Evidence map›Paper›PMID 28193150›Full record

ArticleBioTechniques2017

Maleimide scavenging enhances determination of protein S-palmitoylation state in acyl-exchange methods.

Charlotte H Hurst, Dionne Turnbull, Fiona Plain, William Fuller, Piers A Hemsley

Open access · goldAbstract read
In one paragraph

Article in BioTechniques, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

21 citing papers in PubMed, 34 citations in OpenAlex.

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  16. Open biology · 2022
    Review
  17. Proteome-Scale Analysis of ProteinJournal of proteome research · 2021
    Review
  18. Article
  19. Article
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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 2 institutions in 1 country.

Charlotte H HurstDivision of Plant Sciences, School of Life Sciences, University of Dundee, Dundee, UK; Cell and Molecular Sciences, The James Hutton Institute, Invergowrie, UK.
Dionne TurnbullDivision of Plant Sciences, School of Life Sciences, University of Dundee, Dundee, UK.
Fiona PlainDivision of Cardiovascular and Diabetes Medicine, Medical Research Institute, School of Medicine, Dentistry, and Nursing, University of Dundee, Dundee, UK.
William FullerDivision of Cardiovascular and Diabetes Medicine, Medical Research Institute, School of Medicine, Dentistry, and Nursing, University of Dundee, Dundee, UK.
Piers A HemsleyDivision of Plant Sciences, School of Life Sciences, University of Dundee, Dundee, UK; Cell and Molecular Sciences, The James Hutton Institute, Invergowrie, UK.
University of Dundee · GBJames Hutton Institute · GB

Funding

Biotechnology and Biological Sciences Research Council BB/M024911/1British Heart Foundation FS/13/22/30126British Heart Foundation FS/14/68/30988British Heart Foundation PG/12/6/29366British Heart Foundation PG/15/42/31563British Heart Foundation PG/16/33/32134
6 · The paper itself

Abstract

S-palmitoylation (S-acylation) is emerging as an important dynamic post-translational modification of cysteine residues within proteins. Current assays for protein S-palmitoylation involve either in vivo labeling or chemical cleavage of S-palmitoyl groups to reveal a free cysteine sulfhydryl that can be subsequently labeled with an affinity handle (acyl-exchange). Assays for protein S-palmitoylation using acyl-exchange chemistry therefore require blocking of non-S-palmitoylated cysteines, typically using N-ethylmaleimide (NEM), to prevent non-specific detection. This in turn necessitates multiple precipitation-based clean-up steps to remove reagents between stages, often leading to variable sample loss, reduced signal, or protein aggregation. These combine to reduce the sensitivity, reliability, and accuracy of these assays, which also require a substantial amount of time to perform. By substituting these precipitation steps with chemical scavenging of NEM by 2,3-dimethyl-1,3-butadiene in an aqueous Diels-Alder 4+2 cyclo-addition reaction, it is possible to greatly improve sensitivity and accuracy while reducing the hands-on time and overall time required for the assay.

Indexed as

Protein Processing, Post-TranslationalAcylationAlkenesArabidopsisButanesCysteineEthylmaleimideLipoylationMaleimidesProteinsReproducibility of Results2,3-dimethyl-1,3-butadieneAlkenesButanesCysteineEthylmaleimideMaleimidesProteinsABEacyl biotin exchangeacyl-RACbiotin switchcysteineDiels-AldermaleimideN-ethylmaleimidepalmitoylationS-acylationS-palmitoylationthiol

Identifiers

PMID28193150
PMCPMC5400063
OpenAlexW2588073561

What OpenQuestion holds

Textmetadata
LicenceTDM
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.