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2D-oriented self-assembly of peptides induced by hydrated electrons.水合电子诱导的肽的二维取向自组装。
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Clinical and biomarker changes in dominantly inherited Alzheimer's disease.常染色体显性遗传阿尔茨海默病的临床和生物标志物变化。
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Intracerebral inoculation of pathological α-synuclein initiates a rapidly progressive neurodegenerative α-synucleinopathy in mice.脑内接种病理性 α-突触核蛋白会在小鼠中引发快速进行性神经退行性 α-突触核蛋白病。
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神经退行性疾病中蛋白质错误折叠和结构应变的背景依赖性

Context dependence of protein misfolding and structural strains in neurodegenerative diseases.

作者信息

Mehta Anil K, Rosen Rebecca F, Childers W Seth, Gehman John D, Walker Lary C, Lynn David G

机构信息

Department of Chemistry, Alzheimer's Disease Research Center, Emory University, Atlanta, GA, 30322; Department of Biology, Alzheimer's Disease Research Center, Emory University, Atlanta, GA, 30322.

出版信息

Biopolymers. 2013 Nov;100(6):722-30. doi: 10.1002/bip.22283.

DOI:10.1002/bip.22283
PMID:23893572
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3979318/
Abstract

Vast arrays of structural forms are accessible to simple amyloid peptides and environmental conditions can direct assembly into single phases. These insights are now being applied to the aggregation of the Aβ peptide of Alzheimer's disease and the identification of causative phases. We extend use of the imaging agent Pittsburgh compound B to discriminate among Aβ phases and begin to define conditions of relevance to the disease state. Also, we specifically highlight the development of methods for defining the structures of these more complex phases.

摘要

简单的淀粉样肽可以形成各种各样的结构形式,环境条件能够引导其组装成单相。这些见解目前正应用于阿尔茨海默病β淀粉样肽(Aβ)的聚集以及致病相的识别。我们扩展了成像剂匹兹堡化合物B的用途,以区分不同的Aβ相,并开始确定与疾病状态相关的条件。此外,我们特别强调了定义这些更复杂相结构的方法的发展。