Bibliographic Citation
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DOI | 10.1016/j.bbrc.2006.07.099 |
Title | The self-assembly ability of First microtubule-binding repeat from tau and its modulation by phosphorylation |
Creator/Author | Zhou Lianxiu [Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084 (China)] ; Zeng Zhiyang [Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084 (China)] ; Du Jintang [Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084 (China)] ; Zhao Yufen [Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084 (China)] ; Li Yanmei [Key Laboratory of Bioorganic Phosphorus Chemistry and Chemical Biology (Ministry of Education), Department of Chemistry, Tsinghua University, Beijing 100084 (China)]. E-mail: liym@mail.tsinghua.edu.cn |
Publication Date | 2006 Sep 22 |
OSTI Identifier | OSTI ID: 20854476 |
Other Number(s) | Journal ID: ISSN 0006-291X; BBRCA9; TRN: US07R0251027466 |
Resource Type | Journal Article |
Resource Relation | Journal: Biochemical and Biophysical Research Communications; Journal Volume: 348; Journal Issue: 2; Other Information: DOI: 10.1016/j.bbrc.2006.07.099; PII: S0006-291X(06)01660-3; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA) |
Subject | 60 APPLIED LIFE SCIENCES; DICHROISM; ELECTRON MICROSCOPY; FILAMENTS; MICROTUBULES; MODULATION; NERVOUS SYSTEM DISEASES; NUCLEAR MAGNETIC RESONANCE; PEPTIDES; PHOSPHORYLATION; SPECTROSCOPY; TOXICITY |
Description/Abstract | Aggregation of abnormally phosphorylated tau in the form of tangs of paired helical filaments (PHFs) is one of the hallmarks of Alzheimer's disease (AD) and other tauopathies. It is of fundamental importance to study the mechanism of PHF formation and its modulation by phosphorylation. In this work, we have focused on First microtubule-binding repeat of tau encompassing an abnormal phosphorylation site Ser{sup 262}. The assembly propensities of this repeat and its corresponding phosphorylated form were investigated by turbidity and electron microscopy. Additionally, conformation of the two peptides is also analyzed through circular dichroism (CD) and NMR spectroscopy. Our results reveal that both of them are capable of self-assembly and phosphorylation at Ser{sup 262} could speed up the process of assembly. A possible mechanism of PHF formation is proposed and enhancing effect of phosphorylation on assembly provides an explanation to its toxicity in Alzheimer's disease. |
Country of Publication | United States |
Language | English |
Format | Size: page(s) 637-642 |
System Entry Date | 2007 Apr 23 |
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