Evidence map›Paper›PMID 40853005›Full record

ArticlemSphere2025

Unc-51-like kinase 1 (ULK1) regulates bacterial ubiquitylation and p62 recruitment during xenophagic clearance of

J S Ribeiro, M S Siqueira, T S M Farias, T D P Spinasse, P L O Correia, R M Ribeiro, F M Bastos de Oliveira, L A M Carneiro, L H Travassos

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in mSphere, 2025. 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
–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

1 citing paper in PubMed.

  1. 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

9 authors.

J S Ribeiro *Laboratory of Immunoreceptors and Signaling, Institute of Biophysics Carlos Chagas Filho, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil.
M S Siqueira *Laboratory of Immunoreceptors and Signaling, Institute of Biophysics Carlos Chagas Filho, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil.
T S M Farias *Laboratory of Immunoreceptors and Signaling, Institute of Biophysics Carlos Chagas Filho, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil.
T D P SpinasseLaboratory of Immunoreceptors and Signaling, Institute of Biophysics Carlos Chagas Filho, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil.
P L O CorreiaLaboratory of Immunoreceptors and Signaling, Institute of Biophysics Carlos Chagas Filho, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil.
R M RibeiroLaboratory of Immunoreceptors and Signaling, Institute of Biophysics Carlos Chagas Filho, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil.
F M Bastos de OliveiraLaboratory of Immunoreceptors and Signaling, Institute of Biophysics Carlos Chagas Filho, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil.
L A M CarneiroLaboratory of Innate Immunity and Inflammation, Department of Immunology, Institute of Microbiology Paulo de Góes, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil.
L H TravassosLaboratory of Immunoreceptors and Signaling, Institute of Biophysics Carlos Chagas Filho, Federal University of Rio de Janeiro, Rio de Janeiro, Brazil.ORCID 0000-0003-1323-3797

Funding

Conselho Nacional de Desenvolvimento Científico e TecnológicoCoordenação de Aperfeiçoamento de Pessoal de Nível Superior CAPES/BiocomputacionalFundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiro E-26/200.953/2021Fundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiro E26/200.998/2022Fundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiro E26/211.466/2021Universidade Federal do Rio de Janeiro/PIBIC
6 · The paper itself

Abstract

Autophagy is an essential cellular homeostatic process that also serves as an innate immune mechanism against intracellular bacterial pathogens through a highly selective form of autophagy known as xenophagy. Despite advances in understanding how bacteria are targeted for autophagic degradation, the specific regulatory mechanisms that drive the initial steps and ensure bacterial selection remain incompletely defined. Our study uncovers a pivotal role for Unc-51-like kinase 1 (ULK1) in the xenophagic clearance of the intracellular bacterial pathogen

Indexed as

Autophagy-Related Protein-1 HomologFibroblastsListeria monocytogenesListeriosisMacroautophagyAnimalsAutophagosomesImmunity, InnateMicePhosphorylationSequestosome-1 ProteinUbiquitinationAutophagy-Related Protein-1 HomologSequestosome-1 Proteinautophagybacterial clearancehost-microbe interactionsinfectioninnate immunityListeria monocytogenesp62ubiquitinationULK1xenophagy

Identifiers

PMID40853005
PMCPMC12482158

What OpenQuestion holds

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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.