ArticleScientific reports2015
Rescue from tau-induced neuronal dysfunction produces insoluble tau oligomers.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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
20 citing papers in PubMed, 40 citations in OpenAlex.
- Machine Learning Interpretation of Optical Spectroscopy Using Peak-Sensitive Logistic Regression.ACS nano · 2025Article
- A novel peptide-based tau aggregation inhibitor as a potential therapeutic for Alzheimer's disease and other tauopathies.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2024Article
- Human Tau Aggregates Are Permissive to Protein Synthesis-Dependent Memory inThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2023Article
- Hyperphosphorylated tau (p-tau) and drug discovery in the context of Alzheimer's disease and related tauopathies.Drug discovery today · 2023Review
- String/Cdc25 phosphatase is a suppressor of Tau-associated neurodegeneration.Disease models & mechanisms · 2023Article
- A 3D-induced pluripotent stem cell-derived human neural culture model to study certain molecular and biochemical aspects of Alzheimer's disease.In vitro models · 2022Article
- Amyloid-Driven Tau Accumulation on Mitochondria Potentially Leads to Cognitive Deterioration in Alzheimer's Disease.International journal of molecular sciences · 2021Article
- Article
- The Two Cysteines of Tau Protein Are Functionally Distinct and Contribute Differentially to Its PathogenicityThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2021Article
- Tau Oligomers Neurotoxicity.Life (Basel, Switzerland) · 2021Review
- CSF1R inhibitor JNJ-40346527 attenuates microglial proliferation and neurodegeneration in P301S mice.Brain : a journal of neurology · 2019Article
- Insulin-Mediated Changes in Tau Hyperphosphorylation and Autophagy in aFrontiers in neuroscience · 2019Article
- Tau-mediated synaptic and neuronal dysfunction in neurodegenerative disease.Current opinion in neurobiology · 2018Review
- Potentiating tangle formation reduces acute toxicity of soluble tau species in the rat.Brain : a journal of neurology · 2018Article
- Targeting Prion-like Cis Phosphorylated Tau Pathology in Neurodegenerative Diseases.Journal of Alzheimer's disease & Parkinsonism · 2018Article
- What is the evidence that tau pathology spreads through prion-like propagation?Acta neuropathologica communications · 2017Review
- Amyloidogenesis of Tau protein.Protein science : a publication of the Protein Society · 2017Review
- Microtubule stabilising peptides rescue tau phenotypes in-vivo.Scientific reports · 2016Article
- Uncoupling neuronal death and dysfunction in Drosophila models of neurodegenerative disease.Acta neuropathologica communications · 2016Article
- Potential mechanisms and implications for the formation of tau oligomeric strains.Critical reviews in biochemistry and molecular biologyReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Aggregation of highly phosphorylated tau is a hallmark of Alzheimer's disease and other tauopathies. Nevertheless, animal models demonstrate that tau-mediated dysfunction/toxicity may not require large tau aggregates but instead may be caused by soluble hyper-phosphorylated tau or by small tau oligomers. Challenging this widely held view, we use multiple techniques to show that insoluble tau oligomers form in conditions where tau-mediated dysfunction is rescued in vivo. This shows that tau oligomers are not necessarily always toxic. Furthermore, their formation correlates with increased tau levels, caused intriguingly, by either pharmacological or genetic inhibition of tau kinase glycogen-synthase-kinase-3beta (GSK-3β). Moreover, contrary to common belief, these tau oligomers were neither highly phosphorylated, and nor did they contain beta-pleated sheet structure. This may explain their lack of toxicity. Our study makes the novel observation that tau also forms non-toxic insoluble oligomers in vivo in addition to toxic oligomers, which have been reported by others. Whether these are inert or actively protective remains to be established. Nevertheless, this has wide implications for emerging therapeutic strategies such as those that target dissolution of tau oligomers as they may be ineffective or even counterproductive unless they act on the relevant toxic oligomeric tau species.
Indexed as
Identifiers
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.