A current view on Tau protein phosphorylation in Alzheimer's disease
Current Opinion in Neurobiology, ISSN: 0959-4388, Vol: 69, Page: 131-138
2021
- 221Citations
- 459Captures
- 4Mentions
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Metrics Details
- Citations221
- Citation Indexes220
- 220
- CrossRef128
- Patent Family Citations1
- Patent Families1
- Captures459
- Readers459
- 459
- Mentions4
- News Mentions4
- News4
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Review Description
The functions of the neuronal microtubule-associated protein Tau in the central nervous system are regulated by manifold posttranslational modifications at more than 50 sites. Tau in healthy neurons carries multiple phosphate groups, mostly in its microtubule assembly domain. Elevated phosphorylation and aggregation of Tau are widely considered pathological hallmarks in Alzheimer’s disease (AD) and other tauopathies, triggering the quest for Tau posttranslational modifications in the disease context. However, the phosphorylation patterns of physiological and pathological Tau are surprisingly similar and heterogenous, making it difficult to identify specific modifications as therapeutic targets and biomarkers for AD. We present a concise summary of - and view on - important previous and recent advances in Tau phosphorylation analysis in the context of AD.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0959438821000222; http://dx.doi.org/10.1016/j.conb.2021.03.003; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85104484297&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/33892381; https://linkinghub.elsevier.com/retrieve/pii/S0959438821000222; https://dx.doi.org/10.1016/j.conb.2021.03.003
Elsevier BV
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