| Literature DB >> 28048978 |
Kazutaka Araki1, Ryo Ushioda2, Hidewo Kusano3, Riko Tanaka3, Tomohisa Hatta4, Kazuhiko Fukui3, Kazuhiro Nagata2, Tohru Natsume5.
Abstract
Thiol-based redox control is among the most important mechanisms for maintaining cellular redox homeostasis, with essential participation of cysteine thiols of oxidoreductases. To explore cellular redox regulatory networks, direct interactions among active cysteine thiols of oxidoreductases and their targets must be clarified. We applied a recently described thiol-ene crosslinking-based strategy, named divinyl sulfone (DVSF) method, enabling identification of new potential redox relay partners of the cytosolic oxidoreductases thioredoxin (TXN) and thioredoxin domain containing 17 (TXNDC17). Applying multiple methods, including classical substrate-trapping techniques, will increase understanding of redox regulatory mechanisms in cells.Entities:
Keywords: Interaction; Oxidoreductase; Proteomics; Redox; Thioredoxin
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Year: 2016 PMID: 28048978 DOI: 10.1016/j.ab.2016.12.025
Source DB: PubMed Journal: Anal Biochem ISSN: 0003-2697 Impact factor: 3.365