J
Josep A. Pérez-Pons
Researcher at Autonomous University of Barcelona
Publications - 22
Citations - 1050
Josep A. Pérez-Pons is an academic researcher from Autonomous University of Barcelona. The author has contributed to research in topics: Cellobiose & Virulence. The author has an hindex of 11, co-authored 21 publications receiving 1000 citations.
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Relation between amino acid composition and cellular location of proteins.
TL;DR: A correlation analysis of the amino acid composition and the cellular location of a protein is presented and a program (ProtLock) to predict the cellular where a protein has been designed is designed.
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Analysis of protein conformational characteristics related to thermostability
TL;DR: The thermal stability of proteins was studied, 195 single amino acid residue replacements reported elsewhere being analysed for several protein conformational characteristics.
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Molecular cloning, expression and nucleotide sequence of the endo-beta-1,3-1,4-D-glucanase gene from Bacillus licheniformis. Predictive structural analyses of the encoded polypeptide.
TL;DR: A tentative three-functional-domain structure for the enzyme is assigned (signal peptide, substrate binding and catalytic domains, and a putative lysozyme-like active site) from several structural predictive analyses performed.
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Glycoprotein E of bovine herpesvirus type 1 is involved in virus transmission by direct cell-to-cell spread
Xavier Rebordosa,Jaume Piñol,Josep A. Pérez-Pons,Jorge Lloberas,Jorge Lloberas,Jordi Naval,Xavier Serra-Hartmann,Enric Espuña,Enrique Querol +8 more
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.