Evidence map›Paper›PMID 28392791›Full record

ReviewFrontiers in plant science2017

Progress toward Understanding Protein S-acylation: Prospective in Plants.

Yaxiao Li, Baoxiu Qi

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in plant science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

25 citing papers in PubMed, 48 citations in OpenAlex.

  1. Global analysis of membrane protein S-acylation in the model plantbioRxiv : the preprint server for biology · 2025
    Article
  2. Review
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  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
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  12. Review
  13. Alternative splicing ofFrontiers in plant science · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. HJournal of advanced research · 2020
    Review
  18. Knockout of the S-acyltransferase Gene,International journal of molecular sciences · 2019
    Article
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Yaxiao LiDepartment of Biology and Biochemistry, University of Bath Bath, UK.
Baoxiu QiDepartment of Biology and Biochemistry, University of Bath Bath, UK.
University of Bath · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

S-acylation, also known as S-palmitoylation or palmitoylation, is a reversible post-translational lipid modification in which long chain fatty acid, usually the 16-carbon palmitate, covalently attaches to a cysteine residue(s) throughout the protein via a thioester bond. It is involved in an array of important biological processes during growth and development, reproduction and stress responses in plant. S-acylation is a ubiquitous mechanism in eukaryotes catalyzed by a family of enzymes called Protein S-Acyl Transferases (PATs). Since the discovery of the first PAT in yeast in 2002 research in S-acylation has accelerated in the mammalian system and followed by in plant. However, it is still a difficult field to study due to the large number of PATs and even larger number of putative S-acylated substrate proteins they modify in each genome. This is coupled with drawbacks in the techniques used to study S-acylation, leading to the slower progress in this field compared to protein phosphorylation, for example. In this review we will summarize the discoveries made so far based on knowledge learnt from the characterization of protein S-acyltransferases and the S-acylated proteins, the interaction mechanisms between PAT and its specific substrate protein(s) in yeast and mammals. Research in protein S-acylation and PATs in plants will also be covered although this area is currently less well studied in yeast and mammalian systems.

Indexed as

lipid modificationmammalianPATsplantsS-acylationsubstrate recognition and specificityyeast

Identifiers

PMID28392791
PMCPMC5364179
OpenAlexW2602757324

What OpenQuestion holds

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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.