Evidence map›Paper›PMID 24368788›Full record

ArticleThe Plant cell2013

Highly oxidized peroxisomes are selectively degraded via autophagy in Arabidopsis.

Michitaro Shibata, Kazusato Oikawa, Kohki Yoshimoto, Maki Kondo, Shoji Mano, Kenji Yamada, Makoto Hayashi, Wataru Sakamoto, Yoshinori Ohsumi, Mikio Nishimura

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 96 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed, 3 pooled it
10.0field-weighted citation impact, top 1% 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

96 citing papers in PubMed, 3 syntheses or guidelines pooled it, 200 citations in OpenAlex.

  1. Guideline
  2. Pooled it
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  4. Review
  5. Article
  6. PLETHORA-autophagy axis activates organ regeneration through ROS modulation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  8. Article
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  17. SilencingInternational journal of molecular sciences · 2023
    Article
  18. Review
  19. Review
  20. Article

36 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 4 institutions in 2 countries.

Michitaro ShibataDepartment of Cell Biology, National Institute for Basic Biology, Okazaki 444-8585, Japan.
Kazusato Oikawa
Kohki Yoshimoto
Maki Kondo
Shoji Mano
Kenji Yamada
Makoto Hayashi
Wataru Sakamoto
Yoshinori Ohsumi
Mikio Nishimura
National Institute for Basic Biology · JPAgroParisTech · FROkayama University · JPTokyo Institute of Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The positioning of peroxisomes in a cell is a regulated process that is closely associated with their functions. Using this feature of the peroxisomal positioning as a criterion, we identified three Arabidopsis thaliana mutants (peroxisome unusual positioning1 [peup1], peup2, and peup4) that contain aggregated peroxisomes. We found that the PEUP1, PEUP2, and PEUP4 were identical to Autophagy-related2 (ATG2), ATG18a, and ATG7, respectively, which are involved in the autophagic system. The number of peroxisomes was increased and the peroxisomal proteins were highly accumulated in the peup1 mutant, suggesting that peroxisome degradation by autophagy (pexophagy) is deficient in the peup1 mutant. These aggregated peroxisomes contained high levels of inactive catalase and were more oxidative than those of the wild type, indicating that peroxisome aggregates comprise damaged peroxisomes. In addition, peroxisome aggregation was induced in wild-type plants by exogenous application of hydrogen peroxide. The cat2 mutant also contained peroxisome aggregates. These findings demonstrate that hydrogen peroxide as a result of catalase inactivation is the inducer of peroxisome aggregation. Furthermore, an autophagosome marker, ATG8, frequently colocalized with peroxisome aggregates, indicating that peroxisomes damaged by hydrogen peroxide are selectively degraded by autophagy in the wild type. Our data provide evidence that autophagy is crucial for quality control mechanisms for peroxisomes in Arabidopsis.

Indexed as

AutophagyArabidopsisArabidopsis ProteinsHydrogen PeroxideMutationOxidation-ReductionPeroxisomesPhagosomesStress, PhysiologicalArabidopsis ProteinsCAT2 protein, ArabidopsisHydrogen Peroxide

Identifiers

PMID24368788
PMCPMC3903999
OpenAlexW2110448073

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.