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Antonio Casamayor

Researcher at Autonomous University of Barcelona

Publications -  67
Citations -  7129

Antonio Casamayor is an academic researcher from Autonomous University of Barcelona. The author has contributed to research in topics: Saccharomyces cerevisiae & Gene. The author has an hindex of 27, co-authored 60 publications receiving 6868 citations. Previous affiliations of Antonio Casamayor include University of Dundee & Yale University.

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Global analysis of protein activities using proteome chips

TL;DR: In this paper, the authors proposed a method for using proteome chips to systematically assay all protein interactions in a species in a high-throughput manner, and also related to methods for making protein arrays by attaching double-tagged fusion proteins to a solid support.
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Analysis of yeast protein kinases using protein chips.

TL;DR: A novel protein chip technology is developed that allows the high-throughput analysis of biochemical activities, and this approach is used to analyse nearly all of the protein kinases from Saccharomyces cerevisiae, finding many novel activities and that a large number ofprotein kinases are capable of phosphorylating tyrosine.
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3-Phosphoinositide-dependent protein kinase-1 (PDK1): structural and functional homology with the Drosophila DSTPK61 kinase.

TL;DR: Human PDK1 is homologous to the Drosophila protein kinase DSTPK61, which has been implicated in the regulation of sex differentiation, oogenesis and spermatogenesis and is likely to mediate the activation of PKB by insulin or growth factors.
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PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2

TL;DR: PDK1 and PDK2 might be the same enzyme, the substrate specificity and activity of PDK1 being regulated through its interaction with another protein(s), and PRK2 is a probable substrate for PDK 1.
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Role of phosphatidylinositol 3,4,5-trisphosphate in regulating the activity and localization of 3-phosphoinositide-dependent protein kinase-1.

TL;DR: Results indicate that PtdIns(3,4,5)P3 plays several roles in the PDK1-induced activation of P KBalpha, and binds to the PH domain of PKB, altering its conformation so that it can be activated by PDK 1.