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Xavier Rebordosa

Researcher at Autonomous University of Barcelona

Publications -  10
Citations -  213

Xavier Rebordosa is an academic researcher from Autonomous University of Barcelona. The author has contributed to research in topics: Virus & Cellobiose. The author has an hindex of 6, co-authored 10 publications receiving 208 citations.

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Glycoprotein E of bovine herpesvirus type 1 is involved in virus transmission by direct cell-to-cell spread

TL;DR: Results indicate that those conditions which prevent the infection by direct adsorption to the cells (presence of a semi-solid medium or presence of neutralizing antibodies in the medium) selectively inhibit the growth of the gE- strain, suggesting that gE plays a central role in the BHV-1 spread by direct cell-to-cell transmission.
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Properties of a novel glucose-enhanced β-glucosidase purified from Streptomyces sp. (ATCC 11238)

TL;DR: An inducible intracellular beta-glucosidase from Streptomyces sp.
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A beta-glucosidase gene (bgl3) from Streptomyces sp. strain QM-B814. Molecular cloning, nucleotide sequence, purification and characterization of the encoded enzyme, a new member of family 1 glycosyl hydrolases.

TL;DR: An open-reading frame of 1440 nucleotides encoding a polypeptide of 479 amino acids was found by sequencing and the encoded protein appears to be a beta-glucosidase with broad substrate specificity, is active on cellooligomers, and performs transglycosylation reactions.
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Mapping, cloning and sequencing of a glycoprotein-encoding gene from bovine herpesvirus type 1 homologous to the gE gene from HSV-1

TL;DR: A region of the unique short sequence from the BHV-1 genome has been sequenced and presents substantial similarity to that of the glycoprotein gE from HSV- 1 and to homologous proteins of related viruses such as pseudorabies virus, equine herpesvirus type 1 and varicella zoster virus.
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Secretion-dependent proteolysis of recombinant proteins is associated with inhibition of cell growth in Escherichia coli

TL;DR: Recombinant cultures producing the periplasmic, but not the cytoplasmic form show a dramatic arrest of cell growth after induction of gene expression, indicative of toxicity associated to the recombinant protein itself or to its proteolytic processing.