Cited by 166Alzheimer's disease research and treatmentsAutophagy in Disease and TherapyUbiquitin and proteasome pathways

The DOI matches its Crossref record; 102 of the 102 references it cites were found in a registry or an index.

Degradation of tau protein by autophagy and proteasomal pathways

Wang, Yipeng, Mandelkow, Eckhard·2012·Biochemical Society Transactions

Abstract

Tau aggregates are present in several neurodegenerative diseases and correlate with the severity of memory deficit in AD (Alzheimer's disease). However, the triggers of tau aggregation and tau-induced neurodegeneration are still elusive. The impairment of protein-degradation systems might play a role in such processes, as these pathways normally keep tau levels at a low level which may prevent aggregation. Some proteases can process tau and thus contribute to tau aggregation by generating amyloidogenic fragments, but the complete clearance of tau mainly relies on the UPS (ubiquitin–proteasome system) and the ALS (autophagy–lysosome system). In the present paper, we focus on the regulation of the degradation of tau by the UPS and ALS and its relation to tau aggregation. We anticipate that stimulation of these two protein-degradation systems might be a potential therapeutic strategy for AD and other tauopathies.

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Crossref · 10.1042/bst20120071

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Metadata

Authors
Wang, Y., & Mandelkow, E.
Affiliations
  • German Center for Neurodegenerative Diseases (DE)
  • German Center for Neurodegenerative Diseases (DZNE), Bonn, Germany
Corresponding author
Wang, Yipeng
Venue
Biochemical Society Transactions
Published
2012-07-20
Volume
40
Issue
4
Pages
644-652
ISSN
  • 0300-5127 (ISSN-L)
  • 1470-8752
OpenAlex
W2149107089
Cited by
166
References
102
Citations by year
2026: 2 · 2025: 8 · 2024: 10 · 2023: 6 · 2022: 18 · 2021: 16 · 2020: 25 · 2019: 11 · 2018: 13 · 2017: 12 · 2016: 16 · 2015: 14 · 2014: 7 · 2013: 6 · 2012: 2
FWCI
0.98
Type
journal article
Language
en
Open access
closed
Locations
  • Biochemical Society Transactions (publishedVersion)
  • PubMed (publishedVersion)
  • Max Planck Institute for Plasma Physics (submittedVersion)
  • DZNE Pub (submittedVersion)
  • MPG.PuRe (Max Planck Society) (submittedVersion)
Funders
  • Wellcome Trust
  • Bundesministerium für Bildung und Forschung
  • Tau Consortium
  • Medical Research Council (MC_G1000734)
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords
tau protein, tau aggregation, protein degradation, ubiquitin-proteasome system, autophagy-lysosome system, Alzheimer's disease, tauopathy, neurodegeneration, proteolytic enzymes, therapeutic target
MeSH terms
Animals, Autophagy, Humans, Signal Transduction, tau Proteins, Proteasome Endopeptidase Complex

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