Evidence map›Paper›PMID 19152182›Full record

ReviewMolecular membrane biology2009

Palmitoyl acyltransferase assays and inhibitors (Review).

Jeremiah M Draper, Charles D Smith

Open access · greenAbstract readReview
In one paragraph

Review in Molecular membrane biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
1.5field-weighted citation impact, top 16% 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

49 citing papers in PubMed, 84 citations in OpenAlex.

  1. Article
  2. Advances and therapeutic opportunities in visual cycle modulation.Progress in retinal and eye research · 2025
    Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Destabilization of β Cell FIT2 by saturated fatty acids alter lipid droplet numbers and contribute to ER stress and diabetes.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Article
  11. Insights into auto-RSC chemical biology · 2021
    Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. Regulation of Dynamic Protein S-Acylation.Frontiers in molecular biosciences · 2021
    Review
  17. Review
  18. Article
  19. Article
  20. AMPAR Palmitoylation Tunes Synaptic Strength: Implications for Synaptic Plasticity and Disease.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2019
    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

2 authors at 1 institution in 1 country.

Jeremiah M DraperDepartment of Pharmaceutical and Biomedical Sciences, Medical University of South Carolina, Charleston, South Carolina 29425-1400, USA.
Charles D Smith
Medical University of South Carolina · US

Funding

ACYLTRANSFERASE INHIBITORS AS ANTI RAS AGENTSR01CA075248 · NCI · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI SMITH, CHARLES D. · 1997 to 2009
$2.2M
NCI NIH HHS R01 CA075248
6 · The paper itself

Abstract

Palmitoylated proteins have been implicated in several disease states including Huntington's, cardiovascular, T-cell mediated immune diseases, and cancer. To proceed with drug discovery efforts in this area, it is necessary to: identify the target enzymes, establish efficient assays for palmitoylation, and conduct high-throughput screening to identify inhibitors. The primary objectives of this review are to examine the types of assays used to study protein palmitoylation and to discuss the known inhibitors of palmitoylation. Six main palmitoylation assays are currently in use. Four assays, radiolabeled palmitate incorporation, fatty acyl exchange chemistry, MALDI-TOF MS and azido-fatty acid labeling are useful in the identification of palmitoylated proteins and palmitoyl acyltransferase (PAT) enzymes. Two other methods, the in vitro palmitoylation (IVP) assay and a cell-based peptide palmitoylation assay, are useful in the identification of PAT enzymes and are more amenable to screening for inhibitors of palmitoylation. To date, two general types of palmitoylation inhibitors have been identified. Lipid-based palmitoylation inhibitors broadly inhibit the palmitoylation of proteins; however, the mechanism of action of these compounds is unknown, and each also has effects on fatty acid biosynthesis. Conversely, several non-lipid palmitoylation inhibitors have been shown to selectively inhibit the palmitoylation of different PAT recognition motifs. The selective nature of these compounds suggests that they may act as protein substrate competitors, and may produce fewer non-specific effects. Therefore, these molecules may serve as lead compounds for the further development of selective inhibitors of palmitoylation, which may lead to new therapeutics for cancer and other diseases.

Indexed as

AcyltransferasesDrug DiscoveryEnzyme InhibitorsHumansLipoylationAcyltransferasesEnzyme Inhibitors

Identifiers

PMID19152182
PMCPMC2635919
OpenAlexW2028824717

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.