PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10333487-1	1999	Mammalian thioredoxin reductase (TR) is a flavoprotein catalysing reduction of oxidized thioredoxin in an NADPH-dependent manner, and contains a selenocysteine (Sec) residue near the C-terminus.	NADP	106-111	peroxiredoxin 5	Rattus norvegicus	10-31	
10333487-1	1999	Mammalian thioredoxin reductase (TR) is a flavoprotein catalysing reduction of oxidized thioredoxin in an NADPH-dependent manner, and contains a selenocysteine (Sec) residue near the C-terminus.	NADP	106-111	peroxiredoxin 5	Rattus norvegicus	33-35	
10333487-1	1999	Mammalian thioredoxin reductase (TR) is a flavoprotein catalysing reduction of oxidized thioredoxin in an NADPH-dependent manner, and contains a selenocysteine (Sec) residue near the C-terminus.	NADP	106-111	thioredoxin 1	Rattus norvegicus	10-21	
10333487-2	1999	We observed that TR activity was decreased in A549 cells by the lowering of the fetal bovine serum content in the culture medium and was recovered by the addition of selenium.	Selenium	166-174	peroxiredoxin 5	Rattus norvegicus	17-19	
10333487-4	1999	TR activities in COS-1 cells expressing rat TR were increased in accordance with supplemented sodium selenite concentrations, whereas levels of TR protein, examined by Western blotting, were not affected by sodium selenite concentrations.	Sodium Selenite	94-109	peroxiredoxin 5	Rattus norvegicus	0-2	
10333487-4	1999	TR activities in COS-1 cells expressing rat TR were increased in accordance with supplemented sodium selenite concentrations, whereas levels of TR protein, examined by Western blotting, were not affected by sodium selenite concentrations.	Sodium Selenite	94-109	peroxiredoxin 5	Rattus norvegicus	44-46	
10333487-9	1999	These data clearly showed a requirement of selenium for the formation of functional TR protein.	Selenium	43-51	peroxiredoxin 5	Rattus norvegicus	84-86