Evidence map›Paper›PMID 31441992›Full record

ReviewMolecular oncology2019

Emerging roles of HECT-type E3 ubiquitin ligases in autophagy regulation.

Gerry Melino, Francesco Cecconi, Pier Giuseppe Pelicci, Tak Wah Mak, Francesca Bernassola

Open access · goldAbstract readReview
In one paragraph

Review in Molecular oncology, 2019. 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
1.6field-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, 24 citations in OpenAlex.

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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

5 authors at 3 institutions in 4 countries.

Gerry MelinoDepartment of Experimental Medicine, TOR, University of Rome "Tor Vergata", Italy.
Francesco CecconiCell Stress and Survival Unit, Danish Cancer Society Research Center, Copenhagen, Denmark.
Pier Giuseppe PelicciDepartment of Experimental Oncology, IEO, European Institute of Oncology IRCCS, Milan, Italy.
Tak Wah MakThe Campbell Family Institute for Breast Cancer Research, Ontario Cancer Institute, Princess Margaret Hospital, Toronto, ON, Canada.
Francesca BernassolaDepartment of Experimental Medicine, TOR, University of Rome "Tor Vergata", Italy.ORCID 0000-0002-8883-8654
University of Rome Tor Vergata · ITOntario Institute for Cancer Research · CAUniversity of Milan · IT

Funding

Medical Research Council MC_U132670600Medical Research Council MC_UU_00025/2
6 · The paper itself

Abstract

Autophagy is a conserved self-eating process that delivers cytoplasmic material to the lysosome to allow degradation of intracellular components, including soluble, unfolded and aggregated proteins, damaged organelles, and invading microorganisms. Autophagy provides a homeostatic control mechanism and is essential for balancing sources of energy in response to nutrient stress. Autophagic dysfunction or dysregulation has been implicated in several human pathologies, including cancer and neurodegeneration, and its modulation has substantial potential as a therapeutic strategy. Given the relevant clinical and therapeutic implications of autophagy, there is emerging intense interest in the identification of the key factors regulating the components of the autophagic machinery. Various post-translational modifications, including ubiquitylation, have been implicated in autophagy control. The list of the E3 ubiquitin protein ligases involved in the regulation of several steps of the autophagic process is continuously growing. In this review, we will focus on recent advances in the understanding of the role of the homologous to the E6AP carboxyl terminus-type E3 ubiquitin ligases in autophagy control.

Indexed as

AutophagyAnimalsHumansNeoplasmsNeurodegenerative DiseasesProtein DomainsProtein Processing, Post-TranslationalUbiquitinationUbiquitin-Protein LigasesUbiquitin-Protein LigasesautophagyHECT E3 ubiquitin ligasesproteasomal degradationubiquitylation

Identifiers

PMID31441992
PMCPMC6763782
OpenAlexW2969695551

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.