Cytosolic Triosephosphate Isomerase from Arabidopsis thaliana Is Reversibly Modified by Glutathione on Cysteines 127 and 218-Reference-Cited by-同舟云学术

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Cytosolic Triosephosphate Isomerase from Arabidopsis thaliana Is Reversibly Modified by Glutathione on Cysteines 127 and 218

Published:2016-12-22 Issue: Volume:7 Page:
ISSN:1664-462X
Container-title:Frontiers in Plant Science
language:
Short-container-title:Front. Plant Sci.

Author:

Dumont Sébastien,Bykova Natalia V.,Pelletier Guillaume,Dorion Sonia,Rivoal Jean

Funder

Natural Sciences and Engineering Research Council of Canada

Agriculture and Agri-Food Canada

Publisher

Frontiers Media SA

Subject

Plant Science

Reference70 articles.

1. Reactive oxygen species: metabolism, oxidative stress, and signal transduction.;Apel;Annu. Rev. Plant Biol.,2004

2. Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5 Å resolution: using amino acid sequence data.;Banner;Nature,1975

3. Regulation of PTP1B via glutathionylation of the active site cysteine 215.;Barrett;Biochemistry,1999

4. Glutathionylation of cytosolic glyceraldehyde-3-phosphate dehydrogenase from the model plant Arabidopsis thaliana is reversed by both glutaredoxins and thioredoxins in vitro.;Bedhomme;Biochem. J.,2012

5. Glutaredoxin AtGRXC2 catalyses inhibitory glutathionylation of Arabidopsis BRI1-associated receptor-like kinase 1 (BAK1) in vitro.;Bender;Biochem. J.,2015

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