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Ester Gea-Mallorquí

Researcher at PSL Research University

Publications -  17
Citations -  529

Ester Gea-Mallorquí is an academic researcher from PSL Research University. The author has contributed to research in topics: Medicine & Population. The author has an hindex of 5, co-authored 8 publications receiving 402 citations. Previous affiliations of Ester Gea-Mallorquí include University of Barcelona & Concordia University.

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Constitutive Siglec-1 expression confers susceptibility to HIV-1 infection of human dendritic cell precursors

TL;DR: It is shown that pre-DCs, but not other blood DC subsets, are susceptible to infection by HIV-1 in a Siglec-1–dependent manner, a unique functional feature that might represent a preferential relationship of this emerging cell type with viruses.
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Pre-clinical development of BCG.HIVACAT, an antibiotic-free selection strain, for HIV-TB pediatric vaccine vectored by Lysine Auxotroph of BCG

TL;DR: T-cell immunogenicity of a novel, safer, GLP-compatible BCG-vectored vaccine using prototype immunogen HIVA is demonstrated and second generation immunogens derived from HIV-1 as well as other major pediatric pathogens can be constructed in a similar fashion to prime protective responses soon after birth.
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Engineering new mycobacterial vaccine design for HIV-TB pediatric vaccine vectored by lysine auxotroph of BCG.

TL;DR: This antibiotic-free plasmid selection system based on “double” auxotrophic complementation might be a new mycobacterial vaccine platform to develop not only recombinant BCG-based vaccines expressing second generation of HIV-1 immunogens but also other major pediatric pathogens to prime protective response soon after birth.
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The ability of an arginine to tryptophan substitution in Saccharomyces cerevisiae tRNA nucleotidyltransferase to alleviate a temperature-sensitive phenotype suggests a role for motif C in active site organization.

TL;DR: The results, along with overexpression and deletion analyses, show that the ts phenotype of cca1-E189F does not arise from thermal instability of the variant tRNA nucleotidyltransferase but instead from the inability of a partially active enzyme to support growth only at higher temperatures.