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Mirella S. Pilone

Researcher at University of Insubria

Publications -  51
Citations -  3040

Mirella S. Pilone is an academic researcher from University of Insubria. The author has contributed to research in topics: D-amino acid oxidase & Flavoprotein. The author has an hindex of 31, co-authored 51 publications receiving 2862 citations. Previous affiliations of Mirella S. Pilone include University of Naples Federico II.

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Physiological functions of D-amino acid oxidases: from yeast to humans

TL;DR: Current research is attempting to delineate the regulation of DAAO functions in the contest of complex biochemical and physiological networks.
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D-Amino acid oxidase: new findings.

TL;DR: The active site can be clearly depicted: the striking absence of essential residues acting in acid-base catalysis and the mode of substrate orientation into the active site clearly support a hydrid transfer type of mechanism in which the orbital steering between the substrate and the isoalloxazine atoms plays a crucial role during catalysis.
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The x-ray structure of d-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation

TL;DR: The very high-resolution structures of yeast DAAO complexed with d-alanine, d-trifluoroalanines, and l-lactate provide strong evidence for hydride transfer as the mechanism of dehydrogenation, and point to orbital orientation/steering as the major factor in catalysis.
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PLG72 Modulates Intracellular D-Serine Levels through Its Interaction with D-Amino Acid Oxidase : EFFECT ON SCHIZOPHRENIA SUSCEPTIBILITY

TL;DR: It is demonstrated that overexpression of hDAAO in glioblastoma cells decreases the levels of d-serine, an effect that is null when p LG72 is coexpressed, indicating that pLG72 acts as a negative effector of h DAAO.
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Properties and applications of microbial D-amino acid oxidases: current state and perspectives.

TL;DR: The aim of this paper is to provide an overview of the main biotechnological applications of DAAO (ranging from biocatalysis to convert cephalosporin C into 7-amino cep Halosporanic acid to gene therapy for tumor treatment) and to illustrate the advantages of using the microbial DAAOs, employing both the native and the improved DAAo variants obtained by enzyme engineering.