Evidence map›Paper›PMID 27148305›Full record

ArticleFrontiers in plant science2016

Proteomic Analysis of a Poplar Cell Suspension Culture Suggests a Major Role of Protein S-Acylation in Diverse Cellular Processes.

Vaibhav Srivastava, Joseph R Weber, Erik Malm, Bruce W Fouke, Vincent Bulone

Open access · goldAbstract read
In one paragraph

Article in Frontiers in plant science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-weighted citation impact, top 20% 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

14 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Global analysis of membrane protein S-acylation in the model plantbioRxiv : the preprint server for biology · 2025
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  13. Protein S-palmitoylation in cellular differentiation.Biochemical Society transactions · 2017
    Review
  14. Review
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 3 countries.

Vaibhav SrivastavaDivision of Glycoscience, School of Biotechnology, Royal Institute of Technology, AlbaNova University Centre Stockholm, Sweden.
Joseph R WeberRoy J. Carver Biotechnology Centre, Institute for Genomic Biology, University of Illinois Urbana-Champaign Urbana, IL, USA.
Erik MalmDivision of Glycoscience, School of Biotechnology, Royal Institute of Technology, AlbaNova University Centre Stockholm, Sweden.
Bruce W FoukeRoy J. Carver Biotechnology Centre, Institute for Genomic Biology, University of Illinois Urbana-Champaign Urbana, IL, USA.
Vincent BuloneDivision of Glycoscience, School of Biotechnology, Royal Institute of Technology, AlbaNova University CentreStockholm, Sweden; ARC Centre of Excellence in Plant Cell Walls and School of Agriculture, Food and Wine, The University of Adelaide, Waite CampusUrrbrae, SA, Australia.
AlbaNova · SEUniversity of Illinois Urbana-Champaign · USUniversity of Adelaide · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

S-acylation is a reversible post-translational modification of proteins known to be involved in membrane targeting, subcellular trafficking, and the determination of a great variety of functional properties of proteins. The aim of this work was to identify S-acylated proteins in poplar. The use of an acyl-biotin exchange method and mass spectrometry allowed the identification of around 450 S-acylated proteins, which were subdivided into three major groups of proteins involved in transport, signal transduction, and response to stress, respectively. The largest group of S-acylated proteins was the protein kinase superfamily. Soluble N-ethylmaleimide-sensitive factor-activating protein receptors, band 7 family proteins and tetraspanins, all primarily related to intracellular trafficking, were also identified. In addition, cell wall related proteins, including cellulose synthases and other glucan synthases, were found to be S-acylated. Twenty four of the identified S-acylated proteins were also enriched in detergent-resistant membrane microdomains, suggesting S-acylation plays a key role in the localization of proteins to specialized plasma membrane subdomains. This dataset promises to enhance our current understanding of the various functions of S-acylated proteins in plants.

Indexed as

mass spectrometrypalmitoylationpoplarpost-translational modificationS-acylationspectral counting

Identifiers

PMID27148305
PMCPMC4828459
OpenAlexW2328264310

What OpenQuestion holds

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LicenceCC BY
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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.