Evidence map›Paper›PMID 26348128›Full record

ReviewBiochimica et biophysica acta2016

Pexophagy and peroxisomal protein turnover in plants.

Pierce G Young, Bonnie Bartel

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

33 citing papers in PubMed, 62 citations in OpenAlex.

  1. Review
  2. Article
  3. SilencingInternational journal of molecular sciences · 2023
    Article
  4. Profile of Bonnie Bartel.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  5. Review
  6. Article
  7. Review
  8. SilencingInternational journal of molecular sciences · 2021
    Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Autophagic Machinery of Plant Peroxisomes.International journal of molecular sciences · 2019
    Review
  18. Article
  19. Review
  20. 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

2 authors at 1 institution in 1 country.

Pierce G YoungDepartment of BioSciences, Rice University, Houston, TX 77005, USA. Electronic address: pgy1@rice.edu.
Bonnie BartelDepartment of BioSciences, Rice University, Houston, TX 77005, USA. Electronic address: bartel@rice.edu.
Rice University · US

Funding

Using Arabidopsis to uncover new roles for peroxinsR01GM079177 · NIGMS · RICE UNIVERSITY · PI BARTEL, BONNIE · 2009 to 2017
$2.4M
Laser scanning confocal microscopeS10RR026399 · NCRR · RICE UNIVERSITY · PI BARTEL, BONNIE · 2010 to 2010
$500k
NCRR NIH HHS S10 RR026399NCRR NIH HHS S10RR026399-01NIGMS NIH HHS R01 GM079177NIGMS NIH HHS R01GM079177
6 · The paper itself

Abstract

Peroxisomes are dynamic, vital organelles that sequester a variety of oxidative reactions and their toxic byproducts from the remainder of the cell. The oxidative nature of peroxisomal metabolism predisposes the organelle to self-inflicted damage, highlighting the need for a mechanism to dispose of damaged peroxisomes. In addition, the metabolic requirements of plant peroxisomes change during development, and obsolete peroxisomal proteins are degraded. Although pexophagy, the selective autophagy of peroxisomes, is an obvious mechanism for executing such degradation, pexophagy has only recently been described in plants. Several recent studies in the reference plant Arabidopsis thaliana implicate pexophagy in the turnover of peroxisomal proteins, both for quality control and during functional transitions of peroxisomal content. In this review, we describe our current understanding of the occurrence, roles, and mechanisms of pexophagy in plants.

Indexed as

ArabidopsisArabidopsis ProteinsATP-Dependent ProteasesAutophagyEndoplasmic ReticulumGene Expression Regulation, PlantOxidation-ReductionPeroxisomal Targeting Signal 2 ReceptorPeroxisomesPeroxisome-Targeting Signal 1 ReceptorProtein IsoformsProteolysisReceptors, Cytoplasmic and NuclearSignal TransductionUbiquitinationArabidopsis ProteinsATP-Dependent ProteasesLON2 protein, ArabidopsisPeroxisomal Targeting Signal 2 ReceptorPeroxisome-Targeting Signal 1 ReceptorPEX5 protein, ArabidopsisProtein IsoformsReceptors, Cytoplasmic and NuclearAutophagyLON proteaseOrganelle quality controlPeroxisomePexophagyProtein degradation

Identifiers

PMID26348128
PMCPMC4779433
OpenAlexW1664328131

What OpenQuestion holds

Textmetadata
LicenceTDM
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.