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Tau and tauopathies
Abstract
Most neurodegenerative diseases are characterized by intracellular aggregates of insoluble proteins. As for the majority of these disorders, aetiology and pathogenesis are only poorly understood; current nosological concepts are largely based on these molecular signatures of protein aggregates which also provide valuable tools for neuropathological differential diagnosis. The microtubule associated protein tau is one of these proteins that form intracellular fibrillary deposits in neurons and glial cells of a large variety of disorders today collectively referred to as tauopathies. While dysfunction of tau has unequivocally been shown to be able to cause neurodegeneration, the precise mechanisms of how tau is involved in neurodegenerative disorders is still poorly understood. After research has focused for several decades on the axonal function of tau and on the fibrillar tau aggregation, more recent cell biological studies have opened up new insights into the role of tau at the synapse and in the nucleus. According to currently emerging cell biological concepts, tau might play a role in the regulation of neuronal plasticity in a wide array of neuronal networks. In addition, it might be involved in regulating genome stability. The most intriguing question relevant both to physiological and pathophysiological function of tau is the biological meaning of the large heterogeneity of isoforms of tau which apparently is a rather promiscuous molecule. The present review is divided into two parts. First, we give an overview on the molecular biology and cell biology of tau and its physiological functions. The second part deals with the pathophysiology of tau and description of tauopathies which comprise more than 20 disorders including Alzheimer's disease, progressive supranuclear palsy, cortico basal degeneration, Pick's disease and others.
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“Aggregates composed of both 3R and 4R tau are seen in disease states, though curiously several tauopathies including PSP, CBD, FTDP-17, and AGD exclusively feature 4R tau deposits.”
From Glial contributions to neurodegeneration in tauopathies (2017) · cites this paper as [2]
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Metadata
- Authors
- Arendt, T., Stieler, J. T., & Holzer, M.
- Affiliations
- Leipzig University (DE)
- Corresponding author
- Arendt, Thomas
- Venue
- Brain Research Bulletin
- Publisher
- Elsevier BV
- Published
- 2016-09
- Volume
- 126
- Issue
- Pt 3
- Pages
- 238-292
- ISSN
- 0361-9230 (ISSN-L)
- OpenAlex
- W2519516239
- Cited by
- 609
- References
- 1,115
- Citations by year
- 2026: 34 · 2025: 62 · 2024: 75 · 2023: 65 · 2022: 80 · 2021: 74 · 2020: 74 · 2019: 48 · 2018: 46 · 2017: 49 · 2016: 1
- FWCI
- 5.63
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Brain Research Bulletin (publishedVersion)
- PubMed (publishedVersion)
- Funders
- DFG (AR 200/17-1, HO2368-4/1)
- Era Net Rus Plus (DLR/01DJ16018)
- Fritz Thyssen Foundation
- EU funds (100111005)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- tau protein, tauopathy, neurodegeneration, protein aggregation, synapses, neuroplasticity, genome stability, tau isoforms, Alzheimer's disease, progressive supranuclear palsy, corticobasal degeneration, Pick's disease
- MeSH terms
- Animals, Humans, tau Proteins, Tauopathies
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