Identification of thioredoxin target disulfides in proteins released from barley aleurone layers

Journal of Proteomics
Per HägglundBirte Svensson

Abstract

Thioredoxins are ubiquitous disulfide reductases involved in a wide range of cellular processes including DNA synthesis, oxidative stress response and apoptosis. In cereal seeds thioredoxins are proposed to facilitate the germination process by reducing disulfide bonds in storage proteins and other targets in the starchy endosperm. Here we have applied a thiol-specific labeling approach to identify specific disulfide targets of barley thioredoxin in proteins released from barley aleurone layers incubated in buffer containing gibberellic acid.

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Citations

Dec 6, 2012·International Journal of Plant Genomics·Cosette AbdallahKjell Sergeant
Apr 9, 2013·Plant Physiology and Biochemistry : PPB·Hongxiang GuoJun Yin
Jun 26, 2012·FEBS Letters·Johanne Mørch JensenBirte Svensson
Feb 16, 2016·Biochimica Et Biophysica Acta·Per HägglundBirte Svensson
Dec 8, 2010·Phytochemistry·Christine FinnieKlaus D Grasser
Jan 20, 2011·Proteomics·Laurence V Bindschedler, Rainer Cramer
May 1, 2015·Frontiers in Plant Science·Junjie HuNatalia V Bykova
Oct 28, 2018·The Protein Journal·Benjamin Yii Chung LauUmi Salamah Ramli
Nov 1, 2017·Journal of Agricultural and Food Chemistry·Anne N MurmannMarianne N Lund

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