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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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Specificity of the binding of synapsin I to Src homology 3 domains.

TL;DR: The ability to bind multiple SH3 domains further implicates the synapsins in signal transduction and protein-protein interactions at the nerve terminal level.
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Tyrosine phosphorylation of synapsin I by Src regulates synaptic-vesicle trafficking.

TL;DR: It is demonstrated that Src-mediated tyrosine phosphorylation ofsynapsin I increases its binding to SVs and actin, and increases the formation of synapsin dimers, which are both potentially involved in SV clustering.
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Differential cell adhesion on mesoporous silicon substrates.

TL;DR: Higher rates of proliferation are observed for the two neuronal cell types, the mouse neuroblastoma cells (N2A) and the immortalized human cortical neuronal cells (HCN1A), speculated that the higher adhesion on MeP1 could be attributed to a preferential matching of the substrate topography with the recently observed multiscale molecular architecture of focal adhesions.
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Three-dimensional in vivo scanning microscopy with inertia-free focus control

TL;DR: A laser scanning two-photon microscope with remote and motionless control of the focus position bypasses the limitations of microscopes based on moving objectives, enabling high-resolution inertia-free 3D imaging.
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Kidins220/ARMS mediates the integration of the neurotrophin and VEGF pathways in the vascular and nervous systems

TL;DR: This work has identified Kidins220 as a main player in the modulation of neurotrophin and vascular endothelial growth factor signaling in vivo, and a primary determinant for neuronal and cardiovascular development, and demonstrates that Kidins 220 constitutively interacts with VEGFR2.