A three-way inter-molecular network accounts for the CaVα2δ1-induced functional modulation of the pore-forming CaV1.2 subunit-Reference-Cited by-同舟云学术

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A three-way inter-molecular network accounts for the CaVα2δ1-induced functional modulation of the pore-forming CaV1.2 subunit

Published:2018-05 Issue:19 Volume:293 Page:7176-7188
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Briot Julie,Mailhot Olivier,Bourdin Benoîte,Tétreault Marie-Philippe,Najmanovich Rafael,Parent Lucie

Funder

Fonds de Recherche du Québec - Santé

Gouvernement du Canada | Canadian Institutes of Health Research (CIHR)

Heart and Stroke Foundation of Canada (HSF)

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference48 articles.

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3. Crystal structure of the von Willebrand factor A domain of human capillary morphogenesis protein 2: an anthrax toxin receptor;Lacy;Proc. Natl. Acad. Sci. U.S.A,2004

4. Structure of Plasmodium falciparum TRAP (thrombospondin-related anonymous protein) A domain highlights distinct features in apicomplexan von Willebrand factor A homologues;Pihlajamaa;Biochem. J,2013

5. The protein fold of the von Willebrand factor type A domain is predicted to be similar to the open twisted β-sheet flanked by α-helices found in human ras-p21;Edwards;FEBS Lett,1995

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