Evidence map›Paper›PMID 29239216›Full record

ReviewCritical reviews in biochemistry and molecular biology2018

Protein depalmitoylases.

Sang Joon Won, Melanie Cheung See Kit, Brent R Martin

Open access · greenAbstract readReview
In one paragraph

Review in Critical reviews in biochemistry and molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 126 papers.

0numbers the graph read from it
0cells of the map it votes in
126citing papers in PubMed
4.5field-weighted citation impact, top 4% 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

126 citing papers in PubMed, 181 citations in OpenAlex.

  1. Review
  2. Loss of Intestinal MSTN Promotes GLP-1 Secretion Through SGLT1 Palmitoylation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  3. Article
  4. Review
  5. Review
  6. Transcriptome Sequencing of LYPLA1 Gene Overexpression and Interference.Animals : an open access journal from MDPI · 2026
    Article
  7. Article
  8. Biochemistry · 2026
    Review
  9. Review
  10. Article
  11. Review
  12. ProteinJournal of pharmaceutical analysis · 2026
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Crosstalk between protein lipidation and ubiquitination in tumor biology.Apoptosis : an international journal on programmed cell death · 2026
    Review
  18. Article
  19. Article
  20. Review

66 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

3 authors at 1 institution in 1 country.

Sang Joon Wona Program in Chemical Biology , University of Michigan , Ann Arbor , MI , USA.
Melanie Cheung See Kitb Department of Chemistry , University of Michigan , Ann Arbor , MI , USA.
Brent R Martina Program in Chemical Biology , University of Michigan , Ann Arbor , MI , USA.ORCID 0000-0002-7136-2397
University of Michigan · US

Funding

Multiscale chemical approaches to map oxidative stressDP2GM114848 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MARTIN, BRENT RANDALL · 2014 to 2014
$2.2M
NIGMS NIH HHS DP2 GM114848
6 · The paper itself

Abstract

Protein depalmitoylation describes the removal of thioester-linked long chain fatty acids from cysteine residues in proteins. For many S-palmitoylated proteins, this process is promoted by acyl protein thioesterase enzymes, which catalyze thioester hydrolysis to solubilize and displace substrate proteins from membranes. The closely related enzymes acyl protein thioesterase 1 (APT1; LYPLA1) and acyl protein thioesterase 2 (APT2; LYPLA2) were initially identified from biochemical assays as G protein depalmitoylases, yet later were shown to accept a number of S-palmitoylated protein and phospholipid substrates. Leveraging the development of isoform-selective APT inhibitors, several studies report distinct roles for APT enzymes in growth factor and hormonal signaling. Recent crystal structures of APT1 and APT2 reveal convergent acyl binding channels, suggesting additional factors beyond acyl chain recognition mediate substrate selection. In addition to APT enzymes, the ABHD17 family of hydrolases contributes to the depalmitoylation of Ras-family GTPases and synaptic proteins. Overall, enzymatic depalmitoylation ensures efficient membrane targeting by balancing the palmitoylation cycle, and may play additional roles in signaling, growth, and cell organization. In this review, we provide a perspective on the biochemical, structural, and cellular analysis of protein depalmitoylases, and outline opportunities for future studies of systems-wide analysis of protein depalmitoylation.

Indexed as

LipoylationProtein Processing, Post-TranslationalAnimalsHumansModels, MolecularMonoacylglycerol LipasesProteinsSerine ProteasesThiolester HydrolasesMonoacylglycerol LipasesProteinsSerine ProteasesThiolester HydrolasesinhibitorPalmitoylationpost-translational modificationserine hydrolasethioesterase

Identifiers

PMID29239216
PMCPMC6009847
OpenAlexW4233242988

What OpenQuestion holds

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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.