Surface behavior of apolipoprotein A-I and its deletion mutants at model lipoprotein interfaces
出版年份 2013 全文链接
标题
Surface behavior of apolipoprotein A-I and its deletion mutants at model lipoprotein interfaces
作者
关键词
-
出版物
JOURNAL OF LIPID RESEARCH
Volume 55, Issue 3, Pages 478-492
出版商
American Society for Biochemistry & Molecular Biology (ASBMB)
发表日期
2013-12-06
DOI
10.1194/jlr.m044743
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- Surface pressure-dependent conformation change of apolipoprotein-derived amphipathic α-helices
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- Changes in helical content or net charge of apolipoprotein C-I alter its affinity for lipid/water interfaces
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- 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
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- Crystal Structure of Δ(185–243)ApoA-I Suggests a Mechanistic Framework for the Protein Adaptation to the Changing Lipid Load in Good Cholesterol: From Flatland to Sphereland via Double Belt, Belt Buckle, Double Hairpin and Trefoil/Tetrafoil
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- Surface study of apoB1694–1880, a sequence that can anchor apoB to lipoproteins and make it nonexchangeable
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