Evidence map›Paper›PMID 39814713›Full record

ReviewNature communications2025

Illuminating the impact of N-terminal acetylation: from protein to physiology.

Nina McTiernan, Ine Kjosås, Thomas Arnesen

Abstract readReview
In one paragraph

Review in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing 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

34 citing papers in PubMed.

  1. Article
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  4. Review
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  7. Probing Proteoform Heterogeneity From Single Human Oocytes.Molecular & cellular proteomics : MCP · 2026
    Article
  8. Article
  9. Review
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  11. Review
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  17. Review
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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

3 authors.

Nina McTiernanDepartment of Biomedicine, University of Bergen, Bergen, Norway. Nina.Tiernan@uib.no.ORCID http://orcid.org/0000-0002-1749-6933
Ine KjosåsDepartment of Biomedicine, University of Bergen, Bergen, Norway. Ine.Kjosas@uib.no.ORCID http://orcid.org/0000-0003-0619-9658
Thomas ArnesenDepartment of Biomedicine, University of Bergen, Bergen, Norway. Thomas.Arnesen@uib.no.ORCID http://orcid.org/0000-0002-3005-147X

Funding

EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council) 772039Norges Forskningsråd (Research Council of Norway) 324195Norges Forskningsråd (Research Council of Norway) 325142
6 · The paper itself

Abstract

N-terminal acetylation is a highly abundant protein modification in eukaryotic cells. This modification is catalysed by N-terminal acetyltransferases acting co- or post-translationally. Here, we review the eukaryotic N-terminal acetylation machinery: the enzymes involved and their substrate specificities. We also provide an overview of the impact of N-terminal acetylation, including its effects on protein folding, subcellular targeting, protein complex formation, and protein turnover. In particular, there may be competition between N-terminal acetyltransferases and other enzymes in defining protein fate. At the organismal level, N-terminal acetylation is highly influential, and its impairment was recently linked to cardiac dysfunction and neurodegenerative diseases.

Indexed as

AcetyltransferasesProtein Processing, Post-TranslationalProteinsAcetylationAnimalsHumansNeurodegenerative DiseasesProtein FoldingSubstrate SpecificityAcetyltransferasesProteins

Identifiers

PMID39814713
PMCPMC11735805

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.