Glutaredoxin: Role in Reversible ProteinS-Glutathionylation and Regulation of Redox Signal Transduction and Protein Translocation-Reference-Cited by-同舟云学术

Glutaredoxin: Role in Reversible ProteinS-Glutathionylation and Regulation of Redox Signal Transduction and Protein Translocation

Published:2005-03 Issue:3-4 Volume:7 Page:348-366
ISSN:1523-0864
Container-title:Antioxidants & Redox Signaling
language:en
Short-container-title:Antioxidants & Redox Signaling

Author:

Shelton Melissa D.¹,Chock P. Boon²,Mieyal John J.¹

Affiliation:

1. Department of Pharmacology, Case Western Reserve University, Cleveland, OH.

2. Laboratory of Biochemistry, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD.

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.2005.7.348

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1. PKC-β1 isoform activation is required for EGF-induced NF-κB inactivation and IκBα stabilization and protection of F-actin assembly and barrier function in enterocyte monolayers

2. Identification of a conserved oxidation-sensitive cysteine residue in the NFI family of DNA-binding proteins.

3. Thioltransferase (Glutaredoxin) Reactivates the DNA-binding Activity of Oxidation-inactivated Nuclear Factor I

4. Regulation of PTP1B via Glutathionylation of the Active Site Cysteine 215

5. Roles of Superoxide Radical Anion in Signal Transduction Mediated by Reversible Regulation of Protein-tyrosine Phosphatase 1B

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