Biophysical characterization of Abeta42 C-terminal fragments: inhibitors of Abeta42 neurotoxicity.
about
Disrupting self-assembly and toxicity of amyloidogenic protein oligomers by "molecular tweezers" - from the test tube to animal modelsStructural and functional characterization of a multifunctional alanine-rich peptide analogue from Pleuronectes americanusLymphatics in Neurological Disorders: A Neuro-Lympho-Vascular Component of Multiple Sclerosis and Alzheimer's Disease?Modulation of Amyloid β-Protein (Aβ) Assembly by Homologous C-Terminal Fragments as a Strategy for Inhibiting Aβ Toxicity.Mechanistic investigation of the inhibition of Abeta42 assembly and neurotoxicity by Abeta42 C-terminal fragmentsModeling amyloid-beta as homogeneous dodecamers and in complex with cellular prion protein.Protein amyloids develop an intrinsic fluorescence signature during aggregation.Structural basis for Aβ1–42 toxicity inhibition by Aβ C-terminal fragments: discrete molecular dynamics study.Short Peptides as Inhibitors of Amyloid AggregationDiscrete molecular dynamics study of oligomer formation by N-terminally truncated amyloid β-protein.Biochemistry of amyloid β-protein and amyloid deposits in Alzheimer disease.Aβ42 and Aβ40: similarities and differences.Inhibiting the nucleation of amyloid structure in a huntingtin fragment by targeting α-helix-rich oligomeric intermediates.C-terminal tetrapeptides inhibit Aβ42-induced neurotoxicity primarily through specific interaction at the N-terminus of Aβ42.Rapid α-oligomer formation mediated by the Aβ C terminus initiates an amyloid assembly pathway.A key role for lysine residues in amyloid β-protein folding, assembly, and toxicity.Capping of aβ42 oligomers by small molecule inhibitors.A two-step strategy for structure-activity relationship studies of N-methylated aβ42 C-terminal fragments as aβ42 toxicity inhibitorsA peptide probe for detection of various beta-amyloid oligomers.Small static electric field strength promotes aggregation-prone structures in amyloid-β(29-42).A computational study of self-assembled hexapeptide inhibitors against amyloid-β (Aβ) aggregation.
P2860
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P2860
Biophysical characterization of Abeta42 C-terminal fragments: inhibitors of Abeta42 neurotoxicity.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年学术文章
@wuu
2010年学术文章
@zh-cn
2010年学术文章
@zh-hans
2010年学术文章
@zh-my
2010年学术文章
@zh-sg
2010年學術文章
@yue
2010年學術文章
@zh
2010年學術文章
@zh-hant
name
Biophysical characterization o ...... tors of Abeta42 neurotoxicity.
@en
Biophysical characterization o ...... tors of Abeta42 neurotoxicity.
@nl
type
label
Biophysical characterization o ...... tors of Abeta42 neurotoxicity.
@en
Biophysical characterization o ...... tors of Abeta42 neurotoxicity.
@nl
prefLabel
Biophysical characterization o ...... tors of Abeta42 neurotoxicity.
@en
Biophysical characterization o ...... tors of Abeta42 neurotoxicity.
@nl
P2093
P2860
P356
P1433
P1476
Biophysical characterization o ...... tors of Abeta42 neurotoxicity.
@en
P2093
Bernhard H Monien
Brigita Urbanc
Erica A Fradinger
Huiyuan Li
P2860
P304
P356
10.1021/BI902075H
P407
P577
2010-02-01T00:00:00Z