Evidence map›Paper›PMID 33784857›Full record

ReviewOpen biology2021

Regulatory effects of protein S-acylation on insulin secretion and insulin action.

Luke H Chamberlain, Michael J Shipston, Gwyn W Gould

Open access · goldAbstract readReview
In one paragraph

Review in Open biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

9 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Mechanisms and functions of protein S-acylation.Nature reviews. Molecular cell biology · 2024
    Review
  5. A Novel Peptide COXCurrent protein & peptide science · 2024
    Article
  6. Article
  7. Regulation of insulin secretion by the post-translational modifications.Frontiers in cell and developmental biology · 2023
    Review
  8. Review
  9. 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.

Luke H ChamberlainStrathclyde Institute of Pharmacy and Biomedical Sciences, University of Strathclyde, Glasgow, UK.
Michael J ShipstonCentre for Discovery Brain Sciences, Edinburgh Medical School: Biomedical Sciences, University of Edinburgh, Edinburgh, UK.
Gwyn W GouldStrathclyde Institute of Pharmacy and Biomedical Sciences, University of Strathclyde, Glasgow, UK.
University of Strathclyde · GBUniversity of Edinburgh · GB

Funding

Medical Research Council MR/R010668/1Medical Research Council MR/V012290/1
6 · The paper itself

Abstract

Post-translational modifications (PTMs) such as phosphorylation and ubiquitination are well-studied events with a recognized importance in all aspects of cellular function. By contrast, protein S-acylation, although a widespread PTM with important functions in most physiological systems, has received far less attention. Perturbations in S-acylation are linked to various disorders, including intellectual disability, cancer and diabetes, suggesting that this less-studied modification is likely to be of considerable biological importance. As an exemplar, in this review, we focus on the newly emerging links between S-acylation and the hormone insulin. Specifically, we examine how S-acylation regulates key components of the insulin secretion and insulin response pathways. The proteins discussed highlight the diverse array of proteins that are modified by S-acylation, including channels, transporters, receptors and trafficking proteins and also illustrate the diverse effects that S-acylation has on these proteins, from membrane binding and micro-localization to regulation of protein sorting and protein interactions.

Indexed as

Insulin SecretionProtein Processing, Post-TranslationalAcylationAnimalsHumansInsulinSignal TransductionInsulinacyl protein thioesteraseGLUT4insulin secretioninsulin signallingS-acylationzDHHC enzymes

Identifiers

PMID33784857
PMCPMC8061761
OpenAlexW3139403317

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.