Structural Studies of N- and C-Terminally Truncated Human Apolipoprotein A-I
Author:
Affiliation:
1. Department of Physiology and Biophysics, Boston University School of Medicine, 715 Albany Street, Boston, Massachusetts 02118
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi034152t
Reference41 articles.
Cited by 36 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. N-terminal mutation of apoA-I and interaction with ABCA1 reveal mechanisms of nascent HDL biogenesis;Journal of Lipid Research;2019-01
2. Charge-transfer interactions induce surface dependent conformational changes in apolipoprotein biocorona;Biointerphases;2017-06
3. High-Density Lipoprotein Biogenesis: Defining the Domains Involved in Human Apolipoprotein A-I Lipidation;Biochemistry;2016-08-23
4. Probing the C-terminal domain of lipid-free apoA-I demonstrates the vital role of the H10B sequence repeat in HDL formation;Journal of Lipid Research;2016-08
5. Molecular crowding impacts the structure of apolipoprotein A-I with potential implications on in vivo metabolism and function;Biopolymers;2016-07-22
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