Structural insights into Alzheimer filament assembly pathways based on site-directed mutagenesis andS-glutathionylation of three-repeat neuronal Tau protein-Reference-Cited by-同舟云学术

Structural insights into Alzheimer filament assembly pathways based on site-directed mutagenesis andS-glutathionylation of three-repeat neuronal Tau protein

Published:2005 Issue:3-4 Volume:67 Page:156-163
ISSN:1059-910X
Container-title:Microscopy Research and Technique
language:en
Short-container-title:Microsc. Res. Tech.

Author:

Dinoto Luca,Deture Michael A.,Purich Daniel L.

Publisher

Wiley

Subject

Medical Laboratory Technology,Instrumentation,Histology,Anatomy

Reference65 articles.

1. Structure, Microtubule Interactions, and Paired Helical Filament Aggregation by Tau Mutants of Frontotemporal Dementias

2. Conformational changes and disease — serpins, prions and Alzheimer's

3. The Microtubule-Associated Protein Tau Cross-Links to Two Distinct Sites on Each α and β Tubulin Monomer via Separate Domains

4. Anionic Micelles and Vesicles Induce Tau Fibrillization in Vitro

5. Dithiothreitol, a New Protective Reagent for SH Groups*

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