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