The C-Terminal Active Site Cysteine ofEscherichia coliGlutaredoxin 1 Determines the Glutathione Specificity of the Second Step of Peptide Deglutathionylation-Reference-Cited by-同舟云学术

The C-Terminal Active Site Cysteine ofEscherichia coliGlutaredoxin 1 Determines the Glutathione Specificity of the Second Step of Peptide Deglutathionylation

Published:2009-08 Issue:8 Volume:11 Page:1819-1828
ISSN:1523-0864
Container-title:Antioxidants & Redox Signaling
language:en
Short-container-title:Antioxidants & Redox Signaling

Author:

Saaranen Mirva J.¹,Salo Kirsi E. H.¹,Latva-Ranta Maria K.¹,Kinnula Vuokko L.²,Ruddock Lloyd W.¹

Affiliation:

1. Department of Biochemistry, University of Oulu, Oulu, Finland.

2. Biomedicum Helsinki and Department of Medicine, Division of Pulmonary Diseases, Helsinki University Hospital, Helsinki, Finland.

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.2008.2387

Reference26 articles.

1. Identification, Characterization, and Crystal Structure of the Omega Class Glutathione Transferases

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

3. The Nuclear Magnetic Resonance Solution Structure of the Mixed Disulfide between Escherichia coli Glutaredoxin(C14S) and Glutathione

4. Structural Aspects of the Distinct Biochemical Properties of Glutaredoxin 1 and Glutaredoxin 2 from Saccharomyces cerevisiae

5. Quantifying Escherichia coli Glutaredoxin-3 Substrate Specificity Using Ligand-induced Stability

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