Evidence map›Paper›PMID 15520806›Full record

ReviewEMBO reports2004

On the mechanism of protein palmitoylation.

Lars E P Dietrich, Christian Ungermann

Open access · greenAbstract readReview
In one paragraph

Review in EMBO reports, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
3.1field-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

59 citing papers in PubMed, 134 citations in OpenAlex.

  1. Profiling the landscape of cysteine posttranslational modifications in brain aging and neurodegeneration.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025
    Review
  2. Article
  3. Altered Protein Palmitoylation as Disease Mechanism in Neurodegenerative Disorders.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2024
    Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. APT1-Mediated Depalmitoylation Regulates Hippocampal Synaptic Plasticity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022
    Article
  10. Review
  11. Review
  12. Review
  13. Review
  14. Post-translational modifications of transporters.Pharmacology & therapeutics · 2018
    Review
  15. Review
  16. Article
  17. The Journal of biological chemistry · 2017
    Article
  18. Article
  19. Review
  20. Pharmacological Inhibition of Protein Lipidation.The Journal of membrane biology · 2015
    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.

Lars E P DietrichBiochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany.
Christian Ungermann
Heidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein palmitoylation or, more specifically, S-acylation is a reversible post-translational lipid modification. Despite the identification of several proteins that are altered in this way, our understanding of the enzymology of this process has been hampered by the lack of well-characterized acyltransferases. We now know of three proteins in Saccharomyces cerevisiae that promote palmitoylation: effector of Ras function (Erf2), ankyrin-repeat-containing protein (Akr1) and the SNARE protein Ykt6. Erf2 and Akr1 are integral membrane proteins that contain a cysteine-rich domain and an Asp-His-His-Cys motif, both of which catalyse acylation at the carboxyl terminus of their target proteins. Recently, we discovered that Ykt6 mediates the amino-terminal acylation of the fusion protein Vac8. Even though these three proteins differ in sequence, topology, size and substrate specificity, they might function in a similar manner. In this review, we discuss these observations in the context of a potential general mechanism of acylation.

Indexed as

AcylationFungal ProteinsLipidsModels, BiologicalPalmitic AcidProtein BindingProtein Processing, Post-TranslationalProteinsProtein Structure, TertiarySaccharomyces cerevisiaeSubstrate SpecificityFungal ProteinsLipidsPalmitic AcidProteins

Identifiers

PMID15520806
PMCPMC1299172
OpenAlexW2126722050

What OpenQuestion holds

Textmetadata
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.