Evidence map›Paper›PMID 31268600›Full record

ArticleThe EMBO journal2019

Decreased synthesis of ribosomal proteins in tauopathy revealed by non-canonical amino acid labelling.

Harrison Tudor Evans, Joseph Benetatos, Marloes van Roijen, Liviu-Gabriel Bodea, Jürgen Götz

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
8.6field-weighted citation impact, top 2% of its field
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

75 citing papers in PubMed, 123 citations in OpenAlex.

  1. Bioorthogonal Chemistry in Neurobiology: From Imaging to Proteomics.Chembiochem : a European journal of chemical biology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. The multifaceted roles of ribosomal P complex in cancer.World journal of surgical oncology · 2025
    Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Organelle abnormalities in Alzheimer's disease.Organelle (Tucson, Ariz.) · 2025
    Article
  11. Article
  12. Review
  13. Cellular and pathological functions of tau.Nature reviews. Molecular cell biology · 2024
    Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. TauCell death & disease · 2024
    Article
  20. Review

15 more citing papers are in PubMed but not listed here.

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

5 authors at 2 institutions in 1 country.

Harrison Tudor EvansClem Jones Centre for Ageing Dementia Research, Queensland Brain Institute, The University of Queensland, Brisbane, Qld, Australia.ORCID 0000-0003-0322-0554
Joseph BenetatosClem Jones Centre for Ageing Dementia Research, Queensland Brain Institute, The University of Queensland, Brisbane, Qld, Australia.ORCID 0000-0001-8211-5642
Marloes van RoijenNew South Wales Brain Bank, The University of Sydney, Sydney, NSW, Australia.
Liviu-Gabriel BodeaClem Jones Centre for Ageing Dementia Research, Queensland Brain Institute, The University of Queensland, Brisbane, Qld, Australia.ORCID 0000-0002-9604-9524
Jürgen GötzClem Jones Centre for Ageing Dementia Research, Queensland Brain Institute, The University of Queensland, Brisbane, Qld, Australia.ORCID 0000-0001-8501-7896
The University of Queensland · AUThe University of Sydney · AU

Funding

Brain Tissue Resource Centre for Alcohol ResearchR28AA012725 · NIAAA · UNIVERSITY OF SYDNEY · PI Greg Trevor Sutherland · 2012 to 2026
$7.0M
Department of Education and Training | Australian Research Council (ARC) DP160103812Department of Health | National Health and Medical Research Council (NHMRC) GNT1127999Federal Government of Australia ACT900116National Institute of Alcohol Abuse and Alcoholism of the National Institutes of Health R28AA012725NIAAA NIH HHS R28 AA012725
6 · The paper itself

Abstract

Tau is a scaffolding protein that serves multiple cellular functions that are perturbed in neurodegenerative diseases, including Alzheimer's disease (AD) and frontotemporal dementia (FTD). We have recently shown that amyloid-β, the second hallmark of AD, induces de novo protein synthesis of tau. Importantly, this activation was found to be tau-dependent, raising the question of whether FTD-tau by itself affects protein synthesis. We therefore applied non-canonical amino acid labelling to visualise and identify newly synthesised proteins in the K369I tau transgenic K3 mouse model of FTD. This revealed massively decreased protein synthesis in neurons containing pathologically phosphorylated tau, a finding confirmed in P301L mutant tau transgenic rTg4510 mice. Using quantitative SWATH-MS proteomics, we identified changes in 247 proteins of the de novo proteome of K3 mice. These included decreased synthesis of the ribosomal proteins RPL23, RPLP0, RPL19 and RPS16, a finding that was validated in both K3 and rTg4510 mice. Together, our findings present a potential pathomechanism by which pathological tau interferes with cellular functions through the dysregulation of ribosomal protein synthesis.

Indexed as

Amino AcidsAnimalsDisease Models, AnimalFrontotemporal DementiaGene Expression RegulationHEK293 CellsHumansMiceMice, TransgenicMutationNeuronsPhosphorylationProteomicsRibosomal ProteinsStaining and Labelingtau ProteinsAmino AcidsMAPT protein, humanRibosomal Proteinstau Proteinsneurodegenerative diseasenon-canonical amino acid labellingprotein synthesisribosomal proteinstauopathy

Identifiers

PMID31268600
PMCPMC6600635
OpenAlexW2945882822

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.