Posttranslational Modification of Cysteine in Redox Signaling and Oxidative Stress: Focus on S-Glutathionylation-Reference-Cited by-同舟云学术

Posttranslational Modification of Cysteine in Redox Signaling and Oxidative Stress: Focus on S-Glutathionylation

Published:2012-03-15 Issue:6 Volume:16 Page:471-475
ISSN:1523-0864
Container-title:Antioxidants & Redox Signaling
language:en
Short-container-title:Antioxidants & Redox Signaling

Author:

Mieyal John J.¹²,Chock P. Boon³

Affiliation:

1. Department of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, Ohio.

2. Louis B. Stokes Veterans Affairs Medical Research Center, Cleveland, Ohio.

3. Laboratory of Biochemistry, BBC, NHLBI, National Institutes of Health, Bethesda, Maryland.

Publisher

Mary Ann Liebert Inc

Subject

Cell Biology,Clinical Biochemistry,Molecular Biology,Physiology,Biochemistry,Cell Biology,Clinical Biochemistry,Molecular Biology,Physiology,Biochemistry

Link

http://www.liebertpub.com/doi/pdf/10.1089/ars.2011.4454

Reference31 articles.

1. Protocols for the Detection of S-Glutathionylated and S-Nitrosylated Proteins In Situ

2. Redox-Based Regulation of Apoptosis: S-Glutathionylation As a Regulatory Mechanism to Control Cell Death

3. Mechanism of action of enzymes catalyzing thiol-disulfide interchange. Thioltransferases rather than transhydrogenases

4. Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14.fwdarw.S) and its mixed disulfide with glutathione

5. Protein Glutathionylation in the Regulation of Peroxiredoxins: A Family of Thiol-Specific Peroxidases That Function As Antioxidants, Molecular Chaperones, and Signal Modulators

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