Evidence map›Paper›PMID 37848407›Full record

ArticleAutophagy2024

The role of the N terminus of lipidated human Atg8-family proteins in

Hana Popelka, Daniel J Klionsky

Open access · greenAbstract readEditorial
PubMed Full text at PMC Publisher
In one paragraph

Article in Autophagy, 2024. 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
0.6field-weighted citation impact, top 28% 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

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.

Hana PopelkaLife Sciences Institute, University of Michigan, Ann Arbor, MI, USA.
Daniel J KlionskyLife Sciences Institute, University of Michigan, Ann Arbor, MI, USA.ORCID 0000-0002-7828-8118
University of Michigan · US

Funding

The mechanism and regulation of autophagyR35GM131919 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI DANIEL J. KLIONSKY · 2019 to 2026
$6.4M
NIGMS NIH HHS R35 GM131919
6 · The paper itself

Abstract

A multifunctional role of Atg8-family proteins (Atg8 from yeast and human LC3 and GABARAP subfamilies, all referred to here as ATG8s) in macroautophagy/autophagy is carried out by two protein domains, the N-terminal helical domain (NHD) and ubiquitin-like (UBL) domain. Previous studies showed that the NHD of PE-conjugated ATG8s mediates membrane hemifusion via a direct interaction with lipids in

Indexed as

AutophagyMicrotubule-Associated ProteinsAutophagy-Related Protein 8 FamilyHumansMacroautophagyAutophagy-Related Protein 8 FamilyMicrotubule-Associated ProteinsATG8 proteinscis- and trans-membrane association of lipidated ATG8sN-terminal helical domainopen-closed conformation of ATG8subiquitin-like

Identifiers

PMID37848407
PMCPMC10761052
OpenAlexW4387696347

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.