Evidence map›Paper›PMID 20379138›Full record

ArticleNature protocols2010

Analysis of protein S-acylation by gas chromatography-coupled mass spectrometry using purified proteins.

Nadav Sorek, Shaul Yalovsky

Abstract read
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In one paragraph

Article in Nature protocols, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Review
  7. ProteinOpen biology · 2021
    Review
  8. Article
  9. Article
  10. Proteomic analysis of fatty-acylated proteins.Current opinion in chemical biology · 2016
    Review
  11. Article
  12. The physiology of protein S-acylation.Physiological reviews · 2015
    Review
  13. Review
  14. Ion channel regulation by protein S-acylation.The Journal of general physiology · 2014
    Review
  15. Article
  16. Article
  17. 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

2 authors.

Nadav SorekDepartment of Plant Sciences, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel.
Shaul Yalovsky

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

S-acylation, also known as palmitoylation, involves the attachment of acyl fatty acids to thiol groups of cysteine residues through a reversible thioester bond. Owing to its reversibility, S-acylation is important in regulation of diverse signaling cascades, including Ras-associated cancers in mammals, stress response and metabolic regulation. Here we describe a simple protocol for analysis of protein S-acylation using gas chromatography-coupled mass spectrometry. Analysis can be carried out with as little as 1 microg of purified protein and allows chemical identification and, potentially, quantification of the acyl moieties. The method is based on cleavage of the fatty acids from proteins by hydrogenation with platinum (IV) oxide. This causes an acid transesterification of the acyl groups, adding an ethyl group to the carboxyl head of the fatty acid. The addition of the ethyl group reduces the polarity of the fatty acids, allowing their efficient separation by gas chromatography.

Indexed as

AcylationEsterificationGas Chromatography-Mass SpectrometryLipoylationProteinsProteomicsProteins

Identifiers

PMID20379138

What OpenQuestion holds

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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.