Novel N-terminal mutation of human apolipoprotein A-I reduces self-association and impairs LCAT activation-Reference-Cited by-同舟云学术

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Novel N-terminal mutation of human apolipoprotein A-I reduces self-association and impairs LCAT activation

Published:2011-01 Issue:1 Volume:52 Page:35-44
ISSN:0022-2275
Container-title:Journal of Lipid Research
language:en
Short-container-title:Journal of Lipid Research

Author:

Weers Paul M.M.,Patel Arti B.,Wan Leon C-P.,Guigard Emmanuel,Kay Cyril M.,Hafiane Anouar,McPherson Ruth,Marcel Yves L.,Kiss Robert S.

Publisher

Elsevier BV

Subject

Cell Biology,Endocrinology,Biochemistry

Reference47 articles.

1. Three-dimensional models of HDL apoA-I: implications for its assembly and function;Thomas;J. Lipid Res.,2008

2. The structure of apolipoprotein A-I in high density lipoproteins;Davidson;J. Biol. Chem.,2007

3. Structural organization of the N-terminal domain of apolipoprotein A-I: studies of tryptophan mutants;Davidson;Biochemistry.,1999

4. Properties of an N-terminal proteolytic fragment of apolipoprotein AI in solution and in reconstituted high density lipoproteins;Ji;J. Biol. Chem.,1995

5. Structure-function relationships of apolipoprotein A-I: a flexible protein with dynamic lipid associations;Marcel;Curr. Opin. Lipidol.,2003

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3. Abdominal obesity negatively influences key metrics of reverse cholesterol transport;Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids;2022-02

4. Current models of apolipoprotein A-I lipidation by adenosine triphosphate binding cassette transporter A1;Current Opinion in Lipidology;2021-09-27

5. Analysis of pyrene-labelled apolipoprotein A-I oligomerization in solution: Spectra deconvolution and changes in P-value and excimer formation;Archives of Biochemistry and Biophysics;2021-03

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