PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 28961169-1 2017 Human thioredoxin (TRX) is a 12-kDa protein with redox-active dithiol in the active site -Cys-Gly-Pro-Cys-, which is induced by biological stress due to oxidative damage, metabolic dysfunction, chemicals, infection/inflammation, irradiation, or hypoxia/ischemia-reperfusion. Glycine 94-97 thioredoxin Homo sapiens 6-17 9143692-4 1997 TRX is a small multifunctional protein that has a redox-active disulfide/dithiol within the conserved active site sequence: Cys-Gly-Pro-Cys. Glycine 128-131 thioredoxin Homo sapiens 0-3 3122752-1 1988 The thioredoxin peptide Trp-Cys-Gly-Pro-Cys-Lys, which contains the redox active dithiol, was found to be reduced by lipoamide in a coupled reaction with lipoamide dehydrogenase and NADH. Glycine 32-35 thioredoxin Homo sapiens 4-15 28961169-1 2017 Human thioredoxin (TRX) is a 12-kDa protein with redox-active dithiol in the active site -Cys-Gly-Pro-Cys-, which is induced by biological stress due to oxidative damage, metabolic dysfunction, chemicals, infection/inflammation, irradiation, or hypoxia/ischemia-reperfusion. Glycine 94-97 thioredoxin Homo sapiens 19-22 24058364-1 2013 Human thioredoxin-1 (TRX) is a 12-kDa protein with redox-active dithiol in the active site -Cys-Gly-Pro-Cys-. Glycine 96-99 thioredoxin Homo sapiens 6-19 28955804-7 2016 Mutation of cysteine-32 but not cysteine-35 in the Trp-Cys32-Gly-Pro-Cys35 motif eliminated the binding of Trx1 with S-sulfhydrated proteins and abolished the S-desulfhydrating effect of Trx1. Glycine 61-64 thioredoxin Homo sapiens 107-111 28955804-7 2016 Mutation of cysteine-32 but not cysteine-35 in the Trp-Cys32-Gly-Pro-Cys35 motif eliminated the binding of Trx1 with S-sulfhydrated proteins and abolished the S-desulfhydrating effect of Trx1. Glycine 61-64 thioredoxin Homo sapiens 187-191 24828203-2 2014 The MALDI-ISD spectra of bovine serum albumin (BSA), myoglobin and thioredoxin show discontinuous intense ion peaks originating from one-side preferential cleavage at the N-Calpha bond of Xxx-Asp, Xxx-Asn, Xxx-Cys and Gly-Xxx residues. Glycine 218-221 thioredoxin Homo sapiens 67-78 24058364-1 2013 Human thioredoxin-1 (TRX) is a 12-kDa protein with redox-active dithiol in the active site -Cys-Gly-Pro-Cys-. Glycine 96-99 thioredoxin Homo sapiens 21-24 19601712-1 2009 Thioredoxin-1 (TRX) is a small (14 kDa) multifunctional protein with the redox-active site Cys-Gly-Pro-Cys. Glycine 95-98 thioredoxin Homo sapiens 0-13 22430737-4 2012 We found that Trx1 is expressed in a redox-active form at the surface of HUVEC and acts as an inhibitor of complement deposition in a manner dependent on its Cys-Gly-Pro-Cys active site. Glycine 162-165 thioredoxin Homo sapiens 14-18 21389620-1 2011 Mammalian thioredoxin reductases (TrxRs) contain selenium as selenocysteine (Sec) in the C-terminal redox center -Gly-Cys-Sec-Gly-OH to reduce Trx and other substrates; a Sec-to-Cys substitution in mammalian TrxR yields an almost inactive enzyme. Glycine 114-117 thioredoxin Homo sapiens 34-37 21389620-1 2011 Mammalian thioredoxin reductases (TrxRs) contain selenium as selenocysteine (Sec) in the C-terminal redox center -Gly-Cys-Sec-Gly-OH to reduce Trx and other substrates; a Sec-to-Cys substitution in mammalian TrxR yields an almost inactive enzyme. Glycine 126-129 thioredoxin Homo sapiens 34-37 20435060-1 2010 Thioredoxin 1 (Trx 1) is a 12-kDa protein with redox-active dithiol in the active site -Cys-Gly-Pro-Cys- that is ubiquitously present in the human body. Glycine 92-95 thioredoxin Homo sapiens 0-13 20435060-1 2010 Thioredoxin 1 (Trx 1) is a 12-kDa protein with redox-active dithiol in the active site -Cys-Gly-Pro-Cys- that is ubiquitously present in the human body. Glycine 92-95 thioredoxin Homo sapiens 15-20 19601712-1 2009 Thioredoxin-1 (TRX) is a small (14 kDa) multifunctional protein with the redox-active site Cys-Gly-Pro-Cys. Glycine 95-98 thioredoxin Homo sapiens 15-18 14604673-1 2003 The thioredoxins are small ubiquitous redox proteins with the conserved redox catalytic sequence-Trp-Cys-Gly-Pro-Cys-Lys, where the Cys residues undergo reversible NADPH dependent reduction by selenocysteine containing flavoprotein thioredoxin reductases. Glycine 105-108 thioredoxin Homo sapiens 4-16 18179361-4 2008 Human thioredoxin 1 (TRX1) is a redox-active protein of approximately 12 kDa that contains a (32)Cys-Gly-Pro-(35)Cys sequence necessary for its activity. Glycine 101-104 thioredoxin Homo sapiens 6-19 18179361-4 2008 Human thioredoxin 1 (TRX1) is a redox-active protein of approximately 12 kDa that contains a (32)Cys-Gly-Pro-(35)Cys sequence necessary for its activity. Glycine 101-104 thioredoxin Homo sapiens 21-25 16513844-3 2006 Here, we show that the heterogenous ribonucleoprotein A18 (hnRNP A18) RNA Binding Domain (RBD) and the arginine, glycine (RGG) rich domain can bind TRX 3"-untranslated region (3"-UTR) independently but both domains are required for maximal binding. Glycine 113-120 thioredoxin Homo sapiens 148-151 14604673-1 2003 The thioredoxins are small ubiquitous redox proteins with the conserved redox catalytic sequence-Trp-Cys-Gly-Pro-Cys-Lys, where the Cys residues undergo reversible NADPH dependent reduction by selenocysteine containing flavoprotein thioredoxin reductases. Glycine 105-108 thioredoxin Homo sapiens 4-15 11726031-3 2001 TRX is a small ubiquitous protein with the redox-active site sequence -Cys-Gly-Pro-Cys-. Glycine 75-78 thioredoxin Homo sapiens 0-3 14569031-2 2003 All known isoenzymes of mammalian thioredoxin (Trx) reductases (TrxRs) employ selenium in the C-terminal redox center -Gly-Cys-Sec-Gly-COOH for reduction of Trx and other substrates, whereas the corresponding sequence in Drosophila melanogaster TrxR is -Ser-Cys-Cys-Ser-COOH. Glycine 119-122 thioredoxin Homo sapiens 34-45 14569031-2 2003 All known isoenzymes of mammalian thioredoxin (Trx) reductases (TrxRs) employ selenium in the C-terminal redox center -Gly-Cys-Sec-Gly-COOH for reduction of Trx and other substrates, whereas the corresponding sequence in Drosophila melanogaster TrxR is -Ser-Cys-Cys-Ser-COOH. Glycine 119-122 thioredoxin Homo sapiens 47-50 14569031-2 2003 All known isoenzymes of mammalian thioredoxin (Trx) reductases (TrxRs) employ selenium in the C-terminal redox center -Gly-Cys-Sec-Gly-COOH for reduction of Trx and other substrates, whereas the corresponding sequence in Drosophila melanogaster TrxR is -Ser-Cys-Cys-Ser-COOH. Glycine 119-122 thioredoxin Homo sapiens 64-67 14569031-2 2003 All known isoenzymes of mammalian thioredoxin (Trx) reductases (TrxRs) employ selenium in the C-terminal redox center -Gly-Cys-Sec-Gly-COOH for reduction of Trx and other substrates, whereas the corresponding sequence in Drosophila melanogaster TrxR is -Ser-Cys-Cys-Ser-COOH. Glycine 131-134 thioredoxin Homo sapiens 34-45 14569031-2 2003 All known isoenzymes of mammalian thioredoxin (Trx) reductases (TrxRs) employ selenium in the C-terminal redox center -Gly-Cys-Sec-Gly-COOH for reduction of Trx and other substrates, whereas the corresponding sequence in Drosophila melanogaster TrxR is -Ser-Cys-Cys-Ser-COOH. Glycine 131-134 thioredoxin Homo sapiens 47-50 14569031-2 2003 All known isoenzymes of mammalian thioredoxin (Trx) reductases (TrxRs) employ selenium in the C-terminal redox center -Gly-Cys-Sec-Gly-COOH for reduction of Trx and other substrates, whereas the corresponding sequence in Drosophila melanogaster TrxR is -Ser-Cys-Cys-Ser-COOH. Glycine 131-134 thioredoxin Homo sapiens 64-67 12677197-1 2002 Thioredoxin (Trx) is a small multifunctional protein with a redox active dithiol/disulfide in the active-site sequence Cys-Gly-Pro-Cys. Glycine 123-126 thioredoxin Homo sapiens 0-11 12677197-1 2002 Thioredoxin (Trx) is a small multifunctional protein with a redox active dithiol/disulfide in the active-site sequence Cys-Gly-Pro-Cys. Glycine 123-126 thioredoxin Homo sapiens 13-16 11509327-3 2001 TRX is a small, ubiquitous protein with two redox-active half-cysteine residues, -Cys-Gly-Pro-Cys, in its active center. Glycine 86-89 thioredoxin Homo sapiens 0-3 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). Glycine 305-308 thioredoxin Homo sapiens 167-178 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). Glycine 323-326 thioredoxin Homo sapiens 167-178 11237106-1 2000 Thioredoxin (TRX) is a 12 kD protein with redox-active dithiol in the active site; -Cys-Gly-Pro-Cys-. Glycine 88-91 thioredoxin Homo sapiens 0-11 11237106-1 2000 Thioredoxin (TRX) is a 12 kD protein with redox-active dithiol in the active site; -Cys-Gly-Pro-Cys-. Glycine 88-91 thioredoxin Homo sapiens 13-16 11035260-1 2000 The thioredoxins are ubiquitous proteins containing a conserved -Trp-Cys-Gly-Pro-Cys-Lys- redox catalytic site. Glycine 73-76 thioredoxin Homo sapiens 4-16 11213485-2 2000 Cytosolic thioredoxin reductase from mammalian cells is a dimeric flavin enzyme comprising a glutathione reductase-like equivalent elongated with 16 residues including the conserved carboxy-terminal sequence, Gly-Cys-SeCys-Gly, where SeCys is selenocysteine. Glycine 209-212 thioredoxin Homo sapiens 10-21 11213485-2 2000 Cytosolic thioredoxin reductase from mammalian cells is a dimeric flavin enzyme comprising a glutathione reductase-like equivalent elongated with 16 residues including the conserved carboxy-terminal sequence, Gly-Cys-SeCys-Gly, where SeCys is selenocysteine. Glycine 223-226 thioredoxin Homo sapiens 10-21