Structurally distinct toxicity inhibitors bind at common loci on β-amyloid fibril.
about
Disrupting self-assembly and toxicity of amyloidogenic protein oligomers by "molecular tweezers" - from the test tube to animal modelsTechniques for Monitoring Protein Misfolding and Aggregation in Vitro and in Living CellsSite-specific inhibitory mechanism for amyloid β42 aggregation by catechol-type flavonoids targeting the Lys residues.Insight into amyloid structure using chemical probes.Amino acid substitutions [K16A] and [K28A] distinctly affect amyloid β-protein oligomerization.The role of molecular simulations in the development of inhibitors of amyloid β-peptide aggregation for the treatment of Alzheimer's diseaseBiophysical studies of the amyloid β-peptide: interactions with metal ions and small molecules.Perspectives on Inhibiting β-Amyloid Aggregation through Structure-Based Drug Design.Characteristics of C-terminal, β-amyloid peptide binding fragment of neuroprotective protease inhibitor, cystatin C.A key role for lysine residues in amyloid β-protein folding, assembly, and toxicity.Inhibiting, promoting, and preserving stability of functional proteinfibrils
P2860
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P2860
Structurally distinct toxicity inhibitors bind at common loci on β-amyloid fibril.
description
2010 nî lūn-bûn
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2010年の論文
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年學術文章
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2010年學術文章
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name
Structurally distinct toxicity inhibitors bind at common loci on β-amyloid fibril.
@en
Structurally distinct toxicity inhibitors bind at common loci on β-amyloid fibril.
@nl
type
label
Structurally distinct toxicity inhibitors bind at common loci on β-amyloid fibril.
@en
Structurally distinct toxicity inhibitors bind at common loci on β-amyloid fibril.
@nl
prefLabel
Structurally distinct toxicity inhibitors bind at common loci on β-amyloid fibril.
@en
Structurally distinct toxicity inhibitors bind at common loci on β-amyloid fibril.
@nl
P2860
P356
P1433
P1476
Structurally distinct toxicity inhibitors bind at common loci on β-amyloid fibril.
@en
P2093
Ben Keshet
Theresa A Good
P2860
P304
P356
10.1002/PRO.509
P577
2010-12-01T00:00:00Z