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21 results on '"Cubellis, MARIA VITTORIA"'

7. CDKN1C mutations: two sides of the same coin

Author

Eggermann, Thomas, primary, Binder, Gerhard, additional, Brioude, Frédéric, additional, Maher, Eamonn R., additional, Lapunzina, Pablo, additional, Cubellis, Maria Vittoria, additional, Bergadá, Ignacio, additional, Prawitt, Dirk, additional, and Begemann, Matthias, additional

Published
2014
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9. Ribonucleases and Angiogenins from Fish

Author

Pizzo, Elio, primary, Buonanno, Pasquale, additional, Di Maro, Antimo, additional, Ponticelli, Salvatore, additional, De Falco, Sandro, additional, Quarto, Natalina, additional, Cubellis, Maria Vittoria, additional, and D'Alessio, Giuseppe, additional

Published
2006
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12. Relaxation of Insulin-like Growth Factor 2 Imprinting and Discordant Methylation at KvDMR1 in Two First Cousins Affected by Beckwith-Wiedemann and Klippel-Trenaunay-Weber Syndromes

Author

Sperandeo, Maria Pia, primary, Ungaro, Paola, additional, Vernucci, Maria, additional, Pedone, Paolo V., additional, Cerrato, Flavia, additional, Perone, Lucia, additional, Casola, Stefano, additional, Cubellis, Maria Vittoria, additional, Bruni, Carmelo B., additional, Andria, Generoso, additional, Sebastio, Gianfranco, additional, and Riccio, Andrea, additional

Published
2000
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19. Ribonucleases and Angiogenins from Fish

Author

Giuseppe D'Alessio, Sandro De Falco, Maria Vittoria Cubellis, Elio Pizzo, Antimo Di Maro, Natalina Quarto, Salvatore Ponticelli, Pasquale Buonanno, Pizzo, Eliodoro, Buonanno, P., Di Maro, A., Ponticelli, S., De Falco, S., Quarto, Natalina, Cubellis, MARIA VITTORIA, D'Alessio, Giuseppe, Pizzo, E, Buonanno, P, DI MARO, Antimo, Ponticelli, S, DE FALCO, S, Quarto, N, CUBELLIS M., V, and D'Alessio, G.

Subjects
Models, Molecular, Angiogenin, RNase P, Molecular Sequence Data, Danio, Neovascularization, Physiologic, Bioinformatics, Biochemistry, law.invention, Ribonucleases, law, biology.animal, Animals, Humans, Amino Acid Sequence, Cloning, Molecular, Molecular Biology, Gene, Zebrafish, Phylogeny, Neovascularization, Pathologic, Sequence Homology, Amino Acid, biology, Vertebrate, Ribonuclease, Pancreatic, Cell Biology, biology.organism_classification, Kinetics, Phylogenesis, Recombinant DNA
Abstract

For the first time fish RNases have been isolated and characterized. Their functional and structural properties indicate that they belong to the RNase A superfamily (or tetrapod RNase superfamily), now more appropriately described as the vertebrate RNase superfamily. Our findings suggest why previously repeated efforts to isolate RNases from fish tissues have met with no success; fish RNases have a very low ribonucleolytic activity, and their genes have a low sequence identity with those of mammalian RNases. The investigated RNases are from the bony fish Danio rerio (or zebrafish). Their cDNAs have been cloned and expressed, and the three recombinant proteins have been purified to homogeneity. Their characterization has revealed that they have indeed a very low RNA-degrading activity, when compared with that of RNase A, the superfamily prototype, but comparable with that of mammalian angiogenins; that two of them have angiogenic activity that is inhibited by the cytosolic RNase inhibitor. These data and a phylogenetic analysis indicate that angiogenic fish RNases are the earliest diverging members of the vertebrate superfamily, suggesting that ribonucleases with angiogenic activity were the ancestors of all ribonucleases in the superfamily. They later evolved into both mammalian angiogenins and, through a successful phylogenesis, RNases endowed with digestive features or with diverse bioactivities. © 2006 by The American Society for Biochemistry and Molecular Biology, Inc.

Published
2006
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20. The urokinase receptor: Structure, regulation and inhibitor-mediated internalization

Author

Pura Muñoz-Cánoves, Francesco Blasi, Leena Riittinen, Ugo Cavallaro, Daniela Talarico, E. Soravia, Lisbeth Birk Møller, Paola Limongi, Massimo Resnati, S. Valcamonica, M P Stoppelli, L. Hemandez-Marrero, Nicolai Sidenius, Marco R. Soria, Tambet Teesalu, F. Fazioli, Maria Vittoria Cubellis, Massimo Conese, N. Pedersen, F., Blasi, M., Conese, L. B., Møller, N., Pedersen, U., Cavallaro, Cubellis, MARIA VITTORIA, F., Fazioli, L., Hemandez Marrero, P., Limongi, P., Munoz Canove, M., Resnati, L., Riittinen, N., Sideniu, E., Soravia, M. R., Soria, M. P., Stoppelli, D., Talarico, T., Teesalu, and S., Valcamonica

Subjects
media_common.quotation_subject, Cell, Hematology, Adhesion, Biology, Molecular biology, In vitro, Cell biology, Urokinase receptor, medicine.anatomical_structure, In vivo, medicine, Receptor, Internalization, Human cancer, media_common
Abstract

The receptor for urokinase plasminogen activator (uPAR) acts as an anchorage site for uPA on the cell surface where it stimulates pro-uPA activation, allows the internalization of uPA:inhibitor and other complexes and sends directly or indirectly signals into the cell that may promote migration, adhesion and growth. It is a GPI-anchored, three-domain protein that belongs to the Ly6 family and is present at the focal and cell-to-cell contacts, where it concentrates uPA activity. Its activity appears to be important to regulate the invasiveness of human cancer cells both in vitro and in vivo, and its inhibition is now a target for antimetastatic therapy.

Published
1994
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21. Isolation and sequencing of a new β-galactosidase-encoding archaebacterial gene

Author

Piercarlo Montecucchi, Maria Vittoria Cubellis, Mosè Rossi, Carla Rozzo, Cubellis, MARIA VITTORIA, Carla, Rozzo, Piercarlo, Montecucchi, and Mosè, Rossi

Subjects
DNA, Bacterial, Protein subunit, Molecular Sequence Data, Restriction Mapping, ved/biology.organism_classification_rank.species, Biology, medicine.disease_cause, Homology (biology), Genetics, medicine, Amino Acid Sequence, Cloning, Molecular, Codon, Escherichia coli, Gene, Base Sequence, ved/biology, Sulfolobus solfataricus, Nucleic acid sequence, General Medicine, beta-Galactosidase, Archaea, Molecular biology, Genes, Bacterial, Regulatory sequence, Codon usage bias, Oligonucleotide Probes
Abstract

The gene lacS coding for a β-galactosidase (βGal; EC 3.2.1.23) has been cloned from the thermoacidophilic archaebacterium Sulfolobus solfataricus, strain MT-4. It encodes a polypeptide chain of 489 amino acids (aa) (56764 Da) in good agreement with the value directly measured for the enzyme ( 60 ± 2 kDa per subunit). The aa composition of the enzyme and, in particular, its peculiarly low cysteine content (one Cys per subunit) has been confirmed; at the same time, it has been observed that the very low G + C content of the S. solfataricus genome strongly influences the codoon usage preferences in the lacS sequence. There appears to be no evident similarity between this and the Escherichia coli lacZ sequence, thus suggesting that the two enzymes have analogous function, but are not homologous. By comparison with the published sequences of archaebacterial promoters, terminators and ribosome-binding sites, potential regulatory sites have been identified in the flanking regions of the S. solfataricus lacS gene.

Published
1990
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