PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
12215223-0	2002	Dihydrolipoic acid as an effective cofactor for peptide methionine sulfoxide reductase in enzymatic repair of oxidative damage to both lipid-free and lipid-bound apolipoprotein a-I.	dihydrolipoic acid	0-18	methionine sulfoxide reductase A	Homo sapiens	48-86	
12215223-2	2002	We show that DHLA acts as an effective cofactor for PMSR, mediating restoration of the native secondary structure, tertiary structure, stability, and lipid-binding properties of the native unoxidized protein.	dihydrolipoic acid	13-17	methionine sulfoxide reductase A	Homo sapiens	52-56	
12215223-1	2002	The aim of this study was to examine the possible use of dihydrolipoic acid (DHLA), the reduced form of lipoic acid, in the reduction of oxidized apolipoprotein A-I mediated by peptide methionine sulfoxide reductase (PMSR), and to test the accessibility of methionine sulfoxides in the lipid-bound oxidized apolipoprotein A-I to this reaction.	dihydrolipoic acid	57-75	methionine sulfoxide reductase A	Homo sapiens	177-215	
12215223-1	2002	The aim of this study was to examine the possible use of dihydrolipoic acid (DHLA), the reduced form of lipoic acid, in the reduction of oxidized apolipoprotein A-I mediated by peptide methionine sulfoxide reductase (PMSR), and to test the accessibility of methionine sulfoxides in the lipid-bound oxidized apolipoprotein A-I to this reaction.	dihydrolipoic acid	57-75	methionine sulfoxide reductase A	Homo sapiens	217-221	
12215223-1	2002	The aim of this study was to examine the possible use of dihydrolipoic acid (DHLA), the reduced form of lipoic acid, in the reduction of oxidized apolipoprotein A-I mediated by peptide methionine sulfoxide reductase (PMSR), and to test the accessibility of methionine sulfoxides in the lipid-bound oxidized apolipoprotein A-I to this reaction.	dihydrolipoic acid	77-81	methionine sulfoxide reductase A	Homo sapiens	177-215	
12215223-1	2002	The aim of this study was to examine the possible use of dihydrolipoic acid (DHLA), the reduced form of lipoic acid, in the reduction of oxidized apolipoprotein A-I mediated by peptide methionine sulfoxide reductase (PMSR), and to test the accessibility of methionine sulfoxides in the lipid-bound oxidized apolipoprotein A-I to this reaction.	dihydrolipoic acid	77-81	methionine sulfoxide reductase A	Homo sapiens	217-221	
9541724-0	1998	Effects of dihydrolipoic acid on peptide methionine sulfoxide reductase.	dihydrolipoic acid	11-29	methionine sulfoxide reductase A	Homo sapiens	33-71	
9541724-6	1998	It is found that DHLA acts as a reducing cofactor for PMSR.	dihydrolipoic acid	17-21	methionine sulfoxide reductase A	Homo sapiens	54-58	
9541724-8	1998	Generally, by stimulating PMSR, DHLA may exert a curative effect in diseases accompanied by oxidative stress.	dihydrolipoic acid	32-36	methionine sulfoxide reductase A	Homo sapiens	26-30