Evidence map›Paper›PMID 32060627›Full record

ReviewCurrent genetics2020

How does protein degradation regulate TOM machinery-dependent mitochondrial import?

Mohamed A Eldeeb, Mohamed A Ragheb, Mansoore Esmaili

Abstract readReview
PubMed Publisher
In one paragraph

Review in Current genetics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Article
  6. ING2 Controls Mitochondrial RespirationFrontiers in cell and developmental biology · 2021
    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.

Mohamed A EldeebChemistry Department (Biochemistry Division), Faculty of Science, Cairo University, Giza, Egypt. Eldeeb@ualberta.ca.ORCID http://orcid.org/0000-0001-9671-9340
Mohamed A RaghebChemistry Department (Biochemistry Division), Faculty of Science, Cairo University, Giza, Egypt.
Mansoore EsmailiDepartment of Biochemistry, University of Alberta, Edmonton, AB, Canada.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondrial dysregulation is a pivotal hallmark of aging-related disorders. Although there is a considerable understanding of the molecular counteracting responses toward damaged mitochondria, the molecular underpinnings connecting the abnormal aggregation of mitochondrial precursor protein fragments and abrogation of mitochondrial import machinery are far from clear. Recently, proteasomal-dependent degradation was unveiled as a pivotal fine-tuner of TOM machinery-dependent mitochondrial import. Herein, the role of proteasomal-mediated degradation in regulating fidelity of TOM-dependent import is briefly discussed and analyzed. The insights obtained from the characterization of this process may be applied to targeting mitochondrial import dysfunction in some neurodegenerative disorders.

Indexed as

AnimalsCarrier ProteinsHumansMembrane Transport ProteinsMitochondriaMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsProteolysisCarrier ProteinsMembrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMitochondrial ProteinsMitochondrial importMitochondrial quality controlMitophagyProteasomeProtein degradationProtein quality controlTOM complexUbiquitin

Identifiers

PMID32060627

What OpenQuestion holds

Textmetadata
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.