A folding transition underlies the emergence of membrane affinity in amyloid-β.
about
Maximally asymmetric transbilayer distribution of anionic lipids alters the structure and interaction with lipids of an amyloidogenic protein dimer bound to the membrane surfaceAmyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Steric Crowding of the Turn Region Alters the Tertiary Fold of Amyloid-β18-35 and Makes It Soluble.Effect of amyloids on the vesicular machinery: implications for somatic neurotransmission.Glucose directs amyloid-beta into membrane-active oligomers.Investigation of the interaction of amyloid β peptide (11-42) oligomers with a 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) membrane using molecular dynamics simulation.Major Reaction Coordinates Linking Transient Amyloid-β Oligomers to Fibrils Measured at Atomic Level.Significant structural differences between transient amyloid-β oligomers and less-toxic fibrils in regions known to harbor familial Alzheimer's mutations.pH changes the aggregation propensity of amyloid-β without altering the monomer conformation.
P2860
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P2860
A folding transition underlies the emergence of membrane affinity in amyloid-β.
description
2013 nî lūn-bûn
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name
A folding transition underlies the emergence of membrane affinity in amyloid-β.
@en
A folding transition underlies the emergence of membrane affinity in amyloid-β.
@nl
type
label
A folding transition underlies the emergence of membrane affinity in amyloid-β.
@en
A folding transition underlies the emergence of membrane affinity in amyloid-β.
@nl
prefLabel
A folding transition underlies the emergence of membrane affinity in amyloid-β.
@en
A folding transition underlies the emergence of membrane affinity in amyloid-β.
@nl
P2093
P2860
P50
P356
P1476
A folding transition underlies the emergence of membrane affinity in amyloid-β
@en
P2093
Debanjan Bhowmik
Elisha Haas
Mamata Kombrabail
Muralidharan Chandrakesan
Rajiv Abhyanakar
Sucheta Dandekar
P2860
P304
19129-19133
P356
10.1039/C3CP52732H
P407
P577
2013-11-01T00:00:00Z