Evidence map›Paper›PMID 38383789›Full record

ArticleNature2024

The UFM1 E3 ligase recognizes and releases 60S ribosomes from ER translocons.

Linda Makhlouf, Joshua J Peter, Helge M Magnussen, Rohan Thakur, David Millrine, Thomas C Minshull, Grace Harrison, Joby Varghese, Frederic Lamoliatte, Martina Foglizzo and 4 more

Open access · hybridAbstract read
In one paragraph

Article in Nature, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
11.7field-weighted citation impact, top 1% 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

39 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. NFYB Integrates Hormonal Signals into Tissue Allometry by Promoting Protein Biosynthesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  5. Article
  6. Evaluating evidence for UFMylation client diversity.Nature reviews. Molecular cell biology · 2026
    Article
  7. The mechanistic basis and cellular functions of UFMylation.Nature reviews. Molecular cell biology · 2026
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. UFMylation of Pyruvate Dehydrogenase Regulates Mitochondrial Metabolism.bioRxiv : the preprint server for biology · 2026
    Article
  15. Article
  16. Ribosome-associated quality control and related mechanisms.Nature structural & molecular biology · 2026
    Review
  17. Review
  18. Quality control and signaling pathways at stalled ribosomes.Experimental & molecular medicine · 2026
    Review
  19. Article
  20. 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

14 authors at 3 institutions in 1 country.

Linda Makhlouf *Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK.
Joshua J Peter *MRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
Helge M Magnussen *MRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
Rohan ThakurMRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
David MillrineMRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.ORCID 0000-0002-8041-0151
Thomas C MinshullAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK.
Grace HarrisonMRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
Joby VargheseMRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
Frederic LamoliatteMRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.
Martina FoglizzoAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK.ORCID 0000-0001-9132-4737
Thomas MacartneyMRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK.ORCID 0000-0002-6745-183X
Antonio N CalabreseAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK.ORCID 0000-0003-2437-7761
Elton ZeqirajAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK. e.zeqiraj@leeds.ac.uk.ORCID 0000-0003-0239-5926
Yogesh KulathuMRC Protein Phosphorylation and Ubiquitylation Unit, University of Dundee, Dundee, UK. ykulathu@dundee.ac.uk.ORCID 0000-0002-3274-1642
University of Leeds · GBUniversity of Dundee · GBMRC Protein Phosphorylation and Ubiquitylation Unit · GB

Funding

Medical Research Council MC_UU_00018/3Wellcome Trust 220628Wellcome Trust 223810
6 · The paper itself

Abstract

Stalled ribosomes at the endoplasmic reticulum (ER) are covalently modified with the ubiquitin-like protein UFM1 on the 60S ribosomal subunit protein RPL26 (also known as uL24)

Indexed as

Endoplasmic ReticulumProtein Processing, Post-TranslationalRibosome Subunits, Large, EukaryoticUbiquitin-Protein LigasesAdaptor Proteins, Signal TransducingBinding SitesCell Cycle ProteinsCryoelectron MicroscopyHomeostasisIntracellular MembranesPeptidyl TransferasesRibosomal ProteinsRNA, TransferSEC Translocation ChannelsTumor Suppressor ProteinsAdaptor Proteins, Signal TransducingCell Cycle ProteinsPeptidyl TransferasesRibosomal ProteinsRNA, TransferSEC Translocation ChannelsTumor Suppressor ProteinsUbiquitin-Protein Ligases

Identifiers

PMID38383789
PMCPMC10937380
OpenAlexW4391994171

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.