Evidence map›Paper›PMID 32958557›Full record

ArticleThe Journal of biological chemistry2020

Pex3 confines pexophagy receptor activity of Atg36 to peroxisomes by regulating Hrr25-mediated phosphorylation and proteasomal degradation.

Sota Meguro, Xizhen Zhuang, Hiromi Kirisako, Hitoshi Nakatogawa

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.3field-weighted citation impact, top 18% 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

9 citing papers in PubMed, 14 citations in OpenAlex.

  1. Core principles of autophagy initiation mechanisms.Nature structural & molecular biology · 2026
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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

4 authors at 1 institution in 1 country.

Sota MeguroSchool of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.
Xizhen ZhuangSchool of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.
Hiromi KirisakoSchool of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan.
Hitoshi NakatogawaSchool of Life Science and Technology, Tokyo Institute of Technology, Yokohama, Japan. Electronic address: hnakatogawa@bio.titech.ac.jp.
Tokyo Institute of Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In macroautophagy (hereafter autophagy), cytoplasmic molecules and organelles are randomly or selectively sequestered within double-membrane vesicles called autophagosomes and delivered to lysosomes or vacuoles for degradation. In selective autophagy, the specificity of degradation targets is determined by autophagy receptors. In the budding yeast

Indexed as

ProteolysisAutophagy-Related ProteinsCasein Kinase IMembrane ProteinsPeroxinsPhosphorylationProteasome Endopeptidase ComplexSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsATG36 protein, S cerevisiaeAutophagy-Related ProteinsCasein Kinase IHRR25 protein, S cerevisiaeMembrane ProteinsPeroxinsPEX3 protein, S cerevisiaeProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsAtg36autophagyHrr25peroxisomePex3pexophagyproteasomeprotein degradationprotein phosphorylationSaccharomyces cerevisiaeselective autophagyyeast

Identifiers

PMID32958557
PMCPMC7705307
OpenAlexW3087575702

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.