A dihydropyridine receptor α1s loop region critical for skeletal muscle contraction is intrinsically unstructured and binds to a SPRY domain of the type 1 ryanodine receptor-Reference-Cited by-同舟云学术

A dihydropyridine receptor α1s loop region critical for skeletal muscle contraction is intrinsically unstructured and binds to a SPRY domain of the type 1 ryanodine receptor

Published:2009-03 Issue:3 Volume:41 Page:677-686
ISSN:1357-2725
Container-title:The International Journal of Biochemistry & Cell Biology
language:en
Short-container-title:The International Journal of Biochemistry & Cell Biology

Author:

Cui Yanfang,Tae Han-Shen,Norris Nicole C.,Karunasekara Yamuna,Pouliquin Pierre,Board Philip G.,Dulhunty Angela F.,Casarotto Marco G.

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry

Reference68 articles.

1. Maurocalcine and domain A of the II–III loop of the dihydropyridine receptor Cav 1.1 subunit share common binding sites on the skeletal ryanodine receptor;Altafaj;J Biol Chem,2005

2. The mitochondrial ryanodine receptor in rat heart: a pharmaco-kinetic profile;Altschafl;Biochim Biophys Acta,2007

3. CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices;Baker;Nat Struct Mol Biol,2007

4. Effects of peptide C corresponding to the Glu724–Pro760 region of the II–III loop of the DHP (dihydropyridine) receptor alpha1 subunit on the domain-switch-mediated activation of RyR1 (ryanodine receptor 1) Ca2+ channels;Bannister;Biochem J,2006

5. Removal of clustered positive charge from dihydropyridine receptor II–III loop peptide augments activation of ryanodine receptors;Bannister;Biochem Biophys Res Commun,2004

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