Evidence map›Paper›PMID 23485398›Full record

ArticleBiochimica et biophysica acta2013

N-terminal palmitoylation is required for Toxoplasma gondii HSP20 inner membrane complex localization.

M G De Napoli, N de Miguel, M Lebrun, S N J Moreno, S O Angel, M M Corvi

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.1field-weighted citation impact, top 15% 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

18 citing papers in PubMed, 28 citations in OpenAlex.

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  18. Cell division in apicomplexan parasites.Nature reviews. Microbiology · 2014
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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

6 authors at 3 institutions in 4 countries.

M G De NapoliUniversidad Nacional de San Martín, Consejo Nacional de Investigaciones Científicas y Técnicas, Provincia de Buenos Aires, Argentina.
N de Miguel
M Lebrun
S N J Moreno
S O Angel
M M Corvi
Consejo Nacional de Investigaciones Científicas y Técnicas · ARCentre National de la Recherche Scientifique · FRUniversity of Georgia · US

Funding

The plant-like vacuole of Toxoplasma gondiiR01AI096836 · NIAID · UNIVERSITY OF GEORGIA · PI MORENO, SILVIA N · 2012 to 2016
$1.8M
Research on trypanosomatid and apicomplexan parasitesD43TW007888 · FIC · UNIVERSITY OF GEORGIA · PI DOCAMPO, ROBERTO · 2007 to 2011
$809k
Novel nucleosome composition and modifications in protozoal parasite Toxoplasma gR01AI083162 · NIAID · INSTITUTE/RESEARCH/BIOTECHNOLOGY FDN · PI ANGEL, SERGIO OSCAR · 2009 to 2012
$450k
FIC NIH HHS D43 TW007888FIC NIH HHS D43TW007888NIAID NIH HHS AI083162NIAID NIH HHS AI096836NIAID NIH HHS R01 AI083162NIAID NIH HHS R01 AI096836
6 · The paper itself

Abstract

Toxoplasma gondii is an obligate intracellular parasite and the causative agent of toxoplasmosis. Protein palmitoylation is known to play roles in signal transduction and in enhancing the hydrophobicity of proteins thus contributing to their membrane association. Global inhibition of protein palmitoylation has been shown to affect T. gondii physiology and invasion of the host cell. However, the proteins affected by this modification have been understudied. This paper shows that the small heat shock protein 20 from T. gondii (TgHSP20) is synthesized as a mature protein in the cytosol and is palmitoylated in three cysteine residues. However, its localization at the inner membrane complex (IMC) is dependent only on N-terminal palmitoylation. Absence or incomplete N-terminal palmitoylation causes TgHSP20 to partially accumulate in a membranous structure. Interestingly, TgHSP20 palmitoylation is not responsible for its interaction with the daughter cells IMCs. Together, our data describe the importance of palmitoylation in protein targeting to the IMC in T. gondii.

Indexed as

LipoylationBlotting, WesternCells, CulturedCysteineCytosolFibroblastsFluorescent Antibody TechniqueHSP20 Heat-Shock ProteinsHumansImmunoprecipitationIntracellular MembranesMutationProtein TransportSignal TransductionToxoplasmaToxoplasmosisCysteineHSP20 Heat-Shock Proteins

Identifiers

PMID23485398
PMCPMC3628096
OpenAlexW2154138962

What OpenQuestion holds

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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.