Evidence map›Paper›PMID 28607426›Full record

ArticleScientific reports2017

Analysis of the brain palmitoyl-proteome using both acyl-biotin exchange and acyl-resin-assisted capture methods.

Matthew J Edmonds, Bethany Geary, Mary K Doherty, Alan Morgan

Abstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Global analysis of membrane protein S-acylation in the model plantbioRxiv : the preprint server for biology · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Regulation of Dynamic Protein S-Acylation.Frontiers in molecular biosciences · 2021
    Review
  17. Detection of Protein S-Acylation using Acyl-Resin Assisted Capture.Journal of visualized experiments : JoVE · 2020
    Article
  18. 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

4 authors.

Matthew J EdmondsDepartment of Cellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, Crown St., Liverpool, L69 3BX, UK.
Bethany GearyDivision of Health Research, University of the Highlands and Islands, Centre for Health Science, Old Perth Road, Inverness, IV2 3JH, UK.
Mary K DohertyDivision of Health Research, University of the Highlands and Islands, Centre for Health Science, Old Perth Road, Inverness, IV2 3JH, UK.ORCID 0000-0002-3480-4088
Alan MorganDepartment of Cellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, Crown St., Liverpool, L69 3BX, UK. amorgan@liverpool.ac.uk.ORCID 0000-0002-0346-1289

Funding

Wellcome Trust
6 · The paper itself

Abstract

Palmitoylation is a reversible post-translational protein modification in which palmitic acid is added to cysteine residues, allowing association with different cellular membranes and subdomains. Recently, techniques have been developed to identify palmitoylation on a proteome-wide scale in order to reveal the full cellular complement of palmitoylated proteins. However, in the studies reported to date, there is considerable variation between the sets of identified palmitoyl-proteins and so there remains some uncertainty over what constitutes the definitive complement of palmitoylated proteins even in well-studied tissues such as brain. To address this issue, we used both acyl-biotin exchange and acyl-resin-assisted capture approaches using rat brain as a common protein source. The palmitoyl-proteins identified from each method by mass spectrometry were then compared with each other and previously published studies. There was generally good agreement between the two methods, although many identifications were unique to one method, indicating that at least some of the variability in published palmitoyl proteomes is due to methodological differences. By combining our new data with previous publications using mammalian cells/tissues, we propose a high confidence set of bona fide palmitoylated proteins in brain and provide a resource to help researchers prioritise candidate palmitoyl-proteins for investigation.

Indexed as

AcylationAnimalsBiotinBrainLipoylationMass SpectrometryPalmitic AcidProteomeProteomicsRatsResins, SyntheticBiotinPalmitic AcidProteomeResins, Synthetic

Identifiers

PMID28607426
PMCPMC5468251

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Registered trials

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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.