Characterization of Mammalian Sulfiredoxin and Its Reactivation of Hyperoxidized Peroxiredoxin through Reduction of Cysteine Sulfinic Acid in the Active Site to Cysteine-Reference-Cited by-同舟云学术

Characterization of Mammalian Sulfiredoxin and Its Reactivation of Hyperoxidized Peroxiredoxin through Reduction of Cysteine Sulfinic Acid in the Active Site to Cysteine

Published:2004-12 Issue:49 Volume:279 Page:50994-51001
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Chang Tong-Shin,Jeong Woojin,Woo Hyun Ae,Lee Sun Mi,Park Sunjoo,Rhee Sue Goo

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference31 articles.

1. Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes.

2. Peroxiredoxin, a Novel Family of Peroxidases

3. Structure, mechanism and regulation of peroxiredoxins

4. Characterization of a Mammalian Peroxiredoxin That Contains One Conserved Cysteine

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