Redox Potential and the Response of Cardiac Ryanodine Receptors to CLIC-2, a Member of the Glutathione S-Transferase Structural Family-Reference-Cited by-同舟云学术

Redox Potential and the Response of Cardiac Ryanodine Receptors to CLIC-2, a Member of the Glutathione S-Transferase Structural Family

Published:2008-10 Issue:10 Volume:10 Page:1675-1686
ISSN:1523-0864
Container-title:Antioxidants & Redox Signaling
language:en
Short-container-title:Antioxidants & Redox Signaling

Author:

Jalilian Chris¹,Gallant Esther M.¹,Board Philip G.¹,Dulhunty Angela F.¹

Affiliation:

1. Division of Molecular Bioscience, John Curtin School of Medical Research, Australian National University, ACT, Australia.

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.2007.1994

Reference31 articles.

1. The Mu class glutathione transferase is abundant in striated muscle and is an isoform-specific regulator of ryanodine receptor calcium channels

2. Preferential Transport of Glutathione versusGlutathione Disulfide in Rat Liver Microsomal Vesicles

3. CLIC4 is enriched at cell-cell junctions and colocalizes with AKAP350 at the centrosome and midbody of cultured mammalian cells

4. CLIC-2 modulates cardiac ryanodine receptor Ca2+ release channels

5. [4] Isolation of sarcoplasmic reticulum fractions referable to longitudinal tubules and functional terminal cisternae from rabbit skeletal muscle

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