F
Fabio Beltram
Researcher at Nest Labs
Publications - 56
Citations - 9063
Fabio Beltram is an academic researcher from Nest Labs. The author has contributed to research in topics: Superlattice & Chemistry. The author has an hindex of 28, co-authored 45 publications receiving 8660 citations. Previous affiliations of Fabio Beltram include Bell Labs & Istituto Italiano di Tecnologia.
Papers
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Journal ArticleDOI
Terahertz semiconductor-heterostructure laser
R. Kohler,Alessandro Tredicucci,Fabio Beltram,Harvey E. Beere,Edmund H. Linfield,Giles Davies,David A. Ritchie,Rita Claudia Iotti,Fausto Rossi +8 more
TL;DR: A monolithic terahertz injection laser that is based on interminiband transitions in the conduction band of a semiconductor (GaAs/AlGaAs) heterostructure is reported, which is very promising for extending the present laser concept to continuous-wave and high-temperature operation, which would lead to implementation in practical photonic systems.
Terahertz semiconductor heterostructure laser
R. Kohler,Alessandro Tredicucci,Fabio Beltram,Harvey E. Beere,Edmund H. Linfield,Giles Davies,David A. Ritchie,Rita Claudia Iotti,Fausto Rossi +8 more
TL;DR: In this article, a monolithic terahertz injection laser that is based on interminiband transitions in the conduction band of a semiconductor (GaAs/AlGaAs) heterostructure is presented.
Journal ArticleDOI
Empirical spds^* tight-binding calculation for cubic semiconductors : general method and material parameters
TL;DR: In this paper, an empirical tight-binding method for tetrahedrally coordinated cubic materials is presented and applied to group-IV and III-V semiconductors, and the method extends existing calculations by the inclusion of all five $d$ orbitals per atom in the basis set.
Journal ArticleDOI
Cell membrane lipid rafts mediate caveolar endocytosis of HIV-1 Tat fusion proteins.
Antonio Fittipaldi,Aldo Ferrari,Monica Zoppè,Caterina Arcangeli,Vittorio Pellegrini,Fabio Beltram,Mauro Giacca,Mauro Giacca +7 more
TL;DR: It is shown that Tat fusion proteins are internalized by the cells through a temperature-dependent endocytic pathway that originates from cell membrane lipid rafts and follows caveolar endocytosis.
Journal ArticleDOI
Caveolae-mediated internalization of extracellular HIV-1 tat fusion proteins visualized in real time.
Aldo Ferrari,Vittorio Pellegrini,Caterina Arcangeli,Antonio Fittipaldi,Mauro Giacca,Mauro Giacca,Fabio Beltram +6 more
TL;DR: It is demonstrated that the internalization process of full-length Tat and of heterologous proteins fused to the transduction domain of Tat exploits a caveolar-mediated pathway and is inhibited at 4 degrees C.