Furthermore, increased Duox2/DuoxA2 expression was closely associated with a significant increase in the production of both intracellular reactive oxygen species and extracellular H2O2.	Hydrogen Peroxide	180-184	dual oxidase maturation factor 2	Homo sapiens	29-35	
20122987-3	2010	The primary enzyme feeding H(2)O(2) to thyroid peroxidase is a heterodimeric NADPH oxidase complex of dual oxidase 2 (DUOX2) and DUOX maturation factor 2 (DUOXA2) at the apical plasma membrane.	Hydrogen Peroxide	27-35	dual oxidase maturation factor 2	Homo sapiens	129-153	
20122987-3	2010	The primary enzyme feeding H(2)O(2) to thyroid peroxidase is a heterodimeric NADPH oxidase complex of dual oxidase 2 (DUOX2) and DUOX maturation factor 2 (DUOXA2) at the apical plasma membrane.	Hydrogen Peroxide	27-35	dual oxidase maturation factor 2	Homo sapiens	155-161	
19074510-8	2009	Duox1/Duoxa1alpha and Duox2/Duoxa2 pairs produce the highest levels of hydrogen peroxide, as they undergo Golgi-based carbohydrate modifications and form stable cell surface complexes.	Hydrogen Peroxide	71-88	dual oxidase maturation factor 2	Homo sapiens	28-34	
20407074-12	2010	Mutation of either DUOX2 or DUOXA2 gene is a newly recognized cause of hypothyroidism due to insufficient H(2)O(2) production.	Hydrogen Peroxide	106-114	dual oxidase maturation factor 2	Homo sapiens	28-34