Evidence map›Paper›PMID 34154877›Full record

ArticleTrends in biochemical sciences2021

Lipidation status of single membrane-associated ATG8 proteins.

Christophe Viret, Mathias Faure

Open access · bronzeAbstract readComment
PubMed Publisher
In one paragraph

Article in Trends in biochemical sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 49% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 1 country.

Christophe ViretCIRI, Centre International de Recherche en Infectiologie, Université de Lyon, Inserm U1111, Université Claude Bernard Lyon 1, CNRS, UMR5308, ENS de Lyon, F-69007, Lyon, France. Electronic address: christophe.viret@inserm.fr.
Mathias FaureCIRI, Centre International de Recherche en Infectiologie, Université de Lyon, Inserm U1111, Université Claude Bernard Lyon 1, CNRS, UMR5308, ENS de Lyon, F-69007, Lyon, France; Equipe Labellisée par la Fondation pour la Recherche Médicale, FRM, France. Electronic address: mathias.faure@inserm.fr.
Centre National de la Recherche Scientifique · FRUniversité Claude Bernard Lyon 1 · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ATG8 are core autophagy proteins, the lipidated forms of which decorate double-membraned autophagosomes, as well as single-membraned organelles such as endolysosomes. Recent studies from the Florey and Münz laboratories delineate the status of single membrane-associated ATG8 proteins by indicating that their membrane anchoring can involve phosphatidylserine conjugation and their stabilization depends on ATG4 protease inhibition.

Indexed as

Membrane ProteinsMicrotubule-Associated ProteinsAutophagosomesAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsMembrane ProteinsMicrotubule-Associated ProteinsaminoglycerophospholipidsATG4 proteasesATG8 proteinslipidationnoncanonical autophagyoxidation

Identifiers

PMID34154877
OpenAlexW3175022796

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.