Protective spin-labeled fluorenes maintain amyloid beta peptide in small oligomers and limit transitions in secondary structure.

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A Metal-Free Method for Producing MRI Contrast at Amyloid-β.A Bifunctional Anti-Amyloid Blocks Oxidative Stress and the Accumulation of Intraneuronal Amyloid-Beta

P2860

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P2860

Protective spin-labeled fluorenes maintain amyloid beta peptide in small oligomers and limit transitions in secondary structure.

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http://www.wikidata.org/entity/Q36244824

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2015 nî lūn-bûn

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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2015年论文

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2015年论文

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name

Protective spin-labeled fluore ...... itions in secondary structure.

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Protective spin-labeled fluore ...... itions in secondary structure.

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label

Protective spin-labeled fluore ...... itions in secondary structure.

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Protective spin-labeled fluore ...... itions in secondary structure.

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prefLabel

Protective spin-labeled fluore ...... itions in secondary structure.

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Protective spin-labeled fluore ...... itions in secondary structure.

@en

P1476

Protective spin-labeled fluore ...... itions in secondary structure.

@en

P2093

Izumi Maezawa

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Jitka Petrlova

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Kálmán Hideg

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Lee-Way Jin

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Robin Altman

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Silvia Hilt

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

Sonny Ly

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

Tamás Kálai

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

Ted A Laurence

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P2860

The structural basis of protein folding and its links with human disease

Amyloid-beta protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory

Transient dynamics of Aβ contribute to toxicity in Alzheimer's disease

Functional impairment of microglia coincides with Beta-amyloid deposition in mice with Alzheimer-like pathology

Solution structure of the Alzheimer amyloid beta-peptide (1-42) in an apolar microenvironment. Similarity with a virus fusion domain

The molecular assembly of amyloid aβ controls its neurotoxicity and binding to cellular proteins

A specific amyloid-beta protein assembly in the brain impairs memory

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

Natural oligomers of the amyloid-beta protein specifically disrupt cognitive function

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

P304

1860-1870

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scholarly article

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10.1016/J.BBAPAP.2015.09.002

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English

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1854

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John C Voss

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2015-09-13T00:00:00Z

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26374940

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P932

4631661

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Protective spin-labeled fluorenes maintain amyloid beta peptide in small oligomers and limit transitions in secondary structure.

about

P2860

P2860

Protective spin-labeled fluorenes maintain amyloid beta peptide in small oligomers and limit transitions in secondary structure.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P50

P577

P698

P932