The extreme N-terminal region of human apolipoprotein A-I has a strong propensity to form amyloid fibrils-Reference-Cited by-同舟云学术

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The extreme N-terminal region of human apolipoprotein A-I has a strong propensity to form amyloid fibrils

Published:2013-12-05 Issue:3 Volume:588 Page:389-394
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Adachi Emi,Kosaka Asako,Tsuji Kohei,Mizuguchi Chiharu,Kawashima Hiroyuki,Shigenaga Akira,Nagao Kohjiro,Akaji Kenichi,Otaka Akira,Saito Hiroyuki

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/j.febslet.2013.11.031/fullpdf

Reference30 articles.

1. Cholesterol efflux and atheroprotection: advancing the concept of reverse cholesterol transport;Rosenson;Circulation,2012

2. The role of reverse cholesterol transport in animals and humans and relationship to atherosclerosis;Rader;J. Lipid Res.,2009

3. The effects of altered apolipoprotein A-I structure on plasma HDL concentration;Sorci-Thomas;Trends Cardiovasc. Med.,2002

4. Apolipoprotein A-I: structure-function relationships;Frank;J. Lipid Res.,2000

5. The new apolipoprotein A-I variant leu(174) -> Ser causes hereditary cardiac amyloidosis, and the amyloid fibrils are constituted by the 93-residue N-terminal polypeptide;Obici;Am. J. Pathol.,1999

Cited by 24 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. Amyloidogenic 60–71 deletion/ValThr insertion mutation of apolipoprotein A-I generates a new aggregation-prone segment that promotes nucleation through entropic effects;Scientific Reports;2023-10-28

2. Looking Beyond the Core: The Role of Flanking Regions in the Aggregation of Amyloidogenic Peptides and Proteins;Frontiers in Neuroscience;2020-12-01

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

4. Inborn errors of apolipoprotein A-I metabolism;Current Opinion in Lipidology;2020-04

5. Mechanisms of aggregation and fibril formation of the amyloidogenic N-terminal fragment of apolipoprotein A-I;Journal of Biological Chemistry;2019-09

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