The skeletal muscle calcium release channel: coupled O(sub)2 sensor and NO siganling functions
Article Abstract:
Results show that the redox state of the skeletal muscle calcium release channel/ryanodine receptor is controlled by physiological oxygen tension and that it involves thiol groups and a response to nitric oxide. Data further reveal that nitric acid activates the calcium channel by S-nitrosylation of cysteine residue.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2000
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Nitrosylation: the prototypic redox-based signaling mechanism
Article Abstract:
The authors discuss the signaling systems based on the protein post-translational modification principle. The subjects of interest include the importance of allostery in posttranslational protein modification by nitrogen oxide and the role of O (sub)2 /redox as the allosteric effector.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2001
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Nitrosative stress: activation of the transcription factor OxyR
Article Abstract:
Nitrosative stress in Escherichia coli results from the formation of certain S-nitrosothiols and is associated with a decrease in intracellular thiol and the expression of OxyR, the hydrogen peroxide-responsive activator of E. coli antioxidant genes. Oxidation of OxyR prevents cellular damage caused by oxidative stress by induction of resistance or antinitrosative genes. A diagram comparing nitrosative and oxidative stress is presented.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
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