N
Nicola Giangregorio
Researcher at National Research Council
Publications - 45
Citations - 1236
Nicola Giangregorio is an academic researcher from National Research Council. The author has contributed to research in topics: Carnitine & Medicine. The author has an hindex of 18, co-authored 39 publications receiving 982 citations. Previous affiliations of Nicola Giangregorio include University of Calabria & University of Bari.
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Journal ArticleDOI
The mitochondrial carnitine/acylcarnitine carrier: Function, structure and physiopathology
Cesare Indiveri,Vito Iacobazzi,Annamaria Tonazzi,Nicola Giangregorio,Vittoria Infantino,Vittoria Infantino,Paolo Convertini,Lara Console,Ferdinando Palmieri +8 more
TL;DR: The functional data indicate that CAC plays the important function of catalyzing transport of acylcarnitines into the mitochondria in exchange for intramitochondrial free carnitine, demonstrating the essential role of the transporter in cell metabolism.
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The mitochondrial carnitine carrier protein: cDNA cloning, primary structure and comparison with other mitochondrial transport proteins.
TL;DR: The hydropathy analysis of the carnitine carrier supports the view that the domains are folded into similar structural motifs, consisting of two transmembrane alpha-helices joined by an extensive extramembranous hydrophilic region.
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Bacterial overexpression, purification, and reconstitution of the carnitine/acylcarnitine carrier from rat liver mitochondria.
TL;DR: These studies represent the first overexpression of the functionally active mitochondrial carnitine/acylcarnitine carrier, thus enabling structure/function analysis of this protein by site-directed mutagenesis.
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Proteoliposomes as Tool for Assaying Membrane Transporter Functions and Interactions with Xenobiotics
TL;DR: Proteoliposomes have recently been used for studying the interaction of some plasma membrane and mitochondrial transporters with toxic compounds, such as mercurials, H2O2 and some drugs.
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Identification by Site-directed Mutagenesis and Chemical Modification of Three Vicinal Cysteine Residues in Rat Mitochondrial Carnitine/Acylcarnitine Transporter *
TL;DR: Results indicate that Cys58, Cys136, and Cys155 become close in the tertiary structure of the CAC during its catalytic cycle, which is interpreted in light of the homology model of CAC based on the available x-rayructure of the ADP/ATP carrier.