ReviewCellular and molecular neurobiology
Intrinsically disordered proteins in the neurodegenerative processes: formation of tau protein paired helical filaments and their analysis.
Review in Cellular and molecular neurobiology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 71 citations in OpenAlex.
- Prospect in Alzheimer's disease integrative therapy targeting both amyloid-beta and tau.Neural regeneration research · 2026Article
- Tau Oligomers Resist Phase Separation.Biomolecules · 2025Article
- Molecular Mechanism of Tau Misfolding and Aggregation: Insights from Molecular Dynamics Simulation.Current medicinal chemistry · 2024Review
- Tau Lysine Pseudomethylation Regulates Microtubule Binding and Enhances Prion-like Tau Aggregation.International journal of molecular sciences · 2023Article
- Therapeutic strategies for tauopathies and drug repurposing as a potential approach.Biochemical pharmacology · 2022Review
- Effect of Trehalose and Ceftriaxone on the Stability of Aggregating-Prone Tau Peptide Containing PHF6* Sequence: An SRCD Study.International journal of molecular sciences · 2022Article
- CSF p-tau as a potential cognition impairment biomarker in ALS.Frontiers in neurology · 2022Article
- Mechanism by Which Aluminum Regulates the Abnormal Phosphorylation of the Tau Protein in Different Cell Lines.ACS omega · 2021Article
- Effect of the micro-environment on α-synuclein conversion and implication in seeded conversion assays.Translational neurodegeneration · 2020Review
- Impaired tau-microtubule interactions are prevalent among pathogenic tau variants arising from missense mutations.The Journal of biological chemistry · 2019Article
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- A walk through tau therapeutic strategies.Acta neuropathologica communications · 2019Review
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- AADvac1, an Active Immunotherapy for Alzheimer's Disease and Non Alzheimer Tauopathies: An Overview of Preclinical and Clinical Development.The journal of prevention of Alzheimer's disease · 2019Review
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- Amyloidogenesis of Tau protein.Protein science : a publication of the Protein Society · 2017Review
- Implications of peptide assemblies in amyloid diseases.Chemical Society reviews · 2017Review
- The Ubiquitin-Proteasome System and Molecular Chaperone Deregulation in Alzheimer's Disease.Molecular neurobiology · 2016Review
- Tau Structures.Frontiers in aging neuroscience · 2016Review
- Ion Channel Formation by Tau Protein: Implications for Alzheimer's Disease and Tauopathies.Biochemistry · 2015Article
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
1. Several intrinsically disordered proteins (IDPs) play principal role in the neurodegenerative processes of various types. Among them, alpha-synuclein is involved in Parkinson's disease, prion protein in transmissible spongiform encephalopathies, and tau protein in Alzheimer's disease (AD) and related tauopathies. Neuronal damage in AD is accompanied by the presence of tau protein fibrils composed of paired helical filaments (PHF). 2. Tau protein represents a typical IDP. IDPs do not exhibit any stable secondary structure in the free form, but they are able to fold after binding to targets and contain regions with large propensity to adopt a defined type of secondary structure. Binding-folding event at tau protein leading to PHF generation is believed to happen in the course of tauopathies. 3. Detailed molecular topology of PHF formation is unknown. There are evidences about the cross-beta structure in PHF core; however the precise arrangement of the tau polypeptide chain is unclear. In this review we summarize current attempts at in vitro PHF reconstruction and the development of methods for PHF structure determination. The emphasis is put on the monoclonal antibodies used as structural molecular probes for research on the role of IDPs in pathogenesis of neurodegenerative diseases.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.