Evidence map›Paper›PMID 24879160›Full record

ArticleAutophagy2014

A histone point mutation that switches on autophagy.

Tobias Eisenberg, Sabrina Schroeder, Sabrina Büttner, Didac Carmona-Gutierrez, Tobias Pendl, Aleksandra Andryushkova, Guillermo Mariño, Federico Pietrocola, Alexandra Harger, Andreas Zimmermann and 8 more

Open access · hybridAbstract readComment
In one paragraph

Article in Autophagy, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

17 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. NOP53 Suppresses Autophagy throughInternational journal of molecular sciences · 2021
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Mitochondrial health, the epigenome and healthspan.Clinical science (London, England : 1979) · 2016
    Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Rewiring yeast acetate metabolism throughMicrobial cell (Graz, Austria) · 2014
    Article
  17. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

18 authors at 6 institutions in 5 countries.

Tobias EisenbergInstitute of Molecular Biosciences; University of Graz; Graz, Austria.
Sabrina SchroederInstitute of Molecular Biosciences; University of Graz; Graz, Austria.
Sabrina BüttnerInstitute of Molecular Biosciences; University of Graz; Graz, Austria.
Didac Carmona-GutierrezInstitute of Molecular Biosciences; University of Graz; Graz, Austria.
Tobias PendlInstitute of Molecular Biosciences; University of Graz; Graz, Austria.
Aleksandra AndryushkovaInstitute of Molecular Biosciences; University of Graz; Graz, Austria.
Guillermo MariñoINSERM U848; Pavillon de Recherche 1; Villejuif, France; Metabolomics and Cell Biology Platforms; Institut Gustave Roussy; Pavillon de Recherche 1; Villejuif, France; Université Paris Sud, Faculté de Médecine; Le Kremlin Bicêtre; Paris, France.
Federico PietrocolaINSERM U848; Pavillon de Recherche 1; Villejuif, France; Metabolomics and Cell Biology Platforms; Institut Gustave Roussy; Pavillon de Recherche 1; Villejuif, France; Université Paris Sud, Faculté de Médecine; Le Kremlin Bicêtre; Paris, France.
Alexandra HargerInstitute of Molecular Biosciences; University of Graz; Graz, Austria; Division of Endocrinology and Metabolism; Department of Internal Medicine; Medical University of Graz; Graz, Austria.
Andreas ZimmermannInstitute of Molecular Biosciences; University of Graz; Graz, Austria.
Christoph MagnesHEALTH-Institute for Biomedicine and Health Sciences; Joanneum Research Forschungsgesellschaft m.b.H.; Graz, Austria.
Frank SinnerDivision of Endocrinology and Metabolism; Department of Internal Medicine; Medical University of Graz; Graz, Austria; HEALTH-Institute for Biomedicine and Health Sciences; Joanneum Research Forschungsgesellschaft m.b.H.; Graz, Austria.
Simon SedejDepartment of Cardiology; Medical University of Graz; Graz, Austria.
Thomas R PieberDivision of Endocrinology and Metabolism; Department of Internal Medicine; Medical University of Graz; Graz, Austria; HEALTH-Institute for Biomedicine and Health Sciences; Joanneum Research Forschungsgesellschaft m.b.H.; Graz, Austria.
Jörn DengjelDepartment of Dermatology; University Freiburg Medical Center; Freiburg, Germany.
Stephan SigristInstitute for Biology/Genetics; Freie Universität; Berlin, Germany; NeuroCure, Charité; Berlin, Germany.
Guido KroemerINSERM U848; Pavillon de Recherche 1; Villejuif, France; Metabolomics and Cell Biology Platforms; Institut Gustave Roussy; Pavillon de Recherche 1; Villejuif, France; Université Paris Sud, Faculté de Médecine; Le Kremlin Bicêtre; Paris, France; Equipe 11 Labellisée Ligue Contre le Cancer; INSERM U1138; Centre de Recherche des Cordeliers; Paris, France; Pôle de Biologie; Hôpital Européen Georges Pompidou; AP-HP; Paris, France; Université Paris Descartes; Sorbonne Paris Cité; Paris, France.
Frank MadeoInstitute of Molecular Biosciences; University of Graz; Graz, Austria.
University of Graz · ATJoanneum Research · ATUniversité Paris-Sud · FRCURE International UK · GBMedical University of Graz · ATUniversity Medical Center Freiburg · DE

Funding

Austrian Science Fund FWF P 23490Austrian Science Fund FWF V 235
6 · The paper itself

Abstract

The multifaceted process of aging inevitably leads to disturbances in cellular metabolism and protein homeostasis. To meet this challenge, cells make use of autophagy, which is probably one of the most important pathways preserving cellular protection under stressful conditions. Thus, efficient autophagic flux is required for healthy aging in many if not all eukaryotic organisms. The regulation of autophagy itself is affected by changing metabolic conditions, but the precise metabolic circuitries are poorly understood. Recently, we found that the nucleocytosolic pool of acetyl-coenzyme A (AcCoA) functions as a major and dominant suppressor of cytoprotective autophagy during aging. Here, we propose an epigenetic mechanism for AcCoA-mediated autophagy suppression that causally involves the regulation of histone acetylation and changes in the autophagy-relevant transcriptome.

Indexed as

AutophagyLongevityAnimalsCoenzyme A LigasesDrosophila ProteinsCoenzyme A LigasesDrosophila Proteinsacetyl-coenzyme AagingATGautophagyepigenetichistone acetylationtranscription

Identifiers

PMID24879160
PMCPMC4091175
OpenAlexW2014902417

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.