Verification of the intermolecular parallel beta-sheet in E22K-Abeta42 aggregates by solid-state NMR using rotational resonance: implications for the supramolecular arrangement of the toxic conformer of Abeta42.
about
The turn formation at positions 22 and 23 in the 42-mer amyloid beta peptide: the emerging role in the pathogenesis of Alzheimer's disease.Taxifolin inhibits amyloid-β oligomer formation and fully restores vascular integrity and memory in cerebral amyloid angiopathy.Familial Alzheimer's Disease Mutations within the Amyloid Precursor Protein Alter the Aggregation and Conformation of the Amyloid-β Peptide.Silymarin attenuated the amyloid β plaque burden and improved behavioral abnormalities in an Alzheimer's disease mouse model.Differential effect of amyloid beta peptides on mitochondrial axonal trafficking depends on their state of aggregation and binding to the plasma membrane.
P2860
Verification of the intermolecular parallel beta-sheet in E22K-Abeta42 aggregates by solid-state NMR using rotational resonance: implications for the supramolecular arrangement of the toxic conformer of Abeta42.
description
2008 nî lūn-bûn
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2008年の論文
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2008年学术文章
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2008年学术文章
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2008年学术文章
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2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
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2008年學術文章
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2008年學術文章
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name
Verification of the intermolec ...... he toxic conformer of Abeta42.
@en
Verification of the intermolec ...... he toxic conformer of Abeta42.
@nl
type
label
Verification of the intermolec ...... he toxic conformer of Abeta42.
@en
Verification of the intermolec ...... he toxic conformer of Abeta42.
@nl
prefLabel
Verification of the intermolec ...... he toxic conformer of Abeta42.
@en
Verification of the intermolec ...... he toxic conformer of Abeta42.
@nl
P2093
P2860
P356
P1476
Verification of the intermolec ...... the toxic conformer of Abeta42
@en
P2093
Azusa Nakanishi
Ryutaro Ohashi
Takahiko Shimizu
Takuji Shirasawa
Yuichi Masuda
P2860
P304
P356
10.1271/BBB.80250
P577
2008-08-07T00:00:00Z