Shared resource to develop tools and reagents to study structural polymorphisms in Abeta amyloid aggregates in AD

共享资源开发工具和试剂来研究 AD 中 Abeta 淀粉样蛋白聚集体的结构多态性

基本信息

  • 批准号:
    10549101
  • 负责人:
  • 金额:
    $ 126.52万
  • 依托单位:
  • 依托单位国家:
    美国
  • 项目类别:
  • 财政年份:
    2022
  • 资助国家:
    美国
  • 起止时间:
    2022-09-30 至 2027-05-31
  • 项目状态:
    未结题

项目摘要

Project Abstract Alzheimer’s disease (AD) is currently an incurable neurodegenerative disease that affects over 35 million people worldwide, including 5.4 million individuals in the USA with a new case diagnosed every minute. Amyloids occur commonly as key pathological features in a wide variety of neurodegenerative diseases such as AD and despite 30 years of intensive research, important questions about the significance, mechanisms and role in pathogenesis of amyloids remain unresolved. Because of the strong implication of amyloid Aß peptide in familial AD, preparations of amyloid aggregates (oligomers, fibrils) have been featured in over 100,000 publications over the past 30 years. In many cases, conflicting, contradictory and non-reproducible data obfuscate the underlying mechanisms of pathogenesis. Advances in structural biology have established the structures of several distinct types of amyloid, leading to the discovery that amyloid structures are highly polymorphic with the same protein sequence adopting distinct beta sheet folds. Moreover, different structures seem to correlate with different disease subtypes, indicating that structural variation plays a role in pathogenesis. This polymorphism and structural heterogeneity may also underly the irreproducibility and conflicting results that have plagued amyloid research. This suggests a critical need for well-characterized, standardized protocols for the preparation of different types of amyloid Aß aggregates and reagents to authenticate these preparations and specifically identify and quantify these polymorphs in vitro and in brain in order to support basic research to understand the roles and mechanisms of amyloids in disease pathogenesis. Therefore, the overall goal of this resource initiative is to establish a source network for the development of reagents and protocols for the production, standardization, characterization, authentication of amyloid oligomers and fibrils and the dissemination of these materials to investigators.
项目摘要 阿尔茨海默病(AD)是目前影响超过3500万人的不可治愈的神经退行性疾病 全球范围内,包括美国的540万人,每分钟诊断出一个新病例。淀粉样蛋白 通常作为各种神经退行性疾病如AD的关键病理特征, 30年的深入研究,重要问题的意义,机制和作用的发病机制 淀粉样蛋白的问题仍未解决。由于淀粉样蛋白A肽在家族性AD中的强烈暗示, 淀粉样蛋白聚集体(低聚物、原纤维)的制备已经在超过100,000篇出版物中进行了描述。 过去30年在许多情况下,相互冲突、矛盾和不可复制的数据混淆了基本的 发病机制。结构生物学的进展已经建立了几个不同的结构 淀粉样蛋白的类型,导致发现淀粉样蛋白的结构是高度多态性的同一蛋白质 采用不同β折叠的序列。此外,不同的结构似乎与不同的 疾病亚型,表明结构变异在发病机制中起作用。这种多态性和 结构异质性也可能是困扰淀粉样蛋白的不可重复性和相互矛盾的结果的基础。 research.这表明迫切需要良好表征的标准化方案,用于制备 不同类型的淀粉样蛋白聚集体和试剂来鉴定这些制剂并特异性地鉴定 并在体外和大脑中量化这些多晶型物,以支持基础研究, 以及淀粉样蛋白在疾病发病机制中的作用。因此,这一资源倡议的总体目标是 建立一个用于开发试剂和生产,标准化, 淀粉样蛋白低聚物和原纤维的表征、鉴定以及这些材料在 investigators.

项目成果

期刊论文数量(0)
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Charles G. Glabe其他文献

Amyloid Oligomers Increase the Lifetime and Single Channel Conductance of Gramicidin Channels
  • DOI:
    10.1016/j.bpj.2009.12.1527
  • 发表时间:
    2010-01-01
  • 期刊:
  • 影响因子:
  • 作者:
    Yuri Sokolov;Saskia C. Milton;Charles G. Glabe;James E. Hall
  • 通讯作者:
    James E. Hall
Amyloid Oligomers Increase the Lifetime and Single Channel Conductance of Gramicidin Channels
  • DOI:
    10.1016/j.bpj.2010.12.2034
  • 发表时间:
    2011-02-02
  • 期刊:
  • 影响因子:
  • 作者:
    Yuri V. Sokolov;Saskia C. Milton;Charles G. Glabe;James E. Hall
  • 通讯作者:
    James E. Hall
Die spezifische Zellerkennung
特殊的泽勒肯农
  • DOI:
    10.1002/ciuz.19940280111
  • 发表时间:
    1994
  • 期刊:
  • 影响因子:
    0.8
  • 作者:
    A. Hofmann;Charles G. Glabe
  • 通讯作者:
    Charles G. Glabe
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
撤回文章:大脑中一种特定的淀粉样β蛋白聚集体损害记忆
  • DOI:
    10.1038/nature04533
  • 发表时间:
    2006-03-16
  • 期刊:
  • 影响因子:
    48.500
  • 作者:
    Sylvain Lesné;Ming Teng Koh;Linda Kotilinek;Rakez Kayed;Charles G. Glabe;Austin Yang;Michela Gallagher;Karen H. Ashe
  • 通讯作者:
    Karen H. Ashe
Amyloid Oligomers Alter The Conductance Of The Gramicidin Channel
  • DOI:
    10.1016/j.bpj.2008.12.719
  • 发表时间:
    2009-02-01
  • 期刊:
  • 影响因子:
  • 作者:
    Yuri V. Sokolov;Saskia C. Milton;Charles G. Glabe;James E. Hall
  • 通讯作者:
    James E. Hall

Charles G. Glabe的其他文献

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{{ truncateString('Charles G. Glabe', 18)}}的其他基金

Shared resource to develop tools and reagents to study structural polymorphisms in Abeta amyloid aggregates in AD
共享资源开发工具和试剂来研究 AD 中 Abeta 淀粉样蛋白聚集体的结构多态性
  • 批准号:
    10706566
  • 财政年份:
    2022
  • 资助金额:
    $ 126.52万
  • 项目类别:
Temporal, Spatial and Cellular Dynamics of Amyloid Plaque Deposition
淀粉样蛋白斑沉积的时间、空间和细胞动力学
  • 批准号:
    10525630
  • 财政年份:
    2022
  • 资助金额:
    $ 126.52万
  • 项目类别:
Structure and conformational diversity of amyloid oligomers
淀粉样蛋白寡聚物的结构和构象多样性
  • 批准号:
    8235899
  • 财政年份:
    2010
  • 资助金额:
    $ 126.52万
  • 项目类别:
Structure and conformational diversity of amyloid oligomers
淀粉样蛋白寡聚物的结构和构象多样性
  • 批准号:
    8445260
  • 财政年份:
    2010
  • 资助金额:
    $ 126.52万
  • 项目类别:
Structure and conformational diversity of amyloid oligomers
淀粉样蛋白寡聚物的结构和构象多样性
  • 批准号:
    8053831
  • 财政年份:
    2010
  • 资助金额:
    $ 126.52万
  • 项目类别:
STRUCTURE & CONFORMATIONAL DIVERSITY OF AMYLOID AGGREGATES BY FCS
结构
  • 批准号:
    8170964
  • 财政年份:
    2010
  • 资助金额:
    $ 126.52万
  • 项目类别:
SITE-SPECIFIC STUDIES PROVIDE STRUCTURAL INFORMATION ON AMYLOID BETA OLIGOMERS
特定位点研究提供了淀粉样β低聚物的结构信息
  • 批准号:
    8170990
  • 财政年份:
    2010
  • 资助金额:
    $ 126.52万
  • 项目类别:
Structure and conformational diversity of amyloid oligomers
淀粉样蛋白寡聚物的结构和构象多样性
  • 批准号:
    7897965
  • 财政年份:
    2010
  • 资助金额:
    $ 126.52万
  • 项目类别:
STRUCTURE & CONFORMATIONAL DIVERSITY OF AMYLOID AGGREGATES BY FCS
结构
  • 批准号:
    7956535
  • 财政年份:
    2009
  • 资助金额:
    $ 126.52万
  • 项目类别:
Amyloid Accumulation Mechanisms/Pathogenesis in AD Brain
AD 脑中淀粉样蛋白积累机制/发病机制
  • 批准号:
    6587293
  • 财政年份:
    2002
  • 资助金额:
    $ 126.52万
  • 项目类别:

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