Evidence map›Paper›PMID 38355760›Full record

ReviewNature reviews. Molecular cell biology2024

Mechanisms and functions of protein S-acylation.

Francisco S Mesquita, Laurence Abrami, Maurine E Linder, Shernaz X Bamji, Bryan C Dickinson, F Gisou van der Goot

Open access · greenAbstract readReview
In one paragraph

Review in Nature reviews. Molecular cell biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 140 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
140citing papers in PubMed, 1 pooled it
40.2field-weighted citation impact, top 1% 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

140 citing papers in PubMed, 1 synthesis or guideline pooled it, 172 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Loss of Intestinal MSTN Promotes GLP-1 Secretion Through SGLT1 Palmitoylation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Metrnl in mitigating radiation enteritisActa pharmaceutica Sinica. B · 2026
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Advances in Lipid Metabolism Reprogramming in Hepatocellular Carcinoma.Journal of clinical and translational hepatology · 2026
    Review
  18. Article
  19. Article
  20. Review

80 more citing papers are in PubMed but not listed here.

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

6 authors at 4 institutions in 3 countries.

Francisco S MesquitaGlobal Health Institute, School of Life Sciences, École Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland.
Laurence AbramiGlobal Health Institute, School of Life Sciences, École Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland.ORCID http://orcid.org/0000-0002-1774-0481
Maurine E LinderDepartment of Molecular Medicine, Cornell University, Ithaca, NY, USA.ORCID http://orcid.org/0000-0003-2202-9712
Shernaz X BamjiDepartment of Cellular and Physiological Sciences, University of British Columbia, Vancouver, British Columbia, Canada.
Bryan C DickinsonDepartment of Chemistry, University of Chicago, Chicago, IL, USA.
F Gisou van der GootGlobal Health Institute, School of Life Sciences, École Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland. gisou.vandergoot@epfl.ch.ORCID http://orcid.org/0000-0002-8522-274X
École Polytechnique Fédérale de Lausanne · CHCornell University · USUniversity of British Columbia · CAUniversity of Chicago · US

Funding

Rapid selection approaches to understand and reprogram proteins and peptidesR35GM119840 · NIGMS · UNIVERSITY OF CHICAGO · PI Bryan Dickinson · 2016 to 2026
$4.8M
NIGMS NIH HHS R35 GM119840
6 · The paper itself

Abstract

Over the past two decades, protein S-acylation (often referred to as S-palmitoylation) has emerged as an important regulator of vital signalling pathways. S-Acylation is a reversible post-translational modification that involves the attachment of a fatty acid to a protein. Maintenance of the equilibrium between protein S-acylation and deacylation has demonstrated profound effects on various cellular processes, including innate immunity, inflammation, glucose metabolism and fat metabolism, as well as on brain and heart function. This Review provides an overview of current understanding of S-acylation and deacylation enzymes, their spatiotemporal regulation by sophisticated multilayered mechanisms, and their influence on protein function, cellular processes and physiological pathways. Furthermore, we examine how disruptions in protein S-acylation are associated with a broad spectrum of diseases from cancer to autoinflammatory disorders and neurological conditions.

Indexed as

Protein Processing, Post-TranslationalAcylationAnimalsHumansLipoylationProteinsSignal TransductionProteins

Identifiers

PMID38355760
PMCPMC12010433
OpenAlexW4391823142

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.