PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
7744824-0	1995	Human thioredoxin reductase directly reduces lipid hydroperoxides by NADPH and selenocystine strongly stimulates the reaction via catalytically generated selenols.	Lipid Peroxides	45-65	thioredoxin	Homo sapiens	6-17	
11006259-1	2000	PURPOSE: To investigate whether lipid peroxides play a role in retinal cell death due to ischemia-reperfusion injury, whether recombinant human thioredoxin (rhTRX) treatment reduces production of lipid peroxides of the retina, and whether such treatment reduces the number of cells expressing c-Jun and cyclin D1.	Lipid Peroxides	196-211	thioredoxin	Homo sapiens	144-155	
11213474-5	2000	The TRX levels were significantly correlated with serum lipid peroxide levels and indocyanine green exclusion test values, and were markedly decreased following treatment with Stronger Neo-Minophagen C or ursodeoxycholic acid.	Lipid Peroxides	56-70	thioredoxin	Homo sapiens	4-7	
7785012-12	1995	Lipid peroxide, superoxide dismutase, and glutathione peroxide levels in the control group were higher than in the hTRX group and in the non-ischaemic groups.	Lipid Peroxides	0-14	thioredoxin	Homo sapiens	115-119	
16343416-7	2006	Taken together, these results suggested that HSA has a capability to reduce lipid hydroperoxide with the use of Trx as an in vivo electron donor, and that the redox-active disulfide between Cys392 and Cys438 acts as a primary site of the catalysis for the Trx-linked lipid peroxidase activity.	Lipid Peroxides	76-95	thioredoxin	Homo sapiens	112-115	
20513473-2	2010	Hydrogen peroxide, peroxynitrite, or lipid hydroperoxides are all able to oxidize cysteines to form cysteine sulfenic acids; this reactive intermediate can be directly reduced to thiol by cellular reductants such as thioredoxin or further participate in disulfide bond formation with glutathione or cysteine residues in the same or another protein.	Lipid Peroxides	37-57	thioredoxin	Homo sapiens	216-227	
19406206-6	2009	A selenazol drug like ebselen is a direct substrate for mammalian TrxR and dithiol Trx and ebselen selenol is readily reoxidized by hydrogen peroxide and lipid hydroperoxides, acting as an anti-oxidant and anti-inflammatory drug.	Lipid Peroxides	154-174	thioredoxin	Homo sapiens	66-69	
19216714-3	2008	NADPH-dependent thioredoxin reductase, which reduces a broad range of substrates including oxidized form of thioredoxin, can also directly reduce lipid hydroperoxides, H2O2, and dehydroascorbic and lipoic acids.	Lipid Peroxides	146-166	thioredoxin	Homo sapiens	16-27	
19216714-3	2008	NADPH-dependent thioredoxin reductase, which reduces a broad range of substrates including oxidized form of thioredoxin, can also directly reduce lipid hydroperoxides, H2O2, and dehydroascorbic and lipoic acids.	Lipid Peroxides	146-166	thioredoxin	Homo sapiens	108-119	
15556050-8	2004	Trx elevation correlated well with increased oxidative stress (lipid peroxides, P<0.0001), circulatory P-selectin (P<0.0001), morning level of free salivary cortisol (P=0.0002), and serum creatinine (P=0.0417), but not with pro-inflammatory cytokines TNF and IL-6.	Lipid Peroxides	63-78	thioredoxin	Homo sapiens	0-3	
11165879-5	2001	In the presence of palmitoyl coenzyme A (palmitoyl-CoA) however, HSA used Trx as an electron donor to the reduction of lipid hydroperoxide.	Lipid Peroxides	119-138	thioredoxin	Homo sapiens	74-77	
11165879-8	2001	Together, these data suggest that palmitoyl-CoA-bound HSA has a capability to remove lipid peroxide with the use of electrons given by Trx system.	Lipid Peroxides	85-99	thioredoxin	Homo sapiens	135-138