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Access to the article is free, however registration and sign-in are required. Reduced thioredoxin denitrosylates caspase-3, a key protein involved in cell death. Nitric oxide acts as a mild oxidant (1, 2) that reacts with a cysteine residue's thiol group (thiolate) to form an S-nitrosothiol (SNO). This modification affects most classes of proteins and alters protein function. Thus, in the context of redox-based regulation of cell signaling, it is a highly dynamic posttranslational regulatory mechanism of physiological and pathophysiological importance. On page 1050 of this issue (3), Benhar et al. show that thioredoxin and thioredoxin reductase in the cytosol and mitochondria, respectively, constitute a major physiological denitrosylation mechanism that controls programmed cell death (apoptosis) in response to particular stimuli.

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Resource Type: Journal article/Issue, Review, Diagram
Audience Level: Undergraduate lower division 13-14, Undergraduate upper division 15-16

Author and Copyright

Authors and Editors: Arne Holmgren of Medical Nobel Institute for Biochemistry, Karolinska Institutet
Publisher: AAAS
Format: text/html
Copyright and other restrictions: Yes
Cost: No


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