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Anal Biochem. 2017 Mar 1;520:22-26. doi: 10.1016/j.ab.2016.12.025. Epub 2016 Dec 31.

A crosslinker-based identification of redox relay targets.

Author information

1
Molecular Profiling Research Center for Drug Discovery, National Institute of Advanced Industrial Science and Technology, Tokyo 135-0064, Japan. Electronic address: k-araki@aist.go.jp.
2
Faculty of Life Sciences, Kyoto Sangyo University, Kita-Ku, Kyoto 603-8555, Japan.
3
Molecular Profiling Research Center for Drug Discovery, National Institute of Advanced Industrial Science and Technology, Tokyo 135-0064, Japan.
4
Robotic Biology Institute, Inc., Tokyo 135-0064, Japan.
5
Molecular Profiling Research Center for Drug Discovery, National Institute of Advanced Industrial Science and Technology, Tokyo 135-0064, Japan; Robotic Biology Institute, Inc., Tokyo 135-0064, Japan.

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.

KEYWORDS:

Interaction; Oxidoreductase; Proteomics; Redox; Thioredoxin

PMID:
28048978
DOI:
10.1016/j.ab.2016.12.025
[Indexed for MEDLINE]

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