PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
31590044-5	2020	Here, we report data on the interaction of p-benzoquinone (BQ) with the selenoprotein thioredoxin reductase-1 (TrxR1), which exposes an accessible Sec residue upon physiological reduction by NADPH.	quinone	43-57	2,4-dienoyl CoA reductase 1, mitochondrial	Mus musculus	191-196	
6316886-3	1983	A new hypothesis for oestrogen action at the molecular level is that the phenolic moiety of an oestrogen is oxidized to the corresponding quinone methide which is rapidly reduced with, say, NADPH to regenerate the oestrogen; the feedback from the rapid consumption of oxidant and/or reductant in the target organs might be responsible for the local increase in RNA synthesis, and its consequent phenomena.	quinone	138-145	2,4-dienoyl CoA reductase 1, mitochondrial	Mus musculus	190-195	
31590044-5	2020	Here, we report data on the interaction of p-benzoquinone (BQ) with the selenoprotein thioredoxin reductase-1 (TrxR1), which exposes an accessible Sec residue upon physiological reduction by NADPH.	quinone	59-61	2,4-dienoyl CoA reductase 1, mitochondrial	Mus musculus	191-196	
31590044-6	2020	Our results reveal that BQ targets NADPH-reduced TrxR1 and inhibits its activity using 5,5"-dithiobis(2-nitrobenzoic acid) or juglone as model substrates, consistent with the targeting of both the Cys and Sec residues of TrxR1.	quinone	24-26	2,4-dienoyl CoA reductase 1, mitochondrial	Mus musculus	35-40	
31590044-9	2020	Addition of NADPH after BQ pre-treatment could resolve the disulfide-linked crosslinking.	quinone	24-26	2,4-dienoyl CoA reductase 1, mitochondrial	Mus musculus	12-17