Structural differences between apolipoprotein E3 and E4 as measured by (19)F NMR.
about
The binding of apolipoprotein E to oligomers and fibrils of amyloid-β alters the kinetics of amyloid aggregation.ApoE: In Vitro Studies of a Small Molecule Effector.Mass spectrometry-based protein footprinting characterizes the structures of oligomeric apolipoprotein E2, E3, and E4.Hydrogen/deuterium exchange and electron-transfer dissociation mass spectrometry determine the interface and dynamics of apolipoprotein E oligomerizationStructural differences between apoE3 and apoE4 may be useful in developing therapeutic agents for Alzheimer's disease.The association−dissociation behavior of the ApoE proteins: kinetic and equilibrium studiesDissociation of apolipoprotein E oligomers to monomer is required for high-affinity binding to phospholipid vesicles.Fluorescence study of domain structure and lipid interaction of human apolipoproteins E3 and E4.
P2860
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P2860
Structural differences between apolipoprotein E3 and E4 as measured by (19)F NMR.
description
2010 nî lūn-bûn
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2010年の論文
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2010年論文
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2010年論文
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2010年論文
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2010年論文
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2010年論文
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2010年论文
@wuu
2010年论文
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2010年论文
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name
Structural differences between apolipoprotein E3 and E4 as measured by (19)F NMR.
@en
type
label
Structural differences between apolipoprotein E3 and E4 as measured by (19)F NMR.
@en
prefLabel
Structural differences between apolipoprotein E3 and E4 as measured by (19)F NMR.
@en
P2093
P2860
P356
P1433
P1476
Structural differences between apolipoprotein E3 and E4 as measured by (19)F NMR.
@en
P2093
Berevan Baban
Carl Frieden
Kanchan Garai
Sourajit M Mustafi
P2860
P356
10.1002/PRO.283
P577
2010-01-01T00:00:00Z