Apolipoprotein C-I Binds More Strongly to Phospholipid/Triolein/Water than Triolein/Water Interfaces: A Possible Model for Inhibiting Cholesterol Ester Transfer Protein Activity and Triacylglycerol-Rich Lipoprotein Uptake-Reference-Cited by-同舟云学术

Apolipoprotein C-I Binds More Strongly to Phospholipid/Triolein/Water than Triolein/Water Interfaces: A Possible Model for Inhibiting Cholesterol Ester Transfer Protein Activity and Triacylglycerol-Rich Lipoprotein Uptake

Published:2012-02-02 Issue:6 Volume:51 Page:1238-1248
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Meyers Nathan L.¹,Wang Libo¹,Small Donald M.¹

Affiliation:

1. Department of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts 02118, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi2015212

Reference73 articles.

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2. Plasma lipoproteins: apolipoprotein structure and function.

3. Inhibitory effects of C apolipoproteins from rats and humans on the uptake of triglyceride-rich lipoproteins and their remnants by the perfused rat liver.

4. Effect of the human plasma apolipoproteins and phosphatidylcholine acyl donor on the activity of lecithin. Cholesterol acyltransferase

5. Discoidal complexes of A and C apolipoproteins with lipids and their reactions with lecithin: cholesterol acyltransferase.

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