Evidence map›Paper›PMID 31002009›Full record

ArticleAutophagy2019

Proteasome dysfunction induces excessive proteome instability and loss of mitostasis that can be mitigated by enhancing mitochondrial fusion or autophagy.

Eleni N Tsakiri, Sentiljana Gumeni, Konstantinos Vougas, Diana Pendin, Issidora Papassideri, Andrea Daga, Vassilis Gorgoulis, Gábor Juhász, Luca Scorrano, Ioannis P Trougakos

Open access · bronzeAbstract read
In one paragraph

Article in Autophagy, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

27 citing papers in PubMed, 49 citations in OpenAlex.

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  6. The link between Mitochondria and Sarcopenia.Journal of physiology and biochemistry · 2025
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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

10 authors at 5 institutions in 4 countries.

Eleni N TsakiriDepartment of Cell Biology and Biophysics, Faculty of Biology, National and Kapodistrian University of Athens , Athens , Greece.
Sentiljana GumeniDepartment of Cell Biology and Biophysics, Faculty of Biology, National and Kapodistrian University of Athens , Athens , Greece.
Konstantinos VougasGenomics and Proteomics Research Units, Center of Basic Research II, Biomedical Research Foundation, Academy of Athens , Athens , Greece.
Diana PendinDepartment of Biomedical Sciences, University of Padova , Padova , Italy.ORCID 0000-0003-2827-935X
Issidora PapassideriDepartment of Cell Biology and Biophysics, Faculty of Biology, National and Kapodistrian University of Athens , Athens , Greece.
Andrea DagaLaboratory of Molecular Biology, Scientific Institute, IRCCS E. Medea , Lecco , Italy.ORCID 0000-0001-8935-5489
Vassilis GorgoulisGenomics and Proteomics Research Units, Center of Basic Research II, Biomedical Research Foundation, Academy of Athens , Athens , Greece.
Gábor JuhászDepartment of Anatomy, Cell and Developmental Biology, Eötvös Loránd University, Budapest, Hungary and Biological Research Centre, Hungarian Academy of Sciences , Szeged , Hungary.ORCID 0000-0001-8548-8874
Luca ScorranoDulbecco-Telethon Institute, Venetian Institute of Molecular Medicine and Department of Biology, University of Padua , Padova , Italy.
Ioannis P TrougakosDepartment of Cell Biology and Biophysics, Faculty of Biology, National and Kapodistrian University of Athens , Athens , Greece.
National and Kapodistrian University of Athens · GRUniversity of Padua · ITBiomedical Research Foundation of the Academy of Athens · GREötvös Loránd University · HUIRCCS Eugenio Medea · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ubiquitin-proteasome pathway (UPP) is central to proteostasis network (PN) functionality and proteome quality control. Yet, the functional implication of the UPP in tissue homeodynamics at the whole organism level and its potential cross-talk with other proteostatic or mitostatic modules are not well understood. We show here that knock down (KD) of proteasome subunits in

Indexed as

ProteolysisProteostasisAgingAnimalsAnimals, Genetically ModifiedAutophagyDrosophila melanogasterDrosophila ProteinsLarvaMitochondriaMitochondrial DynamicsProteasome Endopeptidase ComplexProteomeAtg8a protein, DrosophilaDrosophila ProteinsProteasome Endopeptidase ComplexProteomeAgingautophagycncCfoxomitostasisproteasomeproteostasis

Identifiers

PMID31002009
PMCPMC6735541
OpenAlexW2937168301

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.