A conserved GXXXG motif in the transmembrane domain of CLIC proteins is essential for their cholesterol-dependant membrane interaction-Reference-Cited by-同舟云学术

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A conserved GXXXG motif in the transmembrane domain of CLIC proteins is essential for their cholesterol-dependant membrane interaction

Published:2019-08 Issue:8 Volume:1863 Page:1243-1253
ISSN:0304-4165
Container-title:Biochimica et Biophysica Acta (BBA) - General Subjects
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - General Subjects

Author:

Hossain Khondker Rufaka,Turkewitz Daniel R.,Holt Stephen A.,Herson Leonie,Brown Louise J.,Cornell Bruce A.,Curmi Paul M.G.,Valenzuela Stella M.

Funder

Australian Research Council

ARC Industry Transformational Research Hub Scheme

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference59 articles.

1. Regulation of receptor function by cholesterol;Burger;Cell. Mol. Life Sci.,2000

2. Cholesterol and the interaction of proteins with membrane domains;Epand;Prog. Lipid Res.,2006

3. Proteins and cholesterol-rich domains;Epand;Biochim. Biophys. Acta,2008

4. Cholesterol interaction with proteins that partition into membrane domains: an overview;Epand;Subcell Biochem.,2010

5. What's so special about cholesterol?;Mouritsen;Lipids,2004

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