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16 results on '"Varrone, Francesca"'

4. Supplementary Data from Collagen Prolyl Hydroxylation–Dependent Metabolic Perturbation Governs Epigenetic Remodeling and Mesenchymal Transition in Pluripotent and Cancer Cells

Author

D'Aniello, Cristina, primary, Cermola, Federica, primary, Palamidessi, Andrea, primary, Wanderlingh, Luca G., primary, Gagliardi, Miriam, primary, Migliaccio, Agnese, primary, Varrone, Francesca, primary, Casalino, Laura, primary, Matarazzo, Maria R., primary, De Cesare, Dario, primary, Scita, Giorgio, primary, Patriarca, Eduardo J., primary, and Minchiotti, Gabriella, primary

Published
2023
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5. Data from Collagen Prolyl Hydroxylation–Dependent Metabolic Perturbation Governs Epigenetic Remodeling and Mesenchymal Transition in Pluripotent and Cancer Cells

Author

D'Aniello, Cristina, primary, Cermola, Federica, primary, Palamidessi, Andrea, primary, Wanderlingh, Luca G., primary, Gagliardi, Miriam, primary, Migliaccio, Agnese, primary, Varrone, Francesca, primary, Casalino, Laura, primary, Matarazzo, Maria R., primary, De Cesare, Dario, primary, Scita, Giorgio, primary, Patriarca, Eduardo J., primary, and Minchiotti, Gabriella, primary

Published
2023
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8. Collagen Prolyl Hydroxylation–Dependent Metabolic Perturbation Governs Epigenetic Remodeling and Mesenchymal Transition in Pluripotent and Cancer Cells

Author

D'Aniello, Cristina, primary, Cermola, Federica, additional, Palamidessi, Andrea, additional, Wanderlingh, Luca G., additional, Gagliardi, Miriam, additional, Migliaccio, Agnese, additional, Varrone, Francesca, additional, Casalino, Laura, additional, Matarazzo, Maria R., additional, De Cesare, Dario, additional, Scita, Giorgio, additional, Patriarca, Eduardo J., additional, and Minchiotti, Gabriella, additional

Published
2019
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9. Inhibition of Tat activity by the HEXIM1 protein

Author

Majello Barbara, Michels Annemieke A, Napolitano Giuliana, Varrone Francesca, Fraldi Alessandro, Bensaude Olivier, and Lania Luigi

Subjects
Immunologic diseases. Allergy, RC581-607
Abstract

Abstract Background The positive transcription elongation factor b (P-TEFb) composed by CDK9/CyclinT1 subunits is a dedicated co-factor of HIV transcriptional transactivator Tat protein. Transcription driven by the long terminal repeat (LTR) of HIV involves formation of a quaternary complex between P-TEFb, Tat and the TAR element. This recruitment is necessary to enhance the processivity of RNA Pol II from the HIV-1 5' LTR promoter. The activity of P-TEFb is regulated in vivo and in vitro by the HEXIM1/7SK snRNA ribonucleic-protein complex. Results Here we report that Tat transactivation is effectively inhibited by co-expression of HEXIM1 or its paralog HEXIM2. HEXIM1 expression specifically represses transcription mediated by the direct activation of P-TEFb through artificial recruitment of GAL4-CycT1. Using appropriate HEXIM1 mutants we determined that effective Tat-inhibition entails the 7SK snRNA basic recognition motif as well as the C-terminus region required for interaction with cyclin T1. Enhanced expression of HEXIM1 protein modestly affects P-TEFb activity, suggesting that HEXIM1-mediated repression of Tat activity is not due to a global inhibition of cellular transcription. Conclusion These results point to a pivotal role of P-TEFb for Tat's optimal transcription activity and suggest that cellular proteins that regulate P-TEFb activity might exert profound effects on Tat function in vivo.

Published
2005
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11. The Circulating Level of FABP3 Is an Indirect Biomarker of MicroRNA-1

Author

Varrone, Francesca, primary, Gargano, Barbara, additional, Carullo, Pierluigi, additional, Di Silvestre, Dario, additional, De Palma, Antonella, additional, Grasso, Ludovica, additional, Di Somma, Carolina, additional, Mauri, Pierluigi, additional, Benazzi, Louise, additional, Franzone, Anna, additional, Jotti, Gloria Saccani, additional, Bang, Marie-Louise, additional, Esposito, Giovanni, additional, Colao, Annamaria, additional, Condorelli, Gianluigi, additional, and Catalucci, Daniele, additional

Published
2013
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12. Reciprocal Regulation of MicroRNA-1 and Insulin-Like Growth Factor-1 Signal Transduction Cascade in Cardiac and Skeletal Muscle in Physiological and Pathological Conditions

Author

Elia, Leonardo, primary, Contu, Riccardo, additional, Quintavalle, Manuela, additional, Varrone, Francesca, additional, Chimenti, Cristina, additional, Russo, Matteo Antonio, additional, Cimino, Vincenzo, additional, De Marinis, Laura, additional, Frustaci, Andrea, additional, Catalucci, Daniele, additional, and Condorelli, Gianluigi, additional

Published
2009
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16. p14ARF directly interacts with Myc through the Myc BoxII domain

Author

Luigi Lania, Stefano Amente, Barbara Majello, Barbara Gargano, Luca Ruggiero, Francesca Varrone, David Dominguez-Sola, Amente, Stefano, Gargano, Barbara, Varrone, Francesca, Ruggiero, L, DOMINGUEZ SOLA, D, Lania, Luigi, and Majello, Barbara

Subjects
Cancer Research, Transcription, Genetic, Tumor suppressor gene, Nucleolus, Down-Regulation, Repressor, Proto-Oncogene Mas, Cell Line, Proto-Oncogene Proteins c-myc, p14arf, Transcription (biology), Protein Interaction Mapping, Tumor Suppressor Protein p14ARF, Humans, Transcription factor, Pharmacology, Nucleoplasm, Oncogene, Basic Helix-Loop-Helix Leucine Zipper Transcription Factors, Chemistry, Recombinant Proteins, Protein Structure, Tertiary, Oncology, Cancer research, Molecular Medicine, Dimerization, Cell Nucleolus, Gene Deletion, Protein Binding
Abstract

Myc is a well known proto-oncogene encoding for a transcription factor whose activity is tightly regulated in the cellular context. Myc was the first oncogene recognized to activate the ARF tumor suppressor gene which suppresses cell proliferation partly through stabilization of the p53 tumor suppressor protein but which also has p53-independent growth-suppressive functions. Recent studies have indicated that mouse p19ARF negatively regulates Myc's transcriptional activity. We here show that the human p14ARF directly associates with Myc and relocates Myc from the nucleoplasm to the nucleolus. We found that p14ARF interacts with the Myc-Max complex and the binding of p14ARF does not interfere with Myc-Max interaction in vitro. Protein interaction assays define the Myc BoxII as a critical domain required for interaction with p14ARF. Moreover, we identify 30 amino acids encompassing Myc BoxII domain required for p14ARF interaction and colocalization in vivo. Finally, we show that p14ARF down regulates Myc activated transcription and that this activity cannot be addressed to an intrinsic p14ARF repressor domain.

Published
2006
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