Evidence map›Paper›PMID 32096049›Full record

ReviewAdvances in experimental medicine and biology2019

The Pathophysiology of Tau and Stress Granules in Disease.

Anna Cruz, Mamta Verma, Benjamin Wolozin

Abstract readReview
In one paragraph

Review in Advances in experimental medicine and biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing 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

34 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Nanobodies targeting hnRNPA2/B1 and tau.bioRxiv : the preprint server for biology · 2025
    Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Nuclear face of Tau: an inside player in neurodegeneration.Acta neuropathologica communications · 2023
    Review
  17. Article
  18. Review
  19. Article
  20. Cytosolic condensates rich in polyserine define subcellular sites of tau aggregation.Proceedings of the National Academy of Sciences of the United States of America · 2023
    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.

Anna CruzDepartment of Pharmacology and Experimental Therapeutics, Boston University School of Medicine, Boston, MA, USA.
Mamta VermaDepartment of Pharmacology and Experimental Therapeutics, Boston University School of Medicine, Boston, MA, USA.
Benjamin WolozinDepartment of Pharmacology and Experimental Therapeutics, Boston University School of Medicine, Boston, MA, USA. bwolozin@bu.edu.

Funding

Capturing the molecular complexity of Alzheimer's disease through the lens of RNA binding proteinsRF1AG056318 · NIA · BOSTON UNIVERSITY MEDICAL CAMPUS · PI LI, HU, WOLOZIN, BENJAMIN L · 2018 to 2020
$4.4M
Systems-level functional proteomics analysis assemblies in Alzheimer's disease and mouse models of tauopathyRF1AG061706 · NIA · BOSTON UNIVERSITY MEDICAL CAMPUS · PI EMILI, ANDREW, WOLOZIN, BENJAMIN L · 2019 to 2019
$3.9M
Genetic Modifiers of Protein Interaction Networks in TauopathyR01AG064932 · NIA · BOSTON UNIVERSITY MEDICAL CAMPUS · PI EMILI, ANDREW, WOLOZIN, BENJAMIN L · 2019 to 2023
$3.2M
RNA binding proteins as novel targets in Alzheimer's diseaseR01AG050471 · NIA · BOSTON UNIVERSITY MEDICAL CAMPUS · PI WOLOZIN, BENJAMIN L · 2015 to 2019
$2.9M
The role of acetylation in regulating pathophysiology of tauR01NS089544 · NINDS · MAYO CLINIC JACKSONVILLE · PI PETRUCELLI, LEONARD, WOLOZIN, BENJAMIN L · 2014 to 2018
$1.9M
Regulation of brain neuroprotection and inflammation by TIA1R21AG059925 · NIA · BOSTON UNIVERSITY MEDICAL CAMPUS · PI WOLOZIN, BENJAMIN L · 2018 to 2019
$454k
NIA NIH HHS R01 AG050471NIA NIH HHS R01 AG064932NIA NIH HHS R21 AG059925NIA NIH HHS RF1 AG056318NIA NIH HHS RF1 AG061706NINDS NIH HHS R01 NS089544
6 · The paper itself

Abstract

This chapter discusses the relationship between tau, RNA binding proteins and stress granules, which exhibit an intimate bidirectional relationship affecting the functions of both tau and the translational stress response. We describe how tau becomes hyperphosphorylated and oligomerized as part of an endogenous mechanism to promote the translational stress response through interaction with RNA binding proteins. Prior studies demonstrate that dysfunction of RNA binding proteins biology is sufficient to cause neurodegenerative diseases, such as amyotrophic lateral sclerosis and frontotemporal dementia. Emerging evidence indicates that tau-mediated neurodegeneration also occurs through a mechanism that is mediated by RNA binding proteins and the translational stress response. Discovery of the role of RNA metabolism in tauopathy opens a wide variety of novel therapeutic approaches. Multiple studies have already shown that approaches reducing the levels of selected RNA binding proteins or inhibiting the translational stress response can intervene in the pathophysiology of motoneuron diseases. Emerging studies show that reducing the levels of selected RNA binding proteins or inhibiting the translational stress response also reduces neurodegeneration in models of tauopathy and Aβ mediated degeneration. The combined impact of these studies indicate that RNA binding proteins and RNA metabolism represent a valuable new frontier for the investigation and treatment tauopathies.

Indexed as

Amyotrophic Lateral SclerosisCytoplasmic GranulesHumansNeurodegenerative DiseasesRNA-Binding ProteinsTauopathiestau ProteinsRNA-Binding Proteinstau Proteins

Identifiers

PMID32096049
PMCPMC8265570

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.