F
Fabio Benfenati
Researcher at Istituto Italiano di Tecnologia
Publications - 424
Citations - 24243
Fabio Benfenati is an academic researcher from Istituto Italiano di Tecnologia. The author has contributed to research in topics: Synapsin & Synapsin I. The author has an hindex of 77, co-authored 406 publications receiving 21422 citations. Previous affiliations of Fabio Benfenati include University of Padua & University of Modena and Reggio Emilia.
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Journal ArticleDOI
Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin
Giampietro Schiavo,Fabio Benfenati,Bernard Poulain,Ornella Rossetto,Patrizia Polverino de Laureto,Bibhuti R. DasGupta,Cesare Montecucco +6 more
TL;DR: The results indicate that tetanus and botulinum B neurotoxins block neurotransmitter release by cleaving synaptobrevin-2, a protein that, on the basis of the results, seems to play a key part in neurotransmitterRelease.
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Synaptic Vesicle Phosphoproteins and Regulation of Synaptic Function
TL;DR: Current understanding of the mechanism by which synapsin I modulates communication between nerve cells is described and the properties and putative functions of other phosphoproteins associated with synaptic vesicles are reviewed.
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The synapsins: Key actors of synapse function and plasticity
TL;DR: A comprehensive description of the molecular basis ofsynapsin function is given, as well as an overview of the more recent evidence linking mutations in the synapsin proteins to the onset of severe central nervous system diseases such as epilepsy and schizophrenia.
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Identification of the nerve terminal targets of botulinum neurotoxin serotypes A, D, and E.
Giampietro Schiavo,Ornella Rossetto,S Catsicas,Patrizia Polverino de Laureto,B.R. DasGupta,Fabio Benfenati,Cesare Montecucco +6 more
TL;DR: It is shown that botulinum neurotoxin serotypes A, D, and E are zinc endoproteases specific for components of the synaptic vesicle docking and fusion complex, and the proteolytic activity of these neurotoxins is inhibited by EDTA and captopril.
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Botulinum neurotoxins serotypes A and E cleave SNAP-25 at distinct COOH-terminal peptide bonds
Giampietro Schiavo,Annalisa Santucci,Bibhuti R. DasGupta,Prashant P. Mehta,Jaime Jontes,Fabio Benfenati,Michael Wilson,Cesare Montecucco +7 more
TL;DR: Results indicate that the carboxyl‐terminal region of SNAP‐25 plays a crucial role in the multi‐protein complex that mediates vesicle docking and fusion at the nerve terminal.