Evidence map›Paper›PMID 26468752›Full record

ArticleCell host & microbe2015

Global Analysis of Palmitoylated Proteins in Toxoplasma gondii.

Ian T Foe, Matthew A Child, Jaimeen D Majmudar, Shruthi Krishnamurthy, Wouter A van der Linden, Gary E Ward, Brent R Martin, Matthew Bogyo

Open access · bronzeAbstract read
In one paragraph

Article in Cell host & microbe, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
7.5field-weighted citation impact, top 2% 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

53 citing papers in PubMed, 85 citations in OpenAlex.

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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

8 authors at 3 institutions in 1 country.

Ian T FoeDepartment of Pathology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Matthew A ChildDepartment of Pathology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Jaimeen D MajmudarDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.
Shruthi KrishnamurthyDepartment of Microbiology and Molecular Genetics, University of Vermont, Burlington, VT 05405, USA.
Wouter A van der LindenDepartment of Pathology, Stanford University School of Medicine, Stanford, CA 94305, USA.
Gary E WardDepartment of Microbiology and Molecular Genetics, University of Vermont, Burlington, VT 05405, USA.
Brent R MartinDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA. Electronic address: brentrm@umich.edu.
Matthew BogyoDepartment of Pathology, Stanford University School of Medicine, Stanford, CA 94305, USA; Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA. Electronic address: mbogyo@stanford.edu.
Stanford University · USUniversity of Michigan–Ann Arbor · USUniversity of Vermont · US

Funding

MOLECULAR BASIS OF HOST-PARASITE INTERACTIONT32AI007328 · NIAID · STANFORD UNIVERSITY · PI JUSTIN L SONNENBURG · 1987 to 2026
$11.9M
Vermont Immunobioloigy/ Infectious Diseases CenterP20GM103496 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI BUDD, RALPH C · 2012 to 2015
$8.7M
Multiscale chemical approaches to map oxidative stressDP2GM114848 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MARTIN, BRENT RANDALL · 2014 to 2014
$2.2M
Functional Analysis of the T. gondii AMA1 Cytosolic TailR01AI105191 · NIAID · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI WARD, GARY E · 2014 to 2018
$1.9M
Functional Studies of Toxoplasma gondii AMA1 and AMA2R01AI063276 · NIAID · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI WARD, GARY E · 2005 to 2010
$1.8M
Equipment supplement for Chemical methods to study protein palmitoylation pathwaysR01GM111703 · NIGMS · STANFORD UNIVERSITY · PI BOGYO, MATTHEW · 2014 to 2017
$1.6M
Quantitative chemical proteomics of dynamic palmitoylation in cellsR00CA151460 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI MARTIN, BRENT RANDALL · 2011 to 2013
$769k
NCCDPHP CDC HHS DP2GM114848NCI NIH HHS R00 CA151460NCI NIH HHS R00CA151460NIAID NIH HHS 5T32AI007328NIAID NIH HHS R01 AI063276NIAID NIH HHS R01AI063276NIAID NIH HHS R01 AI105191NIAID NIH HHS T32 AI007328NIGMS NIH HHS DP2 GM114848NIGMS NIH HHS P20 GM103496NIGMS NIH HHS R01 GM111703NIGMS NIH HHS R01GM111703
6 · The paper itself

Abstract

Post-translational modifications (PTMs) such as palmitoylation are critical for the lytic cycle of the protozoan parasite Toxoplasma gondii. While palmitoylation is involved in invasion, motility, and cell morphology, the proteins that utilize this PTM remain largely unknown. Using a chemical proteomic approach, we report a comprehensive analysis of palmitoylated proteins in T. gondii, identifying a total of 282 proteins, including cytosolic, membrane-associated, and transmembrane proteins. From this large set of palmitoylated targets, we validate palmitoylation of proteins involved in motility (myosin light chain 1, myosin A), cell morphology (PhIL1), and host cell invasion (apical membrane antigen 1, AMA1). Further studies reveal that blocking AMA1 palmitoylation enhances the release of AMA1 and other invasion-related proteins from apical secretory organelles, suggesting a previously unrecognized role for AMA1. These findings suggest that palmitoylation is ubiquitous throughout the T. gondii proteome and reveal insights into the biology of this important human pathogen.

Indexed as

Protein Processing, Post-TranslationalEndocytosisHumansLocomotionPalmitic AcidsProteinsProteomeToxoplasmaVirulencePalmitic AcidsProteinsProteome

Identifiers

PMID26468752
PMCPMC4694575
OpenAlexW1901593931

What OpenQuestion holds

Textmetadata
LicenceTDM
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.