Evidence map›Paper›PMID 25987439›Full record

ReviewGene2015

The biological functions of Naa10 - From amino-terminal acetylation to human disease.

Max J Dörfel, Gholson J Lyon

Abstract readReview
In one paragraph

Review in Gene, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
4.0field-weighted citation impact, top 4% 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

62 citing papers in PubMed, 100 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Review
  8. Article
  9. Neuroanatomical features of NAA10 and NAA15-related neurodevelopmental syndromes.Journal of neuroradiology = Journal de neuroradiologie · 2025
    Article
  10. Article
  11. Conformational plasticity links structural instability of NAA10Computational and structural biotechnology journal · 2024
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

2 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

2 authors at 1 institution in 1 country.

Max J DörfelStanley Institute for Cognitive Genomics, Cold Spring Harbor Laboratory, NY, USA. Electronic address: MDoerfel@cshl.edu.
Gholson J LyonStanley Institute for Cognitive Genomics, Cold Spring Harbor Laboratory, NY, USA; Department of Psychiatry, Stony Brook University, Stony Brook, NY, USA; Utah Foundation for Biomedical Research, Salt Lake City, UT, USA. Electronic address: gholsonjlyon@gmail.com.
Cold Spring Harbor Laboratory · US

Funding

BioGPS: Extensible Web 2.0 gene portal for structured and unstructured annotationR01GM083924 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SU, ANDREW I, WU, CHUNLEI · 2008 to 2021
$5.6M
The Gene Wiki: Community intelligence applied to gene annotationR01GM089820 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SU, ANDREW I · 2010 to 2021
$5.2M
NIGMS NIH HHS GM089820NIGMS NIH HHS R01 GM083924NIGMS NIH HHS R01 GM089820
6 · The paper itself

Abstract

N-terminal acetylation (NTA) is one of the most abundant protein modifications known, and the N-terminal acetyltransferase (NAT) machinery is conserved throughout all Eukarya. Over the past 50 years, the function of NTA has begun to be slowly elucidated, and this includes the modulation of protein-protein interaction, protein-stability, protein function, and protein targeting to specific cellular compartments. Many of these functions have been studied in the context of Naa10/NatA; however, we are only starting to really understand the full complexity of this picture. Roughly, about 40% of all human proteins are substrates of Naa10 and the impact of this modification has only been studied for a few of them. Besides acting as a NAT in the NatA complex, recently other functions have been linked to Naa10, including post-translational NTA, lysine acetylation, and NAT/KAT-independent functions. Also, recent publications have linked mutations in Naa10 to various diseases, emphasizing the importance of Naa10 research in humans. The recent design and synthesis of the first bisubstrate inhibitors that potently and selectively inhibit the NatA/Naa10 complex, monomeric Naa10, and hNaa50 further increases the toolset to analyze Naa10 function.

Indexed as

Protein Processing, Post-TranslationalAcetylationAmino Acid SequenceAnimalsCell HypoxiaDNA DamageGene Expression RegulationGenetic Diseases, InbornHumansMolecular Sequence DataNeoplasmsN-Terminal Acetyltransferase AN-Terminal Acetyltransferase EProtein Structure, TertiaryNAA10 protein, humanN-Terminal Acetyltransferase AN-Terminal Acetyltransferase EAcetyltransferasesAmino-terminal acetylationard1EnzymologyNAA10NAA15NAA50Ogden syndromeProteinsProteomics

Identifiers

PMID25987439
PMCPMC4461483
OpenAlexW2212538720

What OpenQuestion holds

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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.