Interactions between lipid-free apolipoprotein-AI and a lipopeptide incorporating the RGDS cell adhesion motif
Author:
Publisher
Royal Society of Chemistry (RSC)
Subject
General Materials Science
Link
http://pubs.rsc.org/en/content/articlepdf/2015/NR/C4NR05072J
Reference36 articles.
1. Structural Analysis of Apolipoprotein A-I: Effects of Amino- and Carboxy-Terminal Deletions on the Lipid-Free Structure
2. The Amyloid Beta Peptide: A Chemist’s Perspective. Role in Alzheimer’s and Fibrillization
3. The roles of C-terminal helices of human apolipoprotein A-I in formation of high-density lipoprotein particles
4. Crystal structure of human apolipoprotein A-I: Insights into its protective effect against cardiovascular diseases
5. The role of apolipoprotein AI domains in lipid binding
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1. Cell Adhesion Motif-Functionalized Lipopeptides: Nanostructure and Selective Myoblast Cytocompatibility;Biomacromolecules;2022-12-15
2. Biophysical modulation of peptide-membrane interactions;AMINO ACIDS PEP PROT;2017
3. Reversible, Short α-Peptide Assembly for Controlled Capture and Selective Release of Enantiomers;Journal of the American Chemical Society;2016-05-03
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