Side-chain dynamics reveals transient association of Aβ(1-40) monomers with amyloid fibers.
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Transient dynamics of Aβ contribute to toxicity in Alzheimer's diseaseThe C-terminal threonine of Aβ43 nucleates toxic aggregation via structural and dynamical changes in monomers and protofibrils.Resolution of oligomeric species during the aggregation of Aβ1-40 using (19)F NMR.Ultraviolet light triggers the conversion of Cu2+-bound Aβ42 aggregates into cytotoxic species in a copper chelation-independent manner.Tranilast binds to aβ monomers and promotes aβ fibrillation.Electron Transfer Directed Antibacterial Properties of Graphene Oxide on Metals.Model membrane size-dependent amyloidogenesis of Alzheimer's amyloid-β peptides.Structures and dynamics of β-barrel oligomer intermediates of amyloid-beta16-22 aggregation.Fluorinated amino acids in amyloid formation: a symphony of size, hydrophobicity and α-helix propensity
P2860
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P2860
Side-chain dynamics reveals transient association of Aβ(1-40) monomers with amyloid fibers.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Side-chain dynamics reveals tr ...... monomers with amyloid fibers.
@ast
Side-chain dynamics reveals tr ...... monomers with amyloid fibers.
@en
type
label
Side-chain dynamics reveals tr ...... monomers with amyloid fibers.
@ast
Side-chain dynamics reveals tr ...... monomers with amyloid fibers.
@en
prefLabel
Side-chain dynamics reveals tr ...... monomers with amyloid fibers.
@ast
Side-chain dynamics reveals tr ...... monomers with amyloid fibers.
@en
P2093
P2860
P356
P1476
Side-chain dynamics reveals tr ...... ) monomers with amyloid fibers
@en
P2093
Janarthanan Krishnamoorthy
Nicole Jahr
Subramanian Vivekanandan
P2860
P304
13618-13623
P356
10.1021/JP305279W
P407
P577
2012-11-12T00:00:00Z