ArticleBiochemistry2015
Ion Channel Formation by Tau Protein: Implications for Alzheimer's Disease and Tauopathies.
Article in Biochemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
24 citing papers in PubMed, 1 synthesis or guideline pooled it, 50 citations in OpenAlex.
- Cortical excitability and plasticity in Alzheimer's disease and mild cognitive impairment: A systematic review and meta-analysis of transcranial magnetic stimulation studies.Ageing research reviews · 2022Pooled it
- Cryo-EM structural analyses reveal diverse porous structures in brain-derived tau oligomers.Biochemical and biophysical research communications · 2025Article
- Single-molecule imaging reveals Tau trapping at nanometer-sized dynamic hot spots near the plasma membrane that persists after microtubule perturbation and cholesterol depletion.The EMBO journal · 2022Article
- Hyperphosphorylated tau self-assembles into amorphous aggregates eliciting TLR4-dependent responses.Nature communications · 2022Article
- Review
- The Fate of Tau Aggregates Between Clearance and Transmission.Frontiers in aging neuroscience · 2022Review
- Insights into the Pathogenesis of Neurodegenerative Diseases: Focus on Mitochondrial Dysfunction and Oxidative Stress.International journal of molecular sciences · 2021Review
- Synaptic tau: A pathological or physiological phenomenon?Acta neuropathologica communications · 2021Review
- Membrane interaction and disulphide-bridge formation in the unconventional secretion of Tau.Bioscience reports · 2021Article
- Interaction of Tau construct K18 with model lipid membranes.Nanoscale advances · 2021Article
- Increased Signal Delays and Unaltered Synaptic Input Pattern Recognition in Layer III Neocortical Pyramidal Neurons of the rTg4510 Mouse Model of Tauopathy: A Computer Simulation Study With Passive Membrane.Frontiers in neuroscience · 2021Article
- Tau and Membranes: Interactions That Promote Folding and Condensation.Frontiers in cell and developmental biology · 2021Review
- Review
- Half a century of amyloids: past, present and future.Chemical Society reviews · 2020Review
- High-Speed Atomic Force Microscopy Reveals the Structural Dynamics of the Amyloid-β and Amylin Aggregation Pathways.International journal of molecular sciences · 2020Review
- Mechanisms of secretion and spreading of pathological tau protein.Cellular and molecular life sciences : CMLS · 2020Review
- Mechanisms of Pathogenic Tau and Aβ Protein Spreading in Alzheimer's Disease.Frontiers in aging neuroscience · 2020Review
- The Cell Biology of Tau Secretion.Frontiers in molecular neuroscience · 2020Review
- Electrostatics of Tau Protein by Molecular Dynamics.Biomolecules · 2019Article
- Primate retinal cones express phosphorylated tau associated with neuronal degeneration yet survive in old age.Experimental eye research · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Tau is a microtubule associated protein implicated in the pathogenesis of several neurodegenerative diseases. Because of the channel forming properties of other amyloid peptides, we employed planar lipid bilayers and atomic force microscopy to test tau for its ability to form ion permeable channels. Our results demonstrate that tau can form such channels, but only under acidic conditions. The channels formed are remarkably similar to amyloid peptide channels in their appearance, physical and electrical size, permanence, lack of ion selectivity, and multiple channel conductances. These channels differ from amyloid channels in their voltage dependence and resistance to blockade by zinc ion. These channels could explain tau's pathologic role in disease by lowering membrane potential, dysregulating calcium, depolarizing mitochondria, or depleting energy stores. Tau might also combine with amyloid beta peptides to form toxic channels.
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What OpenQuestion holds
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.