Evidence map›Paper›PMID 30089256›Full record

ArticleCell reports2018

Proximal Cysteines that Enhance Lysine N-Acetylation of Cytosolic Proteins in Mice Are Less Conserved in Longer-Living Species.

Andrew M James, Anthony C Smith, Cassandra L Smith, Alan J Robinson, Michael P Murphy

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.4field-weighted citation impact, top 18% 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

25 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Profiling the landscape of cysteine posttranslational modifications in brain aging and neurodegeneration.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Thiol-Mediated Enhancement of NACS chemical biology · 2024
    Article
  11. Article
  12. The fitness cost of spurious phosphorylation.bioRxiv : the preprint server for biology · 2023
    Article
  13. Review
  14. Review
  15. Article
  16. Acetyl-CoA-mediated autoacetylation of fatty acid synthase as a metabolic switch of de novo lipogenesis inProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  17. Article
  18. Article
  19. Article
  20. Article
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

5 authors at 3 institutions in 1 country.

Andrew M JamesMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, UK. Electronic address: aj@mrc-mbu.cam.ac.uk.
Anthony C SmithMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, UK.
Cassandra L SmithMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, UK.
Alan J RobinsonMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, UK.
Michael P MurphyMedical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, UK. Electronic address: mpm@mrc-mbu.cam.ac.uk.
MRC Mitochondrial Biology Unit · GBUniversity of Cambridge · GBMedical Research Council · GB

Funding

Medical Research Council MC_U105663142Medical Research Council MC_U105674181Wellcome Trust 110158/Z/15/Z
6 · The paper itself

Abstract

Acetyl-coenzyme A (CoA) is an abundant metabolite that can also alter protein function through non-enzymatic N-acetylation of protein lysines. This N-acetylation is greatly enhanced in vitro if an adjacent cysteine undergoes initial S-acetylation, as this can lead to S→N transfer of the acetyl moiety. Here, using modeled mouse structures of 619 proteins N-acetylated in mouse liver, we show lysine N-acetylation is greater in vivo if a cysteine is within ∼10 Å. Extension to the genomes of 52 other mammalian and bird species shows pairs of proximal cysteine and N-acetylated lysines are less conserved, implying most N-acetylation is detrimental. Supporting this, there is less conservation of cytosolic pairs of proximal cysteine and N-acetylated lysines in species with longer lifespans. As acetyl-CoA levels are linked to nutrient supply, these findings suggest how dietary restriction could extend lifespan and how pathologies resulting from dietary excess may occur.

Indexed as

AcetylationAnimalsCysteineCytosolLysineMiceCysteineLysine

Identifiers

PMID30089256
PMCPMC6092265
OpenAlexW2885804421

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.