Evidence map›Paper›PMID 28680068›Full record

ArticleScientific reports2017

Global, site-specific analysis of neuronal protein S-acylation.

Mark O Collins, Keith T Woodley, Jyoti S Choudhary

Open access · goldAbstract 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 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
3.9field-weighted citation impact, top 5% 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

54 citing papers in PubMed, 95 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Global analysis of membrane protein S-acylation in the model plantbioRxiv : the preprint server for biology · 2025
    Article
  7. Article
  8. Article
  9. Reduced Palmitoylation of SQSTM1/p62 in Huntington Disease Is Associated With Impaired Autophagy.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  10. Article
  11. Article
  12. Review
  13. GABATranslational psychiatry · 2024
    Article
  14. Article
  15. Review
  16. Mechanisms and functions of protein S-acylation.Nature reviews. Molecular cell biology · 2024
    Review
  17. Review
  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

3 authors at 2 institutions in 1 country.

Mark O CollinsWellcome Trust Sanger Institute, Hinxton, Cambridge, CB10 1SA, UK. Mark.collins@sheffield.ac.uk.ORCID 0000-0002-7656-4975
Keith T WoodleyDepartment of Biomedical Science & Centre for Membrane Interactions and Dynamics (CMIAD), Firth Court, Western Bank, University of Sheffield, Sheffield, S10 2TN, UK.
Jyoti S ChoudharyWellcome Trust Sanger Institute, Hinxton, Cambridge, CB10 1SA, UK. jc4@sanger.ac.uk.
Wellcome Sanger Institute · GBUniversity of Sheffield · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Protein S-acylation (palmitoylation) is a reversible lipid modification that is an important regulator of dynamic membrane-protein interactions. Proteomic approaches have uncovered many putative palmitoylated proteins however, methods for comprehensive palmitoylation site characterization are lacking. We demonstrate a quantitative site-specific-Acyl-Biotin-Exchange (ssABE) method that allowed the identification of 906 putative palmitoylation sites on 641 proteins from mouse forebrain. 62% of sites map to known palmitoylated proteins and 102 individual palmitoylation sites are known from the literature. 54% of palmitoylation sites map to synaptic proteins including many GPCRs, receptors/ion channels and peripheral membrane proteins. Phosphorylation sites were also identified on a subset of peptides that were palmitoylated, demonstrating for the first time co-identification of these modifications by mass spectrometry. Palmitoylation sites were identified on over half of the family of palmitoyl-acyltransferases (PATs) that mediate protein palmitoylation, including active site thioester-linked palmitoyl intermediates. Distinct palmitoylation motifs and site topology were identified for integral membrane and soluble proteins, indicating potential differences in associated PAT specificity and palmitoylation function. ssABE allows the global identification of palmitoylation sites as well as measurement of the active site modification state of PATs, enabling palmitoylation to be studied at a systems level.

Indexed as

AcylationAnimalsMass SpectrometryMicePhosphorylationProsencephalonProteinsProteomicsProteins

Identifiers

PMID28680068
PMCPMC5498535
OpenAlexW2734199346

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.