Advances in Tau Protein Research
A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biology".
Deadline for manuscript submissions: 20 June 2026 | Viewed by 1842
Special Issue Editor
Interests: tau biology; disease model systems; protein aggregation; tauopathies; neurodegeneration; Alzheimer’s disase; seeded aggregation; amyloid filaments; tau propagation; antibodies; targeted protein degradation; tau therapeutics
Special Issue Information
Dear Colleagues,
Alzheimer’s disease is the most common form of dementia, with the number of patients suffering from this incurable condition currently being estimated at over 57 million worldwide. Despite Alois Alzheimer describing the neurofibrillary tangles over 100 years ago, it was only in the late 1980s that they were shown to be composed of amyloid filaments assembled by hyperphosphorylated forms of the microtubule-associated protein tau. Interestingly, tau filament assemblies with different ultrastructural characteristics represent a key hallmark in various neurodegenerative conditions, collectively called tauopathies. About a decade later, the first mutations in the MAPT gene that encodes the tau protein in humans were reported to cause frontotemporal dementia and parkinsonism. Their discovery was a major milestone, as the disease-causing mutations together with the presence of filamentous tau inclusions suggest that the assembly of tau into filaments is sufficient to cause neurodegeneration. Notably, the emergence of the current hypotheses on the trans-cellular propagation of pathological tau species as a major determinant of disease progression stems from observations of the sequential deposition of aggregated tau species during disease progression as well as from experiments supporting the prion-like nature of such assemblies.
This Special Issue aims to advance our understanding of the physiological and pathological mechanisms around tau protein, including, among others, the interactions with cellular factors, the emerging therapeutic strategies, the molecular mechanisms of templated seeded aggregation, and the toxic functions of protein aggregates. Studies providing such information are welcomed and will help elucidate the molecular basis for the design of new treatments as well as the deeper understanding of protein aggregation pathologies.
Dr. Taxiarchis Katsinelos
Guest Editor
Manuscript Submission Information
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Keywords
- tau biology
- disease model systems
- protein aggregation
- tauopathies
- neurodegeneration
- Alzheimer’s disase
- seeded aggregation
- amyloid filaments
- tau propagation
- antibodies
- targeted protein degradation
- tau therapeutics
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