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Antonio Bernad

Researcher at Spanish National Research Council

Publications -  147
Citations -  11591

Antonio Bernad is an academic researcher from Spanish National Research Council. The author has contributed to research in topics: DNA polymerase & Stem cell. The author has an hindex of 50, co-authored 142 publications receiving 10861 citations. Previous affiliations of Antonio Bernad include Centro Nacional de Investigaciones Cardiovasculares & Carlos III Health Institute.

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Unidirectional transfer of microRNA-loaded exosomes from T cells to antigen-presenting cells

TL;DR: It is shown that exosomes of T, B and dendritic immune cells contain microRNA (miRNA) repertoires that differ from those of their parent cells, and that miRNAs transferred during immune synapsis are able to modulate gene expression in recipient cells.
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Spontaneous human adult stem cell transformation

TL;DR: This is the first report of spontaneous transformation of human adult stem cells, supporting the hypothesis of cancer stem cell origin, and indicates the importance of biosafety studies of mesenchymal stem cell biology to efficiently exploit their full clinical therapeutic potential.
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Highly efficient DNA synthesis by the phage phi 29 DNA polymerase. Symmetrical mode of DNA replication.

TL;DR: In this article, it was shown that the phi 29 DNA polymerase is the only enzyme required for efficient DNA replication with the initiation primer as the only additional protein requirement, and that conditions that increase the stability of secondary structure in the template do not affect the processivity and strand displacement ability of the enzyme.
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Segregation of leading-edge and uropod components into specific lipid rafts during T cell polarization

TL;DR: The data suggest that raft partitioning is a major determinant for protein redistribution in polarized T cells, as ectopic expression of raft-associated proteins results in their asymmetric redistribution, whereas non-raft-partitioned mutants of these proteins are distributed homogeneously in the polarized cell membrane.
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A conserved 3'----5' exonuclease active site in prokaryotic and eukaryotic DNA polymerases.

TL;DR: Site-directed mutagenesis at the predicted exonuclease active site of the phi 29 DNA polymerase, a model enzyme for prokaryotic and eukaryotic alpha-like DNA polymerases, specifically inactivated the 3'----5' exonuclelease activity of the enzyme, reflecting a high evolutionary conservation of this catalytic domain.