Aggregating the amyloid Abeta(11-25) peptide into a four-stranded beta-sheet structure.
about
Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils.Finite size effects in simulations of protein aggregation.Formation and growth of oligomers: a Monte Carlo study of an amyloid tau fragmentEffect of surfaces on amyloid fibril formation.Insight into the stability of cross-β amyloid fibril from VEALYL short peptide with molecular dynamics simulation.Intrinsic determinants of Aβ(12-24) pH-dependent self-assembly revealed by combined computational and experimental studies.All-atom computer simulations of amyloid fibrils disaggregation.Computational simulations of the early steps of protein aggregation.Amyloid-β aggregation with gold nanoparticles on brain lipid bilayer.Coarse-grained protein molecular dynamics simulationsProbing amyloid fibril formation of the NFGAIL peptide by computer simulations
P2860
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P2860
Aggregating the amyloid Abeta(11-25) peptide into a four-stranded beta-sheet structure.
description
2006 nî lūn-bûn
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2006年の論文
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2006年学术文章
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2006年学术文章
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2006年学术文章
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2006年学术文章
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2006年學術文章
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2006年學術文章
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2006年學術文章
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name
Aggregating the amyloid Abeta
@nl
Aggregating the amyloid Abeta(11-25) peptide into a four-stranded beta-sheet structure.
@en
type
label
Aggregating the amyloid Abeta
@nl
Aggregating the amyloid Abeta(11-25) peptide into a four-stranded beta-sheet structure.
@en
prefLabel
Aggregating the amyloid Abeta
@nl
Aggregating the amyloid Abeta(11-25) peptide into a four-stranded beta-sheet structure.
@en
P2860
P356
P1433
P1476
Aggregating the amyloid Abeta(11-25) peptide into a four-stranded beta-sheet structure.
@en
P2093
Philippe Derreumaux
P2860
P304
P356
10.1002/PROT.21134
P407
P577
2006-12-01T00:00:00Z