Evidence map›Paper›PMID 26825284›Full record

ArticleBiochimica et biophysica acta2016

Identification of new palmitoylated proteins in Toxoplasma gondii.

Marina C Caballero, Andrés M Alonso, Bin Deng, Marcia Attias, Wanderley de Souza, María M Corvi

Open access · bronzeAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
6.0field-weighted citation impact, top 3% 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

19 citing papers in PubMed, 36 citations in OpenAlex.

  1. Proteomics Applications inPathogens (Basel, Switzerland) · 2023
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  10. Protein Palmitoylation Plays an Important Role inMolecular & cellular proteomics : MCP · 2018
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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 3 countries.

Marina C CaballeroLaboratorio de Parasitología Molecular, Instituto de Investigaciones Biotecnológicas-Instituto Tecnológico de Chascomús (IIB-INTECH), Universidad Nacional de San Martín (UNSAM) - Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Intendente Marino Km 8.2, B7130 Chascomús, Provincia de Buenos Aires, Argentina.
Andrés M AlonsoLaboratorio de Parasitología Molecular, Instituto de Investigaciones Biotecnológicas-Instituto Tecnológico de Chascomús (IIB-INTECH), Universidad Nacional de San Martín (UNSAM) - Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Intendente Marino Km 8.2, B7130 Chascomús, Provincia de Buenos Aires, Argentina.
Bin DengDepartment of Biology and Vermont Genetics Network Proteomics Facility, University of Vermont, 120A Marsh Life Science Building, Burlington, VT 05405-0086, USA.
Marcia AttiasLaboratório de Ultraestrutura Celular Hertha Meyer, Instituto de Biofísica, Carlos Chagas Filho and Instituto Nacional de Ciência e Tecnologia em Biologia Estrutural e Bioimagens, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil.
Wanderley de SouzaLaboratório de Ultraestrutura Celular Hertha Meyer, Instituto de Biofísica, Carlos Chagas Filho and Instituto Nacional de Ciência e Tecnologia em Biologia Estrutural e Bioimagens, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil.
María M CorviLaboratorio de Parasitología Molecular, Instituto de Investigaciones Biotecnológicas-Instituto Tecnológico de Chascomús (IIB-INTECH), Universidad Nacional de San Martín (UNSAM) - Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Intendente Marino Km 8.2, B7130 Chascomús, Provincia de Buenos Aires, Argentina. Electronic address: mcorvi@intech.gov.ar.
Consejo Nacional de Investigaciones Científicas y Técnicas · ARUniversidade Federal do Rio de Janeiro · BRUniversity of Vermont · US

Funding

Vermont INBRE Administrative Supplement 2024 AWD 118P20GM103449 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI CHRISTOPHER S FRANCKLYN · 2012 to 2026
$58.4M
NIGMS NIH HHS P20 GM103449
6 · The paper itself

Abstract

Protein palmitoylation has been shown to be an important post-translational modification in eukaryotic cells. This modification alters the localization and/or the function of the targeted protein. In recent years, protein palmitoylation has risen in importance in apicomplexan parasites as well. In Toxoplasma gondii, some proteins have been reported to be modified by palmitate. With the development of new techniques that allow the isolation of palmitoylated proteins, this significant post-translational modification has begun to be studied in more detail in T. gondii. Here we describe the palmitoylome of the tachyzoite stage of T. gondii using a combination of the acyl-biotin exchange chemistry method and mass spectrometry analysis. We identified 401 proteins found in multiple cellular compartments, with a wide range of functions that vary from metabolic processes, gliding and host-cell invasion to even regulation of transcription and translation. Besides, we found that more rhoptry proteins than the ones already described for Toxoplasma are palmitoylated, suggesting an important role for this modification in the invasion mechanism of the host-cell. This study documents that protein palmitoylation is a common modification in T. gondii that could have an impact on different cellular processes.

Indexed as

Protein Processing, Post-TranslationalLipoylationProtozoan ProteinsToxoplasmaProtozoan ProteinsAcyl-biotin exchangeHost-cell invasionPalmitoylomeProtein identificationRhoptryToxoplasma gondii

Identifiers

PMID26825284
PMCPMC4857766
OpenAlexW2251058886

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.