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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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TBC1D24, an ARF6-Interacting Protein, Is Mutated in Familial Infantile Myoclonic Epilepsy

TL;DR: A gene mutation involved in autosomal-recessive idiopathic epilepsy is identified, the involvement of ARF6-dependent molecular pathway in brain hyperexcitability and seizures is unveiled, and the emerging role of subtle cytoarchitectural alterations in the etiology of this group of common epileptic disorders is confirmed.
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Electrostatic and hydrophobic interactions of synapsin I and synapsin I fragments with phospholipid bilayers.

TL;DR: The interaction between synapsin I and phospholipid vesicles has been characterized, and the protein domains involved in these interactions have been identified.
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Synapsin Controls Both Reserve and Releasable Synaptic Vesicle Pools during Neuronal Activity and Short-Term Plasticity inAplysia

TL;DR: The data demonstrate that the presence of synapsin-dependent reserve vesicles allows the nerve terminal to release neurotransmitter at rates exceeding the synaptic vesicle recycling capacity and to dynamically change the efficiency of release in response to conditioning stimuli.
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Photothermal cellular stimulation in functional bio-polymer interfaces

TL;DR: This work identifies and fully characterize two concomitant mechanisms, leading to membrane depolarization and hyperpolarisation, both mediated by a thermal effect in Human Embryonic Kidney cells grown on top of a poly(3-hexylthiophene) (P3HT) thin film.
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Structural Domains Involved in the Regulation of Transmitter Release by Synapsins

TL;DR: Interactions of domains C and E with the actin cytoskeleton may allow synapsins to perform two roles in regulating release, whereas domain A has an actin-independent function that regulates transmitter release in a phosphorylation-sensitive manner.