Evidence map›Paper›PMID 31652724›Full record

ReviewInternational journal of molecular sciences2019

A Mechanistic Perspective on PEX1 and PEX6, Two AAA+ Proteins of the Peroxisomal Protein Import Machinery.

Ana G Pedrosa, Tânia Francisco, Maria J Ferreira, Tony A Rodrigues, Aurora Barros-Barbosa, Jorge E Azevedo

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.7field-weighted citation impact, top 30% 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

10 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
  2. Mammalian pexophagy at a glance.Journal of cell science · 2024
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Ophthalmology science · 2021
    Article
  9. Article
  10. Review
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

6 authors at 1 institution in 1 country.

Ana G PedrosaInstituto de Investigação e Inovação em Saúde (i3S), Instituto de Biologia Molecular e Celular (IBMC), Instituto de Ciências Biomédicas de Abel Salazar (ICBAS)-Universidade do Porto, Rua Alfredo Allen, 208, 4200-135 Porto, Portugal. ana.pedrosa@i3s.up.pt.
Tânia FranciscoInstituto de Investigação e Inovação em Saúde (i3S), Instituto de Biologia Molecular e Celular (IBMC), Instituto de Ciências Biomédicas de Abel Salazar (ICBAS)-Universidade do Porto, Rua Alfredo Allen, 208, 4200-135 Porto, Portugal. taniaf@ibmc.up.pt.
Maria J FerreiraInstituto de Investigação e Inovação em Saúde (i3S), Instituto de Biologia Molecular e Celular (IBMC), Instituto de Ciências Biomédicas de Abel Salazar (ICBAS)-Universidade do Porto, Rua Alfredo Allen, 208, 4200-135 Porto, Portugal. maria.ferreira@i3s.up.pt.
Tony A RodriguesInstituto de Investigação e Inovação em Saúde (i3S), Instituto de Biologia Molecular e Celular (IBMC), Instituto de Ciências Biomédicas de Abel Salazar (ICBAS)-Universidade do Porto, Rua Alfredo Allen, 208, 4200-135 Porto, Portugal. tonyr@ibmc.up.pt.
Aurora Barros-BarbosaInstituto de Investigação e Inovação em Saúde (i3S), Instituto de Biologia Molecular e Celular (IBMC), Instituto de Ciências Biomédicas de Abel Salazar (ICBAS)-Universidade do Porto, Rua Alfredo Allen, 208, 4200-135 Porto, Portugal. aurora.barbosa@i3s.up.pt.ORCID 0000-0003-4484-4427
Jorge E AzevedoInstituto de Investigação e Inovação em Saúde (i3S), Instituto de Biologia Molecular e Celular (IBMC), Instituto de Ciências Biomédicas de Abel Salazar (ICBAS)-Universidade do Porto, Rua Alfredo Allen, 208, 4200-135 Porto, Portugal. jazevedo@ibmc.up.pt.
Universidade do Porto · PT

Funding

Fundação para a Ciência e a Tecnologia PTDC/BEX-BCM/2311/2014
6 · The paper itself

Abstract

In contrast to many protein translocases that use ATP or GTP hydrolysis as the driving force to transport proteins across biological membranes, the peroxisomal matrix protein import machinery relies on a regulated self-assembly mechanism for this purpose and uses ATP hydrolysis only to reset its components. The ATP-dependent protein complex in charge of resetting this machinery-the Receptor Export Module (REM)-comprises two members of the "ATPases Associated with diverse cellular Activities" (AAA+) family, PEX1 and PEX6, and a membrane protein that anchors the ATPases to the organelle membrane. In recent years, a large amount of data on the structure/function of the REM complex has become available. Here, we discuss the main findings and their mechanistic implications.

Indexed as

AnimalsATPases Associated with Diverse Cellular ActivitiesHumansPeroxisomesPeroxisome-Targeting Signal 1 ReceptorProtein TransportATPases Associated with Diverse Cellular ActivitiesPeroxisome-Targeting Signal 1 ReceptorAAA+ ATPaseperoxisomePEX1PEX5PEX6protein translocation

Identifiers

PMID31652724
PMCPMC6862443
OpenAlexW2982108185

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.