Evidence map›Paper›PMID 28228066›Full record

ReviewCritical reviews in biochemistry and molecular biology2017

Dynamic protein S-palmitoylation mediates parasite life cycle progression and diverse mechanisms of virulence.

Robert W B Brown, Aabha I Sharma, David M Engman

Open access · greenAbstract readReview
In one paragraph

Review in Critical reviews in biochemistry and molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.6field-weighted citation impact, top 12% 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

15 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Posttranslational modifications in proteins: resources, tools and prediction methods.Database : the journal of biological databases and curation · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. 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

3 authors at 2 institutions in 1 country.

Robert W B Browna Department of Pathology and Laboratory Medicine , Cedars-Sinai Medical Center , Los Angeles , CA , USA.
Aabha I Sharmab Departments of Pathology and Microbiology-Immunology , Northwestern University , Chicago , IL , USA.
David M Engmana Department of Pathology and Laboratory Medicine , Cedars-Sinai Medical Center , Los Angeles , CA , USA.
Northwestern University · USCedars-Sinai Medical Center · US

Funding

Northwestern University Clinical and Translational Science Institute (NUCATS)UL1TR001422 · NCATS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI D'AQUILA, RICHARD · 2015 to 2023
$56.8M
Global Characterization of Protein Palmitoylation in TrypanosomesR01GM102689 · NIGMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI ENGMAN, DAVID M. · 2013 to 2016
$1.5M
NCATS NIH HHS UL1 TR001422NIGMS NIH HHS R01 GM102689
6 · The paper itself

Abstract

Eukaryotic parasites possess complex life cycles and utilize an assortment of molecular mechanisms to overcome physical barriers, suppress and/or bypass the host immune response, including invading host cells where they can replicate in a protected intracellular niche. Protein S-palmitoylation is a dynamic post-translational modification in which the fatty acid palmitate is covalently linked to cysteine residues on proteins by the enzyme palmitoyl acyltransferase (PAT) and can be removed by lysosomal palmitoyl-protein thioesterase (PPT) or cytosolic acyl-protein thioesterase (APT). In addition to anchoring proteins to intracellular membranes, functions of dynamic palmitoylation include - targeting proteins to specific intracellular compartments via trafficking pathways, regulating the cycling of proteins between membranes, modulating protein function and regulating protein stability. Recent studies in the eukaryotic parasites - Plasmodium falciparum, Toxoplasma gondii, Trypanosoma brucei, Cryptococcus neoformans and Giardia lamblia - have identified large families of PATs and palmitoylated proteins. Many palmitoylated proteins are important for diverse aspects of pathogenesis, including differentiation into infective life cycle stages, biogenesis and tethering of secretory organelles, assembling the machinery powering motility and targeting virulence factors to the plasma membrane. This review aims to summarize our current knowledge of palmitoylation in eukaryotic parasites, highlighting five exemplary mechanisms of parasite virulence dependent on palmitoylation.

Indexed as

LipoylationAnimalsHost-Parasite InteractionsHumansMalariaPlasmodiumProtozoan InfectionsProtozoan ProteinsToxoplasmaToxoplasmosisTrypanosomaTrypanosomiasisVirulenceProtozoan ProteinsGiardiapalmitoyl acyltransferasePalmitoylationpathogenesisPlasmodiumToxoplasmaTrypanosoma

Identifiers

PMID28228066
PMCPMC5560270
OpenAlexW2591227622

What OpenQuestion holds

Textmetadata
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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.