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    Home > Biochemistry News > Biotechnology News > Thioredoxin and Redox Regulation of the Nuclear Receptor

    Thioredoxin and Redox Regulation of the Nuclear Receptor

    • Last Update: 2020-11-29
    • Source: Internet
    • Author: User
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    Oxidative stress evokes various cellular responses including alteration of gene expression to preserve cellular homeostasis (
    1
    ,
    2
    ). Thioredoxin (TRX) is a small ubiquitous protein with protein thiol-reducing activity and has been shown to function as a cellular antioxidant buffering system in response to oxidative stress and play essential roles in maintenance of cellular function (
    3
    ,
    4
    ). Recently, a growing number of evidence has shown that TRX plays crucial roles in redox regulation of gene expression via either direct or indirect interaction with various transcription factors including NF-κB (
    5
    ), AP-1 (
    6
    ), and PEBP2 (
    7
    ). Alteration in expression and/or subcellular localization of TRX has been indicated to be involved in such redox-dependent control of the transcription factors (
    8
    ,
    9
    ), however, precise mechanisms remain unknown.
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