Effects ofS-Glutathionylation andS-Nitrosylation on Calmodulin Binding to Triads and FKBP12 Binding to Type 1 Calcium Release Channels
Author:
Affiliation:
1. FONDAP Center for Molecular Studies of the Cell, Facultad de Medicina, Universidad de Chile, Casilla 70005, Santiago 7, Chile.
2. Department of Molecular Physiology and Biophysics, Baylor College of Medicine, Houston, TX.
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.2005.7.870
Reference47 articles.
1. S-Glutathionylation Decreases Mg2+ Inhibition and S-Nitrosylation Enhances Ca2+ Activation of RyR1 Channels
2. FKBP12 Binding to RyR1 Modulates Excitation-Contraction Coupling in Mouse Skeletal Myotubes
3. Annexin VI is Attached to Transverse-Tubule Membranes in Isolated Skeletal Muscle Triads
4. FKBP12 associates tightly with the skeletal muscle type 1 ryanodine receptor, but not with other intracellular calcium release channels
5. Sodium Transport in Triads Isolated from Rabbit Skeletal Muscle
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