Comparison of apoA-I helical structure and stability in discoidal and spherical HDL particles by HX and mass spectrometry-Reference-Cited by-同舟云学术

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Comparison of apoA-I helical structure and stability in discoidal and spherical HDL particles by HX and mass spectrometry

Published:2013-06 Issue:6 Volume:54 Page:1589-1597
ISSN:0022-2275
Container-title:Journal of Lipid Research
language:en
Short-container-title:Journal of Lipid Research

Author:

Chetty Palaniappan Sevugan,Nguyen David,Nickel Margaret,Lund-Katz Sissel,Mayne Leland,Englander S.Walter,Phillips Michael C.

Publisher

Elsevier BV

Subject

Cell Biology,Endocrinology,Biochemistry

Reference40 articles.

1. The structure of human lipoprotein A-I: evidence for the “belt” model;Koppaka;J. Biol. Chem.,1999

2. A detailed molecular belt model for apolipoprotein A-I in discoidal high density lipoprotein;Segrest;J. Biol. Chem.,1999

3. Apolipoprotein structural organization in high density lipoproteins: belts, bundles, hinges and hairpins;Davidson;Curr. Opin. Lipidol.,2005

4. The use of chemical cross-linking and mass spectrometry to elucidate the tertiary conformation of lipid-bound apolipoprotein A-I;Thomas;Curr. Opin. Lipidol.,2006

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

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3. Structure dynamics of ApoA-I amyloidogenic variants in small HDL increase their ability to mediate cholesterol efflux;Journal of Lipid Research;2021

4. High-Density Lipoproteins;Contemporary Cardiology;2020-12-16

5. Novel conformation‐selective monoclonal antibodies against apoA‐I amyloid fibrils;The FEBS Journal;2020-08-04

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