Evidence map›Paper›PMID 28485685›Full record

ArticleExperimental biology and medicine (Maywood, N.J.)2017

Protein palmitoylation: Palmitoyltransferases and their specificity.

Sabina Tabaczar, Aleksander Czogalla, Joanna Podkalicka, Agnieszka Biernatowska, Aleksander F Sikorski

Abstract read
In one paragraph

Article in Experimental biology and medicine (Maywood, N.J.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

64 citing papers in PubMed, 92 citations in OpenAlex.

  1. Article
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  4. Biochemistry · 2026
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  17. Genomic structural variations link multiple genes to bone mineral density in a multi-ethnic cohort study: Louisiana osteoporosis study.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2024
    Article
  18. Article
  19. Article
  20. Review

4 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

5 authors at 1 institution in 1 country.

Sabina TabaczarDepartment of Cytobiochemistry, Faculty of Biotechnology, University of Wrocław, 50-383 Wrocław, Poland.
Aleksander CzogallaDepartment of Cytobiochemistry, Faculty of Biotechnology, University of Wrocław, 50-383 Wrocław, Poland.
Joanna PodkalickaDepartment of Cytobiochemistry, Faculty of Biotechnology, University of Wrocław, 50-383 Wrocław, Poland.
Agnieszka BiernatowskaDepartment of Cytobiochemistry, Faculty of Biotechnology, University of Wrocław, 50-383 Wrocław, Poland.
Aleksander F SikorskiDepartment of Cytobiochemistry, Faculty of Biotechnology, University of Wrocław, 50-383 Wrocław, Poland.
University of Wrocław · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A plethora of novel information has emerged over the past decade regarding protein lipidation. The reversible attachment of palmitic acid to cysteine residues, termed S-palmitoylation, has focused a special attention. This is mainly due to the unique role of this modification in the regulation of protein trafficking and function. A large family of protein acyltransferases (PATs) containing a conserved aspartate-histidine-histidine-cysteine motif use ping-pong kinetic mechanism to catalyze S-palmitoylation of a substrate protein. Here, we discuss the topology of PAT proteins and their cellular localization. We will also give an overview of the mechanism of protein palmitoylation and how it is regulated. New information concerning the recent discovery of depalmitoylating enzymes belonging to the family of α/β-hydrolase domain-containing protein 17 (ABHD17A) is included. Considering the recent advances that have occurred in understanding the mechanisms underlying the interplay between palmitoylation and depalmitoylation, it is clear that we are beginning to understand the fundamental nature of how cellular signal-transduction mediates membrane-level organization in health and disease. Impact statement Protein palmitoylation is one of most important reversible post-translational modifications of protein function in cell-signaling systems. This review gathers the latest information on the molecular mechanism of protein palmitoyl transferase action. It also discusses the issue of substrate specificity of palmitoyl transferases. Another important question is the role of depalmitoylation enzymes. This review should help to formulate questions concerning the regulation of activity of particular PATs as well as of depalmitoylating enzymes (APT).

Indexed as

LipoylationProtein Processing, Post-TranslationalAcetyltransferasesGene Expression RegulationMembrane ProteinsSignal TransductionSubstrate SpecificityAcetyltransferasesMembrane Proteinsprotein acyltransferaseaspartate–histidine–histidine–cysteine proteindepalmitoylationLipidationpalmitoyltransferasesprotein acyl transferasesS-palmitoylation

Identifiers

PMID28485685
PMCPMC5478004
OpenAlexW2612642407

What OpenQuestion holds

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Registered trials

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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.