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Lim, Mi Hee
MetalloNeuroChemistry Lab (MNCL)
Research Interests
  • Neurodegenerative disease, small molecule design, network between metal, proteins, and ROS

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Amyloid-beta adopts a conserved, partially folded structure upon binding to zwitterionic lipid bilayers prior to amyloid formation

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Title
Amyloid-beta adopts a conserved, partially folded structure upon binding to zwitterionic lipid bilayers prior to amyloid formation
Author
Lim, Mi HeeKorshavn, Kyle J.Ramamoorthy, AyyalusamyBhunia, Anirban
Issue Date
2016-01
Publisher
ROYAL SOC CHEMISTRY
Citation
CHEMICAL COMMUNICATIONS, v.52, no.5, pp.882 - 885
Abstract
Aggregation at the neuronal cell membrane's lipid bilayer surface is implicated in amyloid-β (Aβ) toxicity associated with Alzheimer's disease; however, structural and mechanistic insights into the process remain scarce. We have identified a conserved binding mode of Aβ40 on lipid bilayer surfaces with a conserved helix containing the self-recognition site (K16-E22).
URI
https://scholarworks.unist.ac.kr/handle/201301/18092
URL
http://pubs.rsc.org/en/Content/ArticleLanding/2015/CC/C5CC08634E#!divAbstract
DOI
10.1039/C5CC08634E
ISSN
1359-7345
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PHY_Journal Papers
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