PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 22226931-6 2012 Glutathione reductase was also inhibited by PQQ but in contrast to the effects of PQQ on TrxR1, its quinone reduction was not further stimulated. quinone 100-107 glutathione-disulfide reductase Homo sapiens 0-21 3028490-4 1987 Glutathione reductase (EC 1.6.4.2) in the presence of NADPH and oxidised glutathione, and dihydrolipoamide dehydrogenase (EC 1.8.1.4) with NADH and lipoamide, are found to accelerate the radical decay by reducing the quinone or semiquinone. quinone 217-224 glutathione-disulfide reductase Homo sapiens 0-21 14604985-5 2004 Compared with other related pyridine nucleotide-disulfide oxidoreductases such as glutathione reductase or trypanothione reductase, the k(ca)(t)/K(m) value for quinone reduction by TrxR was about 1 order of magnitude higher, and it was not directly related to the one-electron reduction potential of the quinones. quinone 160-167 glutathione-disulfide reductase Homo sapiens 82-103 19263098-4 2009 The compounds studied displays a higher affinity in trypanothione reductase (TR) than glutathione reductase (GR), since only two out of 28 quinone compounds presented more favorable docking energy in the site of human enzyme. quinone 139-146 glutathione-disulfide reductase Homo sapiens 86-107 19263098-4 2009 The compounds studied displays a higher affinity in trypanothione reductase (TR) than glutathione reductase (GR), since only two out of 28 quinone compounds presented more favorable docking energy in the site of human enzyme. quinone 139-146 glutathione-disulfide reductase Homo sapiens 109-111