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Elena Zocchi

Researcher at University of Genoa

Publications -  134
Citations -  5726

Elena Zocchi is an academic researcher from University of Genoa. The author has contributed to research in topics: Cyclic ADP-ribose & NAD+ kinase. The author has an hindex of 42, co-authored 130 publications receiving 5197 citations. Previous affiliations of Elena Zocchi include University of Geneva.

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Connexin 43 hemichannels mediate Ca2+-regulated transmembrane NAD+ fluxes in intact cells

TL;DR: The pleiotropy of NAD+‐dependent cellular events, including redox reactions, signaling, and DNA repair, implicates Cx43 hemichannels in intercellular NAD+ trafficking, which suggests new paracrine functions of NAD+.
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A Single Protein Immunologically Identified as CD38 Displays NAD+ Glycohydrolase, ADP-Ribosyl Cyclase and Cyclic ADP-Ribose Hydrolase Activities at the Outer Surface of Human Erythrocytes

TL;DR: The purification procedure involved three sequential chromatography steps on hydroxylapatite, immobilized Cu++ and immobilized anti-CD38 monoclonal antibody resins, which yielded a single 46 kDa protein displaying all three enzymatic activities.
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Autocrine and Paracrine Calcium Signaling by the CD38/NAD+/Cyclic ADP‐Ribose System

TL;DR: This paradox is solved by identifying some NAD+ and cADPR transmembrane transporters, whose interplay mediates a hitherto‐unrecognized subcellular and intercellular trafficking of nucleotides that enhances intracellular Ca2+ ([Ca2+]i).
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Abscisic acid is an endogenous cytokine in human granulocytes with cyclic ADP-ribose as second messenger

TL;DR: Evidence that ABA stimulates several functional activities of human granulocytes through a signaling pathway sequentially involving a pertussis toxin (PTX)-sensitive G protein/receptor complex, protein kinase A activation, ADP-ribosyl cyclase phosphorylation, and consequent cyclic-ADp-ribose overproduction is provided.
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The transmembrane glycoprotein CD38 is a catalytically active transporter responsible for generation and influx of the second messenger cyclic ADP-ribose across membranes

TL;DR: It is demonstrated that the catalytic functioning of CD38 is accompanied by a cADPR (cGDPR) ‐transporting activity across natural and artificial membranes, which suggests that transmembrane juxtaposition of two or four CD38 monomers can generate a catalytically active channel for selective formation and influx of cADP‐responsive intracellular calcium stores.