PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
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	
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	
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