PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28594389-3	2017	Thioredoxin 2 (TRX2) is a key mitochondrial redox protein that maintains normal protein function and also provides electrons to peroxiredoxin 3 (PRX3) to scavenge H2O2 in mitochondria.	Hydrogen Peroxide	163-167	thioredoxin 2	Homo sapiens	0-13	
29701186-9	2018	Compared with the control group, the expression of Trx-2 protein in the 20, 50 or 100 mumol/L H2O2 groups was decreased (all P<0.05).	Hydrogen Peroxide	94-98	thioredoxin 2	Homo sapiens	51-56	
29701186-10	2018	Compared with the control group, the cell survival rates were decreased in the 100 mumol/L H2O2 group and the negative control group (both P<0.05), along with enhanced apoptotic rates, inhibited cellular SOD activities and CAT activities, reduced GSH contents, augmented MDA contents, down-regulated Trx-2 and Bcl-2 expression and up-regulated Bax and caspase-3 expression (all P<0.05).	Hydrogen Peroxide	91-95	thioredoxin 2	Homo sapiens	303-308	
29701186-13	2018	The overexpression of Trx-2 obviously attenuated H2O2-induced injury of human lens epithelial cells, which might be associated with the inhibition of H2O2-mediated oxidative stress.	Hydrogen Peroxide	49-53	thioredoxin 2	Homo sapiens	22-27	
29701186-13	2018	The overexpression of Trx-2 obviously attenuated H2O2-induced injury of human lens epithelial cells, which might be associated with the inhibition of H2O2-mediated oxidative stress.	Hydrogen Peroxide	150-154	thioredoxin 2	Homo sapiens	22-27	
28594389-3	2017	Thioredoxin 2 (TRX2) is a key mitochondrial redox protein that maintains normal protein function and also provides electrons to peroxiredoxin 3 (PRX3) to scavenge H2O2 in mitochondria.	Hydrogen Peroxide	163-167	thioredoxin 2	Homo sapiens	15-19	
19216714-2	2008	The thioredoxin isoforms Trx1 (cytoplasmic form) and Trx2 (mitochondrial form) can reduce inter- and intramolecular disulfide bonds in proteins, in particular, in oxidized peroxiredoxins, which disrupt organic hydroperoxides, H2O2, and peroxynitrite.	Hydrogen Peroxide	210-224	thioredoxin 2	Homo sapiens	53-57	
19506101-8	2009	Elevated vascular superoxide and hydrogen peroxide levels, as well as expression of NADPH oxidase subunits in response to angiotensin II infusion, were significantly attenuated in Tg(hTrx2) mice.	Hydrogen Peroxide	33-50	thioredoxin 2	Homo sapiens	183-188	
19216714-2	2008	The thioredoxin isoforms Trx1 (cytoplasmic form) and Trx2 (mitochondrial form) can reduce inter- and intramolecular disulfide bonds in proteins, in particular, in oxidized peroxiredoxins, which disrupt organic hydroperoxides, H2O2, and peroxynitrite.	Hydrogen Peroxide	226-230	thioredoxin 2	Homo sapiens	53-57	
11213484-5	2000	A function of the mitochondrial thioredoxin system is as electron donor for a mitochondrial peroxiredoxin, an enzyme that detoxifies the hydrogen peroxide generated by the mitochondrial metabolism.	Hydrogen Peroxide	137-154	thioredoxin 2	Homo sapiens	18-43	
12705894-6	2003	These results suggest that TrxR2 participates in the regulation of protein tyrosine phosphorylation and cell growth as a component of the mitochondria specific H2O2-eliminating system that includes peroxiredoxin III and thioredoxin 2.	Hydrogen Peroxide	160-164	thioredoxin 2	Homo sapiens	220-233