The DOI matches its Crossref record; 62 of the 62 references it cites were found in a registry or an index.
Amyloidogenesis of Tau protein
Open accessAbstract
The role of microtubule‐associated protein Tau in neurodegeneration has been extensively investigated since the discovery of Tau amyloid aggregates in the brains of patients with Alzheimer's disease (AD). The process of formation of amyloid fibrils is known as amyloidogenesis and attracts much attention as a potential target in the prevention and treatment of neurodegenerative conditions linked to protein aggregation. Cerebral deposition of amyloid aggregates of Tau is observed not only in AD but also in numerous other tauopathies and prion diseases. Amyloidogenesis of intrinsically unstructured monomers of Tau can be triggered by mutations in the Tau gene, post‐translational modifications, or interactions with polyanionic molecules and aggregation‐prone proteins/peptides. The self‐assembly of amyloid fibrils of Tau shares a number of characteristic features with amyloidogenesis of other proteins involved in neurodegenerative diseases. For example,in vitro experiments have demonstrated that the nucleation phase, which is the rate‐limiting stage of Tau amyloidogenesis, is shortened in the presence of fragmented preformed Tau fibrils acting as aggregation templates (“seeds”). Accordingly, Tau aggregates released by tauopathy‐affected neurons can spread the neurodegenerative process in the brain through a prion‐like mechanism, originally described for the pathogenic form of prion protein. Moreover, Tau has been shown to form amyloid strains—structurally diverse self‐propagating aggregates of potentially various pathological effects, resembling in this respect prion strains. Here, we review the current literature on Tau aggregation and discuss mechanisms of propagation of Tau amyloid in the light of the prion‐like paradigm.
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Cites
Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17
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Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders
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Reducing Endogenous Tau Ameliorates Amyloid ß-Induced Deficits in an Alzheimer's Disease Mouse Model
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Dendritic Function of Tau Mediates Amyloid-β Toxicity in Alzheimer's Disease Mouse Models
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Transmission and spreading of tauopathy in transgenic mouse brain
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Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
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Tau is a candidate gene for chromosome 17 frontotemporal dementia
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Propagation of Tau Misfolding from the Outside to the Inside of a Cell
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Human ApoE isoforms differentially regulate brain amyloid-β peptide clearance
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Tau pathology in Alzheimer disease and other tauopathies
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Cited by
Nguyen, P. H., Ramamoorthy, A., Sahoo, B. R., Zheng, J., Faller, P., Straub, J. E., Dominguez, L., Shea, J.-E., Dokholyan, N. V., De Simone, A., et al. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01122 · Cited by 678
Multicomponent peptide assemblies
Raymond, D. M., & Nilsson, B. L. (2018) · Chemical Society Reviews · doi:10.1039/c8cs00115d · Cited by 346
Cooper, J. M., Lathuiliere, A., Migliorini, M., Arai, A. L., Wani, M. M., Dujardin, S., Muratoglu, S. C., Hyman, B. T., & Strickland, D. K. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100715 · Cited by 122
Alzheimer’s disease as type 3 diabetes: understanding the link and implications
Kciuk, M., Kruczkowska, W., Gałęziewska, J., Wanke, K., Kałuzińska-Kołat, Ż., Aleksandrowicz, M., & Kontek, R. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252211955 · Cited by 98
(2019) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2019.08.002 · Cited by 78
Metadata
- Authors
- Nizynski, B., Dzwolak, W., & Nieznanski, K.
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 2017-09-13
- Volume
- 26
- Issue
- 11
- Pages
- 2126-2150
- ISSN
- 0961-8368 (ISSN-L)
- 1469-896X
- OpenAlex
- W2748622848
- Cited by
- 162
- References
- 62
- FWCI
- 7.21
- Type
- journal article
- Language
- en
- Open access
- bronze
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