Light-controlled toxicity of engineered amyloid β-peptides.

Item

http://www.wikidata.org/entity/Q39242847

description

2012 nî lūn-bûn

@nan

2012年の論文

@ja

2012年学术文章

@wuu

2012年学术文章

@zh-cn

2012年学术文章

@zh-hans

2012年学术文章

@zh-my

2012年学术文章

@zh-sg

2012年學術文章

@yue

2012年學術文章

@zh

2012年學術文章

@zh-hant

name

Light-controlled toxicity of engineered amyloid β-peptides.

@en

Light-controlled toxicity of engineered amyloid β-peptides.

@nl

type

Item

label

Light-controlled toxicity of engineered amyloid β-peptides.

@en

Light-controlled toxicity of engineered amyloid β-peptides.

@nl

prefLabel

Light-controlled toxicity of engineered amyloid β-peptides.

@en

Light-controlled toxicity of engineered amyloid β-peptides.

@nl

P1476

Light-controlled toxicity of engineered amyloid β-peptides.

@en

P2093

Christian Barucker

http://www.w3.org/2001/XMLSchema#string

Christian Hoppmann

http://www.w3.org/2001/XMLSchema#string

Dorothea Lorenz

http://www.w3.org/2001/XMLSchema#string

Michael Beyermann

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P2860

beta-Amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease

Structural conversion of neurotoxic amyloid-beta(1-42) oligomers to fibrils

Lipids revert inert Abeta amyloid fibrils to neurotoxic protofibrils that affect learning in mice

Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo

The alpha-to-beta conformational transition of Alzheimer's Abeta-(1-42) peptide in aqueous media is reversible: a step by step conformational analysis suggests the location of beta conformation seeding

Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor

Amyloid beta protein forms ion channels: implications for Alzheimer's disease pathophysiology.

Controlled in situ preparation of A beta(1-42) oligomers from the isopeptide "iso-A beta(1-42)", physicochemical and biological characterization.

A photocontrolled beta-hairpin peptide.

P304

2657-2660

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P31

scholarly article

P356

10.1002/CBIC.201200605

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P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Gerd Multhaup

P577

2012-11-19T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

23161824

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