Evidence map›Paper›PMID 40395304›Full record

ReviewAutophagy reports2023

Structural biology of the Atg8 and Atg12 conjugation systems.

Nobuo N Noda

Abstract readReview
In one paragraph

Review in Autophagy reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Autophagy in Ovarian Cancer, an Opportunity or an Additional Threat?International journal of molecular sciences · 2026
    Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Mechanisms of autophagosome formation.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2025
    Review
  7. 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

1 author.

Nobuo N NodaInstitute for Genetic Medicine, Hokkaido University, Sapporo, Japan.ORCID https://orcid.org/0000-0002-6940-8069

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Atg8 and Atg12 are ubiquitin-like proteins, conjugated to phosphatidylethanolamine (PE) and Atg5, respectively, through enzymatic reactions similar to ubiquitylation. The resultant Atg8-PE and Atg12-Atg5 conjugates play crucial roles in autophagy. Structural studies have been extensively performed on all Atg proteins (Atg3, Atg4, Atg5, Atg7, Atg8, Atg10, Atg12, Atg16) involved in these conjugation systems. This review summarizes structural studies and discusses mechanisms of conjugation and deconjugation reactions, as well as autophagic functions of the Atg8 and Atg12 conjugation systems.

Indexed as

Atg10Atg12Atg16Atg3Atg4Atg5Atg7Atg8RavZstructural biology

Identifiers

PMID40395304
PMCPMC12005411

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.