Flipping the switch: How cysteine oxidation directs tau amyloid conformations
Open Access
- 15 October 2021
- journal article
- editorial
- Published by Elsevier BV in Online Journal of Public Health Informatics
- Vol. 297 (5), 101309
- https://doi.org/10.1016/j.jbc.2021.101309
Abstract
No abstract availableFunding Information
- National Health and Medical Research Council (APP1154352)
This publication has 10 references indexed in Scilit:
- A thiol-based intramolecular redox switch in four-repeat tau controls fibril assembly and disassemblyOnline Journal of Public Health Informatics, 2021
- Tau: A Signaling Hub ProteinFrontiers in Molecular Neuroscience, 2021
- Novel tau filament fold in corticobasal degenerationNature, 2020
- Propagation of Protein Aggregation in Neurodegenerative DiseasesAnnual Review of Biochemistry, 2019
- Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic moleculesNature, 2019
- Structures of filaments from Pick’s disease reveal a novel tau protein foldNature, 2018
- Cryo-EM structures of tau filaments from Alzheimer’s diseaseNature, 2017
- Tau Hyperphosphorylation and Oxidative Stress, a Critical Vicious Circle in Neurodegenerative Tauopathies?Oxidative Medicine and Cellular Longevity, 2015
- Assembly of two distinct dimers and higher‐order oligomers from full‐length tauEuropean Journal of Neuroscience, 2007
- Role of Cysteine-291 and Cysteine-322 in the Polymerization of Human Tau into Alzheimer-like FilamentsBiochemical and Biophysical Research Communications, 2001