G
Graziantonio Lauria
Researcher at University of Bari
Publications - 4
Citations - 116
Graziantonio Lauria is an academic researcher from University of Bari. The author has contributed to research in topics: Exon & Gene. The author has an hindex of 4, co-authored 4 publications receiving 106 citations.
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Journal ArticleDOI
Molecular and functional analysis of SLC25A20 mutations causing carnitine-acylcarnitine translocase deficiency.
Vito Iacobazzi,Federica Invernizzi,Silvia Baratta,Roser Pons,Wendy K. Chung,Barbara Garavaglia,Carlo Dionisi-Vici,Antonia Ribes,Rossella Parini,Maria Dolores Huertas,Susana Roldan,Graziantonio Lauria,Ferdinando Palmieri,Franco Taroni +13 more
TL;DR: Combined analysis of clinical, biochemical, and molecular data failed to indicate a correlation between the phenotype and the genotype of six CACT‐deficient patients from Italy, Spain, and North America who exhibited significant clinical heterogeneity.
Journal ArticleDOI
Organization and sequence of the human gene for the mitochondrial citrate transport protein.
TL;DR: The sequence of the human citrate transporter gene is determined from overlapping genomic clones generated by polymerase chain reactions by use of primers and probes based on the rat cDNA sequence and on emerging sequences.
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Extension of the mitochondrial transporter super-family: sequences of five members from the nematode worm, Caenorhabditis elegans.
TL;DR: The sequences are presented of cDNAs encoding five related proteins from the nematode worm, Caenorhabditis elegans, that can be recognised as the homologues of the ADP/ATP, phosphate and oxoglutarate/malate carrier proteins that have been found in the inner membranes of mitochondria in other species.
Journal ArticleDOI
Solution structure of the first and second transmembrane segments of the mitochondrial oxoglutarate carrier
Maria Antonietta Castiglione-Morelli,Angela Ostuni,Antonietta Pepe,Graziantonio Lauria,Ferdinando Palmieri,Faustino Bisaccia +5 more
TL;DR: The structures of the first and the second transmembrane segment of the bovine mitochondrial oxoglutarate carrier (OGC) were studied by circular dichroism (CD) and nuclear magnetic resonance (NMR) spectroscopies and showed that at high concentrations of TFE and SDS both peptides assume α-helical structures, whereas in more hydrophilic environments only peptide 78–108 has a helical structure.