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Eleonora Margheritis

Researcher at Istituto Italiano di Tecnologia

Publications -  16
Citations -  248

Eleonora Margheritis is an academic researcher from Istituto Italiano di Tecnologia. The author has contributed to research in topics: Amino acid transporter & Amino acid. The author has an hindex of 8, co-authored 13 publications receiving 192 citations. Previous affiliations of Eleonora Margheritis include University of Insubria.

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Journal ArticleDOI

Two Na+ Sites Control Conformational Change in a Neurotransmitter Transporter Homolog.

TL;DR: Overall, the results demonstrate that occupation of Na2 stabilizes outward-facing conformations presumably through a direct interaction between Na+ and transmembrane helices 1 and 8, whereas Na+ binding at Na1 influences conformational change through a network of intermediary interactions.
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Nanobeam precession-assisted 3D electron diffraction reveals a new polymorph of hen egg-white lysozyme

TL;DR: In this paper, the first new protein structure determined by 3D electron diffraction data is presented: a previously unobserved polymorph of hen egg-white lysozyme, which grows as needle-shaped submicrometric crystals simply by vapor diffusion starting from previously reported crystallization conditions.
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Bile Acid Recognition by NAPE-PLD

TL;DR: It is demonstrated that in the presence of this secondary bile acid, the stiffness of the protein measured by elastic neutron scattering increases, and NAPE-PLD is ∼7 times faster to catalyze the hydrolysis of the more unsaturated substrate N-arachidonyl-phosphatidylethanolamine, compared with N-palmitoyl- phosphatinolamine.
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Characterization of the transport of lysine-containing dipeptides by PepT1 orthologs expressed in Xenopus laevis oocytes

TL;DR: In this article, the authors explored the kinetic properties in various PepT1 orthologs (Dicentrarchus labrax, Oryctolagus cuniculus, Danio rerio) to determine the transport efficiency of different combinations of lysine, methionine, and glycine.
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Functional properties of a newly cloned fish ortholog of the neutral amino acid transporter B0AT1 (SLC6A19).

TL;DR: The functional properties of an ortholog of the B(0)AT1 (SLC6A19) amino acid transporter, cloned from the intestine of the sea bass Dicentrachus labrax, were investigated and the importance of Na(+) as the driver ion in the transport process is confirmed, although Li(+) is also capable to sustain transport, while K(+ is not.