Evidence map›Paper›PMID 27104579›Full record

ReviewBiomolecules2016

New Features about Tau Function and Dysfunction.

Miguel Medina, Félix Hernández, Jesús Avila

Abstract readReview
In one paragraph

Review in Biomolecules, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from 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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

53 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Review
  7. Article
  8. Tau reduction with artificial microRNAs modulates neuronal physiology and improves tauopathy phenotypes in mice.Molecular therapy : the journal of the American Society of Gene Therapy · 2024
    Article
  9. TBI and Tau Loss of Function Both Affect Naïve Ethanol Sensitivity inInternational journal of molecular sciences · 2024
    Article
  10. Review
  11. Review
  12. Review
  13. Chaperoning activity of the cyclophilin family prevents tau aggregation.Protein science : a publication of the Protein Society · 2022
    Article
  14. Review
  15. Review
  16. Three-repeat and four-repeat tau isoforms form different oligomers.Protein science : a publication of the Protein Society · 2022
    Article
  17. Article
  18. Hydrogen sulfide is neuroprotective in Alzheimer's disease by sulfhydrating GSK3β and inhibiting Tau hyperphosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Miguel MedinaCIBERNED (Centro de Investigación Biomédica en Red de Enfermedades Neurodegenerativas), Valderrebollo 5, 28031 Madrid, Spain. mmedina@ciberned.es.
Félix HernándezCIBERNED (Centro de Investigación Biomédica en Red de Enfermedades Neurodegenerativas), Valderrebollo 5, 28031 Madrid, Spain. fhernandez@cbm.csic.es.
Jesús AvilaCIBERNED (Centro de Investigación Biomédica en Red de Enfermedades Neurodegenerativas), Valderrebollo 5, 28031 Madrid, Spain. javila@cbm.csic.es.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tau is a brain microtubule-associated protein that directly binds to a microtubule and dynamically regulates its structure and function. Under pathological conditions, tau self-assembles into filamentous structures that end up forming neurofibrillary tangles. Prominent tau neurofibrillary pathology is a common feature in a number of neurodegenerative disorders, collectively referred to as tauopathies, the most common of which is Alzheimer's disease (AD). Beyond its classical role as a microtubule-associated protein, recent advances in our understanding of tau cellular functions have revealed novel insights into their important role during pathogenesis and provided potential novel therapeutic targets. Regulation of tau behavior and function under physiological and pathological conditions is mainly achieved through post-translational modifications, including phosphorylation, glycosylation, acetylation, and truncation, among others, indicating the complexity and variability of factors influencing regulation of tau toxicity, all of which have significant implications for the development of novel therapeutic approaches in various neurodegenerative disorders. A more comprehensive understanding of the molecular mechanisms regulating tau function and dysfunction will provide us with a better outline of tau cellular networking and, hopefully, offer new clues for designing more efficient approaches to tackle tauopathies in the near future.

Indexed as

Alzheimer DiseaseAnimalsAntibodies, MonoclonalHumansImmunotherapyMicroRNAsRisk Factorstau ProteinsAntibodies, MonoclonalMicroRNAstau ProteinsAlzheimer’s diseaseimmunotherapyneurodegenerationspreadingtautauopathies

Identifiers

PMID27104579
PMCPMC4919916

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

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.