Aggregation Kinetics and Filament Structure of a Tau Fragment Are Influenced by the Sulfation Pattern of the Cofactor Heparin
Open Access
- 21 September 2020
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 59 (41), 4003-4014
- https://doi.org/10.1021/acs.biochem.0c00443
Abstract
No abstract availableKeywords
Funding Information
- Biotechnology and Biological Sciences Research Council (BB/K015958/1)
This publication has 48 references indexed in Scilit:
- Synthetic Tau Fibrils Mediate Transmission of Neurofibrillary Tangles in a Transgenic Mouse Model of Alzheimer's-Like TauopathyJournal of Neuroscience, 2013
- The fuzzy coat of pathological human Tau fibrils is a two-layered polyelectrolyte brushProceedings of the National Academy of Sciences of the United States of America, 2012
- β-Sheet Core of Tau Paired Helical Filaments Revealed by Solid-State NMRJournal of the American Chemical Society, 2012
- Trans-cellular Propagation of Tau Aggregation by Fibrillar SpeciesOnline Journal of Public Health Informatics, 2012
- Understanding the Kinetic Roles of the Inducer Heparin and of Rod-like Protofibrils during Amyloid Fibril Formation by Tau ProteinOnline Journal of Public Health Informatics, 2011
- Quantitative Characterization of Heparin Binding to Tau ProteinOnline Journal of Public Health Informatics, 2010
- Influence of substitution pattern and cation binding on conformation and activity in heparin derivativesGlycobiology, 2007
- Characterization of paired helical filaments by scanning transmission electron microscopyMicroscopy Research and Technique, 2005
- Tau pathology in Alzheimer disease and other tauopathiesBiochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 2005
- Polymerization of τ into Filaments in the Presence of Heparin: The Minimal Sequence Required for τ ‐ τ InteractionJournal of Neurochemistry, 1996