Search

Your search keyword '"Pirone, Luciano"' showing total 9 results
Start Over Author "Pirone, Luciano" Journal scientific reports
9 results on '"Pirone, Luciano"'

5. Structural Insight of the Full-Length Ros Protein: A Prototype of the Prokaryotic Zinc-Finger Family.

Author

D'Abrosca, Gianluca, Paladino, Antonella, Baglivo, Ilaria, Russo, Luigi, Sassano, Marica, Grazioso, Rinaldo, Iacovino, Rosa, Pirone, Luciano, Pedone, Emilia Maria, Pedone, Paolo Vincenzo, Isernia, Carla, Fattorusso, Roberto, and Malgieri, Gaetano

Subjects
ZINC-finger proteins, BACTERIAL proteins, AGROBACTERIUM tumefaciens, PROTEIN structure, GLOBULAR proteins
Abstract

Ros/MucR is a widespread family of bacterial zinc-finger (ZF) containing proteins that integrate multiple functions such as virulence, symbiosis and/or cell cycle transcription. NMR solution structure of Ros DNA-binding domain (region 56–142, i.e. Ros87) has been solved by our group and shows that the prokaryotic ZF domain shows interesting structural and functional features that differentiate it from its eukaryotic counterpart as it folds in a significantly larger zinc-binding globular domain. We have recently proposed a novel functional model for this family of proteins suggesting that they may act as H-NS-'like' gene silencers. Indeed, the N-terminal region of this family of proteins appears to be responsible for the formation of functional oligomers. No structural characterization of the Ros N-terminal domain (region 1–55) is available to date, mainly because of serious solubility problems of the full-length protein. Here we report the first structural characterization of the N-terminal domain of the prokaryotic ZF family examining by means of MD and NMR the structural preferences of the full-length Ros protein from Agrobacterium tumefaciens. [ABSTRACT FROM AUTHOR]

Published
2020
Full Text
View/download PDF

7. Ml proteins from Mesorhizobium loti and MucR from Brucella abortus: an AT-rich core DNA-target site and oligomerization ability

Author

Baglivo, Ilaria, primary, Pirone, Luciano, additional, Pedone, Emilia Maria, additional, Pitzer, Joshua Edison, additional, Muscariello, Lidia, additional, Marino, Maria Michela, additional, Malgieri, Gaetano, additional, Freschi, Andrea, additional, Chambery, Angela, additional, Roop II, Roy-Martin, additional, and Pedone, Paolo Vincenzo, additional

Published
2017
Full Text
View/download PDF

8. Neuroblastoma tumorigenesis is regulated through the Nm23-H1/h-Prune C-terminal interaction

Author

Carotenuto, Marianeve, primary, Pedone, Emilia, additional, Diana, Donatella, additional, de Antonellis, Pasqualino, additional, Džeroski, Sašo, additional, Marino, Natascia, additional, Navas, Luigi, additional, Di Dato, Valeria, additional, Scoppettuolo, Maria Nunzia, additional, Cimmino, Flora, additional, Correale, Stefania, additional, Pirone, Luciano, additional, Monti, Simona Maria, additional, Bruder, Elisabeth, additional, Ženko, Bernard, additional, Slavkov, Ivica, additional, Pastorino, Fabio, additional, Ponzoni, Mirco, additional, Schulte, Johannes H., additional, Schramm, Alexander, additional, Eggert, Angelika, additional, Westermann, Frank, additional, Arrigoni, Gianluigi, additional, Accordi, Benedetta, additional, Basso, Giuseppe, additional, Saviano, Michele, additional, Fattorusso, Roberto, additional, and Zollo, Massimo, additional

Published
2013
Full Text
View/download PDF

9. The Sam-Sam interaction between Ship2 and the EphA2 receptor: design and analysis of peptide inhibitors

Author

Luciano Pirone, Emilia Pedone, Rosanna Palumbo, Roberta Iannitti, Concetta Di Natale, Daniela Marasco, Marilisa Leone, Flavia Anna Mercurio, Mercurio, Flavia Anna, Di Natale, Concetta, Pirone, Luciano, Iannitti, Roberta, Marasco, Daniela, Pedone, Emilia Maria, Palumbo, Rosanna, and Leone, Marilisa

Subjects
Male, Models, Molecular, 0301 basic medicine, Saccharomyces cerevisiae Proteins, lcsh:Medicine, Antineoplastic Agents, Peptide, Plasma protein binding, Article, Necrosis, 03 medical and health sciences, Cell Line, Tumor, Escherichia coli, Humans, Binding site, Receptor, lcsh:Science, Nuclear Magnetic Resonance, Biomolecular, Ship2 EphA2 receptor KRI peptide, chemistry.chemical_classification, Binding Sites, Multidisciplinary, 030102 biochemistry & molecular biology, Drug discovery, Receptor, EphA2, lcsh:R, Membrane Proteins, Prostatic Neoplasms, Fibroblasts, In vitro, Sterile Alpha Motif, 030104 developmental biology, chemistry, Biochemistry, Drug Design, Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases, Cancer cell, lcsh:Q, Peptides, Sterile alpha motif, Preliminary Data, Protein Binding
Abstract

The lipid phosphatase Ship2 represents a drug discovery target for the treatment of different diseases, including cancer. Its C-terminal sterile alpha motif domain (Ship2-Sam) associates with the Sam domain from the EphA2 receptor (EphA2-Sam). This interaction is expected to mainly induce pro-oncogenic effects in cells therefore, inhibition of the Ship2-Sam/EphA2-Sam complex may represent an innovative route to discover anti-cancer therapeutics. In the present work, we designed and analyzed several peptide sequences encompassing the interaction interface of EphA2-Sam for Ship2-Sam. Peptide conformational analyses and interaction assays with Ship2-Sam conducted through diverse techniques (CD, NMR, SPR and MST), identified a positively charged penta-amino acid native motif in EphA2-Sam, that once repeated three times in tandem, binds Ship2-Sam. NMR experiments show that the peptide targets the negatively charged binding site of Ship2-Sam for EphA2-Sam. Preliminary in vitro cell-based assays indicate that -at 50 µM concentration- it induces necrosis of PC-3 prostate cancer cells with more cytotoxic effect on cancer cells than on normal dermal fibroblasts. This work represents a pioneering study that opens further opportunities for the development of inhibitors of the Ship2-Sam/EphA2-Sam complex for therapeutic applications.

Published
2017
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results