PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11328605-2	2001	The two cysteines in the N-terminal FAD domain (-Cys59-x-x-x-x-Cys64-) and histidine (His472) are conserved between them at corresponding positions, but the mammalian thioredoxin reductase contains a C-terminal extension of selenocysteine (Sec or U) at the penultimate position and a preceding cysteine (-Gly-Cys497-Sec498-Gly).	Flavin-Adenine Dinucleotide	36-39	thioredoxin	Homo sapiens	167-178	
11328605-9	2001	These data and spectral analyses of these enzymes suggest that Cys59 and Cys64 at the N-terminus, in conjunction with His472, function as primary acceptors for electrons from NADPH via FAD, and that the electrons are then transferred to Cys497-Sec498 at the C-terminus for the reduction of oxidized thioredoxin in the mammalian thioredoxin reductase.	Flavin-Adenine Dinucleotide	185-188	thioredoxin	Homo sapiens	299-310	
11328605-9	2001	These data and spectral analyses of these enzymes suggest that Cys59 and Cys64 at the N-terminus, in conjunction with His472, function as primary acceptors for electrons from NADPH via FAD, and that the electrons are then transferred to Cys497-Sec498 at the C-terminus for the reduction of oxidized thioredoxin in the mammalian thioredoxin reductase.	Flavin-Adenine Dinucleotide	185-188	thioredoxin	Homo sapiens	328-339	
11012663-1	2000	Human cytosolic thioredoxin reductase (TrxR), a homodimeric protein containing 1 selenocysteine and 1 FAD per subunit of 55 kDa, catalyses the NADPH-dependent reduction of thioredoxin disulfide and of numerous other oxidized cell constituents.	Flavin-Adenine Dinucleotide	102-105	thioredoxin	Homo sapiens	16-27	
7876079-2	1995	Human thioredoxin reductase is a dimeric enzyme that catalyzes reduction of the disulfide in oxidized thioredoxin by a mechanism involving transfer of electrons from NADPH via FAD to a redox-active disulfide.	Flavin-Adenine Dinucleotide	176-179	thioredoxin	Homo sapiens	6-17	
7876079-2	1995	Human thioredoxin reductase is a dimeric enzyme that catalyzes reduction of the disulfide in oxidized thioredoxin by a mechanism involving transfer of electrons from NADPH via FAD to a redox-active disulfide.	Flavin-Adenine Dinucleotide	176-179	thioredoxin	Homo sapiens	102-113	
8577704-7	1996	The selenoprotein contains FAD as a prosthetic group and catalyzes NADPH-dependent reduction of 5,5"-dithiobis(2-nitrobenzoic acid) (DTNB), and reduction of insulin in the presence of thioredoxin (Trx).	Flavin-Adenine Dinucleotide	27-30	thioredoxin	Homo sapiens	184-195	
8577704-7	1996	The selenoprotein contains FAD as a prosthetic group and catalyzes NADPH-dependent reduction of 5,5"-dithiobis(2-nitrobenzoic acid) (DTNB), and reduction of insulin in the presence of thioredoxin (Trx).	Flavin-Adenine Dinucleotide	27-30	thioredoxin	Homo sapiens	197-200