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Angelo Fontana
Researcher at National Research Council
Publications - 392
Citations - 14287
Angelo Fontana is an academic researcher from National Research Council. The author has contributed to research in topics: Thermolysin & Circular dichroism. The author has an hindex of 52, co-authored 373 publications receiving 13216 citations. Previous affiliations of Angelo Fontana include University of Bari & University of Salerno.
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Journal ArticleDOI
Formation and inactivation of endogenous cannabinoid anandamide in central neurons.
V. Di Marzo,Angelo Fontana,Hugues Cadas,S. Schinelli,Guido Cimino,J.-C. Schwartz,Daniele Piomelli +6 more
TL;DR: It is reported that anandamide is produced in and released from cultured brain neurons in a calcium ion-dependent manner when the neurons are stimulated with membrane-depolarizing agents, indicating that multiple biochemical pathways may participate in an andamide formation in brain tissue.
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Probing protein structure by limited proteolysis.
Angelo Fontana,Patrizia Polverino de Laureto,Barbara Spolaore,Erica Frare,Paola Picotti,Marcello Zambonin +5 more
TL;DR: The results underscore the utility of the limited proteolysis approach for unravelling molecular features of proteins and appear to prompt its systematic use as a simple first step in the elucidation of structure-dynamics-function relationships of a novel and rare protein, especially if available in minute amounts.
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Tomographic flow cytometry by digital holography.
Francesco Merola,Pasquale Memmolo,Lisa Miccio,Roberto Savoia,Martina Mugnano,Angelo Fontana,Giuliana d'Ippolito,Angela Sardo,Achille Iolascon,Antonella Gambale,Pietro Ferraro +10 more
TL;DR: It is demonstrated that by exploiting the random rolling of cells while they are flowing along a microfluidic channel, it is possible to obtain in-line phase-contrast tomography, if smart strategies for wavefront analysis are adopted.
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Probing the partly folded states of proteins by limited proteolysis
Angelo Fontana,Patrizia Polverino de Laureto,Vincenzo De Filippis,Elena Scaramella,Marcello Zambonin +4 more
TL;DR: This review focuses on the use of proteolytic enzymes as probes of the structure and dynamics of folding intermediates and shows that this simple biochemical technique can provide useful information, complementing that obtained by other commonly used techniques and approaches.
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Correlation between sites of limited proteolysis and segmental mobility in thermolysin.
TL;DR: Findings emphasize that apparent thermal motion seen in protein crystals is relevant to motion in solution and appear to be of general significance in protein-protein recognition processes.