Evidence map›Paper›PMID 30878283›Full record

ReviewMolecular cell2019

Co-translational, Post-translational, and Non-catalytic Roles of N-Terminal Acetyltransferases.

Henriette Aksnes, Rasmus Ree, Thomas Arnesen

Open access · bronzeAbstract readReview
In one paragraph

Review in Molecular cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 150 papers.

0numbers the graph read from it
0cells of the map it votes in
150citing papers in PubMed
12.8field-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

150 citing papers in PubMed, 260 citations in OpenAlex.

  1. Trial
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  7. A C-degron regulates Chk1 kinase by allowing stability of inactive Chk1 and by making it short- lived upon activation.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  17. Science advances · 2025
    Article
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  19. Degrons: defining the rules of protein degradation.Nature reviews. Molecular cell biology · 2025
    Review
  20. Article

90 more citing papers are in PubMed but not listed here.

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 at 2 institutions in 1 country.

Henriette AksnesDepartment of Biomedicine, University of Bergen, 5020 Bergen, Norway. Electronic address: henriette.aksnes@uib.no.
Rasmus ReeDepartment of Biomedicine, University of Bergen, 5020 Bergen, Norway.
Thomas ArnesenDepartment of Biomedicine, University of Bergen, 5020 Bergen, Norway; Department of Biological Sciences, University of Bergen, 5020 Bergen, Norway; Department of Surgery, Haukeland University Hospital, 5021 Bergen, Norway. Electronic address: thomas.arnesen@uib.no.
University of Bergen · NOHaukeland University Hospital · NO

Funding

European Research Council 772039
6 · The paper itself

Abstract

Recent studies of N-terminal acetylation have identified new N-terminal acetyltransferases (NATs) and expanded the known functions of these enzymes beyond their roles as ribosome-associated co-translational modifiers. For instance, the identification of Golgi- and chloroplast-associated NATs shows that acetylation of N termini also happens post-translationally. In addition, we now appreciate that some NATs are highly specific; for example, a dedicated NAT responsible for post-translational N-terminal acetylation of actin was recently revealed. Other studies have extended NAT function beyond Nt acetylation, including functions as lysine acetyltransferases (KATs) and non-catalytic roles. Finally, emerging studies emphasize the physiological relevance of N-terminal acetylation, including roles in calorie-restriction-induced longevity and pathological α-synuclein aggregation in Parkinson's disease. Combined, the NATs rise as multifunctional proteins, and N-terminal acetylation is gaining recognition as a major cellular regulator.

Indexed as

Protein Processing, Post-TranslationalAcetylationAnimalsCatalysisHumansN-Terminal AcetyltransferasesProteasome Endopeptidase ComplexProtein DomainsProteolysisSignal TransductionSubstrate SpecificityN-Terminal AcetyltransferasesProteasome Endopeptidase ComplexacetylationactinKATlysine acetyltransferaseNAA10NAA80NATN-terminal acetylationN-terminal acetyltransferaseprotein modifications

Identifiers

PMID30878283
PMCPMC6962057
OpenAlexW2921660925

What OpenQuestion holds

Textmetadata
LicenceTDM
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.