Amyloid-β(25-35) peptides aggregate into cross-β sheets in unsaturated anionic lipid membranes at high peptide concentrations.
about
The Molecular Structure of Human Red Blood Cell Membranes from Highly Oriented, Solid Supported Multi-Lamellar Membranes.Membrane-Accelerated Amyloid-β Aggregation and Formation of Cross-β Sheets.Partitioning of caffeine in lipid bilayers reduces membrane fluidity and increases membrane thickness.A Cytosolic Amphiphilic α-Helix Controls the Activity of the Bile Acid-sensitive Ion Channel (BASIC).Modulation of DEG/ENaCs by Amphiphiles Suggests Sensitivity to Membrane AlterationsMembrane-Modulating Drugs can Affect the Size of Amyloid-β Aggregates in Anionic Membranes
P2860
Amyloid-β(25-35) peptides aggregate into cross-β sheets in unsaturated anionic lipid membranes at high peptide concentrations.
description
2016 nî lūn-bûn
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2016年の論文
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2016年学术文章
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2016年学术文章
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name
Amyloid-β(25-35) peptides aggr ...... t high peptide concentrations.
@en
type
label
Amyloid-β(25-35) peptides aggr ...... t high peptide concentrations.
@en
prefLabel
Amyloid-β(25-35) peptides aggr ...... t high peptide concentrations.
@en
P2093
P2860
P356
P1433
P1476
Amyloid-β(25-35) peptides aggr ...... at high peptide concentrations
@en
P2093
An-Chang Shi
Hannah Dies
Jennifer Tang
Richard J Alsop
P2860
P304
P356
10.1039/C5SM02619A
P577
2016-02-26T00:00:00Z