論文

査読有り
2014年11月

Phosphorylation regulates fibrillation of an aggregation core peptide in the second repeat of microtubule-binding domain of human tau

BIOORGANIC & MEDICINAL CHEMISTRY
  • Masafumi Inoue
  • ,
  • Shinji Kaida
  • ,
  • Shun Nakano
  • ,
  • Chiara Annoni
  • ,
  • Eiji Nakata
  • ,
  • Takashi Konno
  • ,
  • Takashi Morii

22
22
開始ページ
6471
終了ページ
6480
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1016/j.bmc.2014.09.032
出版者・発行元
PERGAMON-ELSEVIER SCIENCE LTD

Hyperphosphorylation of the microtubule-associated protein tau is believed to play a crucial role in the neurofibrillary tangles formation in Alzheimer's disease brain. In this study, fibril formation of peptides containing the critical sequences for tau aggregation VQIINK and a plausible serine phosphorylation site of tau at its C-terminal was investigated. All the peptides formed fibrils with the typical cross-beta structural core. However, stability of the fibrils was highly sensitive to the pH conditions for the phosphorylated VQIINK peptide, suggesting a regulatory role of phosphorylation for the amyloid-formation of tau. (C) 2014 Elsevier Ltd. All rights reserved.

Web of Science ® 被引用回数 : 8

リンク情報
DOI
https://doi.org/10.1016/j.bmc.2014.09.032
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/25440728
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000344472600018&DestApp=WOS_CPL
ID情報
  • DOI : 10.1016/j.bmc.2014.09.032
  • ISSN : 0968-0896
  • eISSN : 1464-3391
  • PubMed ID : 25440728
  • Web of Science ID : WOS:000344472600018

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