The mechanism of Hsp90-induced oligomerizaton of Tau-Reference-Cited by-同舟云学术

登录注册会员服务联系我们

The mechanism of Hsp90-induced oligomerizaton of Tau

Published:2020-03-13 Issue:11 Volume:6 Page:
ISSN:2375-2548
Container-title:Science Advances
language:en
Short-container-title:Sci. Adv.

Author:

Weickert S.¹²^ORCID,Wawrzyniuk M.³^ORCID,John L. H.¹^ORCID,Rüdiger S. G. D.³^ORCID,Drescher M.¹²^ORCID

Affiliation:

1. Department of Chemistry, University of Konstanz, 78457 Konstanz, Germany.

2. Konstanz Research School Chemical Biology (KoRS-CB), University of Konstanz, 78457 Konstanz, Germany.

3. Cellular Protein Chemistry, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht, Netherlands.

Abstract

The chaperone Hsp90 remodels the structural ensemble of Tau, resulting in the formation of potentially neurotoxic oligomers.

Funder

Deutsche Forschungsgemeinschaft

Internationale Stichting Alzheimer Onderzoek

ZonMW

FP7 Marie Curie Initial Training Network

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference62 articles.

1. Biochemistry and Cell Biology of Tau Protein in Neurofibrillary Degeneration

2. Tau in physiology and pathology

3. Near-atomic model of microtubule-tau interactions

4. Alzheimer’s and Parkinson’s diseases: The prion concept in relation to assembled Aβ, tau, and α-synuclein

5. Roles of tau protein in health and disease

Cited by 58 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Updates in Alzheimer's disease: from basic research to diagnosis and therapies;Translational Neurodegeneration;2024-09-04

2. Characterization of HSP90 expression and function following CNS injury;Neuroscience Letters;2024-07

3. Structural basis for the dynamic chaperoning of disordered clients by Hsp90;Nature Structural & Molecular Biology;2024-06-18

4. Chaperone-mediated heterotypic phase separation regulates liquid-to-solid phase transitions into amyloid fibrils;2024-06-16

5. Biochemical approaches to assess the impact of post-translational modifications on pathogenic tau conformations using recombinant protein;Biochemical Society Transactions;2024-02-13

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线，采集、加工和组织学术论文而形成的新型学术文献查询和分析系统，可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容，当前同舟云学术共收录了国内外主流学术期刊6万余种，收集的期刊论文及会议论文总量共计约1.5亿篇，并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询！咨询电话：010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号京ICP备18003416号-3