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Antonio Barragan

Researcher at Stockholm University

Publications -  69
Citations -  4758

Antonio Barragan is an academic researcher from Stockholm University. The author has contributed to research in topics: Toxoplasma gondii & Immune system. The author has an hindex of 33, co-authored 64 publications receiving 4160 citations. Previous affiliations of Antonio Barragan include Washington University in St. Louis & Swedish Institute.

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A secreted serine-threonine kinase determines virulence in the eukaryotic pathogen Toxoplasma gondii.

TL;DR: Genetic mapping revealed two closely adjacent quantitative trait loci on parasite chromosome VIIa that control the extreme virulence of the type I lineage and identified the candidate virulence gene ROP18, a highly polymorphic serine-threonine kinase that was secreted into the host cell during parasite invasion.
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Identification of Plasmodium falciparum Erythrocyte Membrane Protein 1 (PfEMP1) as the Rosetting Ligand of the Malaria Parasite P. falciparum

TL;DR: The identification by single-cell reverse transcriptase PCR and cDNA cloning of the adhesive ligand P. falciparum erythrocyte membrane protein 1 (PfEMP1) is reported on, suggesting PfEMP1 is suggested to be the rosetting ligand and heparan sulfate, or a heparin-Sepharose–like molecule, the receptor both for Pf EMP1 binding and naturally formed ery throatcyte rosettes.
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Transepithelial Migration of Toxoplasma gondii Is Linked to Parasite Motility and Virulence

TL;DR: The potential to up-regulate migratory capacity in T. gondii likely plays an important role in establishing new infections and in dissemination upon reactivation of chronic infections.
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Induction of dendritic cell migration upon Toxoplasma gondii infection potentiates parasite dissemination

TL;DR: Findings show that Toxoplasma is able to subvert the regulation of host cell motility and likely exploits the host’s natural pathways of cellular migration for parasite dissemination.
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The Semiconserved Head Structure of Plasmodium falciparum Erythrocyte Membrane Protein 1 Mediates Binding to Multiple Independent Host Receptors

TL;DR: The exceptional binding activity of the PfEMP1 head structure and its relatively conserved nature argues that it holds an important role in erythrocyte sequestration and therefore in the virulence of the malaria parasite.