ReviewFrontiers in neurology2020
Cellular Biology of Tau Diversity and Pathogenic Conformers.
Review in Frontiers in neurology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
18 citing papers in PubMed, 23 citations in OpenAlex.
- "S-Tau-Lled" Lysosomes Disrupt Autophagic Processes in Neurodegeneration.Traffic (Copenhagen, Denmark) · 2026Article
- Nuclear Speckle Protein SRRM2 Co-localized with Pathological Tau (pTauS396) in Neuronal and Glial Cells in Progressive Supranuclear Palsy.Acta histochemica et cytochemica · 2026Article
- Nuclear tau aggregates inhibit RNA export and form by secondary seeding from cytosolic tau aggregates.bioRxiv : the preprint server for biology · 2026Article
- Investigation of Thiazolidine-2,4-Dione Derivatives as Acetylcholinesterase Inhibitors: Synthesis, In Vitro Biological Activities and In Silico Studies.ChemistryOpen · 2025Article
- Effects of Heparan Sulfate Trisaccharide Containing Oleanolic Acid in Attenuating Hyperphosphorylated Tau-Induced Cell Dysfunction Associated with Alzheimer's Disease.Journal of medicinal chemistry · 2025Article
- Non-enzymatic posttranslational protein modifications in protein aggregation and neurodegenerative diseases.RSC chemical biology · 2025Review
- Cytosolic phospholipase A2 links tau pathology to insulin signaling impairment in Alzheimer's disease.Frontiers in aging neuroscience · 2025Article
- Oligomeric Tau-induced oxidative damage and functional alterations in cerebral endothelial cells: Role of RhoA/ROCK signaling pathway.Free radical biology & medicine · 2024Article
- Genome-wide association studies identify novel loci in rapidly progressive Alzheimer's disease.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2024Article
- Biochemical approaches to assess the impact of post-translational modifications on pathogenic tau conformations using recombinant protein.Biochemical Society transactions · 2024Review
- Evolving prion-like tau conformers differentially alter postsynaptic proteins in neurons inoculated with distinct isolates of Alzheimer's disease tau.Cell & bioscience · 2023Article
- Prion-like strain effects in tauopathies.Cell and tissue research · 2023Review
- Single-nucleus chromatin accessibility profiling highlights distinct astrocyte signatures in progressive supranuclear palsy and corticobasal degeneration.Acta neuropathologica · 2022Article
- Populations of Tau Conformers Drive Prion-like Strain Effects in Alzheimer's Disease and Related Dementias.Cells · 2022Review
- Phosphorylated tau as a toxic agent in synaptic mitochondria: implications in aging and Alzheimer's disease.Neural regeneration research · 2022Review
- Pathologic tau conformer ensembles induce dynamic, liquid-liquid phase separation events at the nuclear envelope.BMC biology · 2021Article
- Structurally distinct external solvent-exposed domains drive replication of major human prions.PLoS pathogens · 2021Article
- Tau: A Signaling Hub Protein.Frontiers in molecular neuroscience · 2021Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Tau accumulation is a prominent feature in a variety of neurodegenerative disorders and remarkable effort has been expended working out the biochemistry and cell biology of this cytoplasmic protein. Tau's wayward properties may derive from germline mutations in the case of frontotemporal lobar degeneration (FTLD-MAPT) but may also be prompted by less understood cues-perhaps environmental or from molecular damage as a consequence of chronological aging-in the case of idiopathic tauopathies. Tau properties are undoubtedly affected by its covalent structure and in this respect tau protein is not only subject to changes in length produced by alternative splicing and endoproteolysis, but different types of posttranslational modifications that affect different amino acid residues. Another layer of complexity concerns alternate conformations-"conformers"-of the same covalent structures;
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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.