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Dottssa. Francesca Bernassola nata a Roma il 3.7.69 RELAZIONE SU ATTIVITA’ DIDATTICA E SCIENTIFICA RICERCATORE UNIVERSITA’ DEGLI STUDI DI ROMA “TOR VERGATA”

1989 Diploma di Maturità Scientifica a Roma 1994 Laurea in Scienze Biologiche presso l'Università degli Studi di Roma “Tor Vergata” con voto 110/110 con lode. 1998 Dottorato di Ricerca in "Biologia e Fisiopatologia degli Epiteli" presso l'Università degli Studi di Roma “Tor Vergata” . 2001/2006 Presta servizio con il Profilo Professionale di Assistente Biologo, nel Laboratorio di Biochimica IDI-IRCSS presso il Dipartimento di Medicina Sperimentale e Scienze Biochimiche, dell’Università degli Studi di Roma “Tor Vergata”. 2006/2011 Presta servizio a decorrere dal mese di dicembre 2006, con il Profilo Professionale di Ricercatore (confermato nel 2010), nel Dipartimento di Medicina Sperimentale e Scienze Biochimiche della Facolta’ di Medicina e Chirurgia presso l’Universita’ di Roma Tor Vergata.

Attività Didattica

Attività Didattica in Sede

− Insegnamento di Biologia Molecolare (modulo didattico nel Corso integrato di Biochimica e Biologia) del Corso di Laurea magistrale in Odontoiatria e protesi dentaria dell’Università degli Studi di Roma "Tor Vergata"

Attività Scientifica

Nel corso degli anni la Dott.ssa. Francesca Bernassola ha indirizzato il proprio lavoro in vari campi di ricerca, tra i quali si possono individuare i seguenti : 1. Studio del ruolo dell’ubiquitinazione nella regolazione della degradazione proteasoma-dipendente e dell’attività trascrizionale degli omologhi di p53, p73 e p63. 2. Studio del ruolo di p73 e p63 nel cancro e nella risposta alla chemioterapia 3. Studio del ruolo di p63 nella regolazione del “self-renewal” delle cellule staminali della ghiandola mammaria Responsabile di gruppo di ricerca per i Progetti: 2000 Telethon Grant 70.000,00 Euro

2002 Istituto Superiore della Sanita’ 77.000,00 Euro

2007 MIUR 30.000,00 Euro

2009 AIRC 240.000,00 Euro

BREVETTI D’INVENZIONE

1. Melino G, Catani V, Bernassola F, Avigliano L, Finazzi-Agro' A, Cotter T, Hayes. Modulation of cutaneous growth. US 8654/1140. 2000. 2. Melino G, De Laurenzi V, Bernassola F, Tobler A, Grob T, Hayes I. Human Delta-N p73 molecules and uses thereof. US 16599/003. 2001. 

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As we provide molecularly oriented definitions of terms including intrinsic apoptosis, extrinsic apoptosis, mitochondrial permeability transition (MPT)-driven necrosis, necroptosis, ferroptosis, pyroptosis, parthanatos, entotic cell death, NETotic cell death, lysosome-dependent cell death, autophagy-dependent cell death, immunogenic cell death, cellular senescence, and mitotic catastrophe, we discuss the utility of neologisms that refer to highly specialized instances of these processes. 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High throughput screening for inhibitors of the HECT ubiquitin E3 ligase ITCH identifies antidepressant drugs as regulators of autophagy. CELL DEATH & DISEASE, 5(5), e1203 [10.1038/cddis.2014.113].";s:4:"data";s:4:"2014";s:2:"id";s:20:"PUBBLICAZIONE_231854";s:6:"handle";s:11:"2108/113677";s:9:"metadata1";s:19:"Articolo su rivista";s:9:"metadata2";s:270:"Antidepressive Agents; Autophagy; Binding Sites; Cell Line, Tumor; Clomipramine; Drug Synergism; Enzyme Inhibitors; High-Throughput Screening Assays; Humans; Models, Molecular; Protein Structure, Tertiary; Reproducibility of Results; Ubiquitin; Ubiquitin-Protein Ligases";s:9:"metadata3";s:14:"Settore BIO/10";s:9:"metadata4";s:1709:"Inhibition of distinct ubiquitin E3 ligases might represent a powerful therapeutic tool. ITCH is a HECT domain-containing E3 ligase that promotes the ubiquitylation and degradation of several proteins, including p73, p63, c-Jun, JunB, Notch and c-FLIP, thus affecting cell fate. Accordingly, ITCH depletion potentiates the effect of chemotherapeutic drugs, revealing ITCH as a potential pharmacological target in cancer therapy. Using high throughput screening of ITCH auto-ubiquitylation, we identified several putative ITCH inhibitors, one of which is clomipramine--a clinically useful antidepressant drug. Previously, we have shown that clomipramine inhibits autophagy by blocking autophagolysosomal fluxes and thus could potentiate chemotherapy in vitro. Here, we found that clomipramine specifically blocks ITCH auto-ubiquitylation, as well as p73 ubiquitylation. By screening structural homologs of clomipramine, we identified several ITCH inhibitors and putative molecular moieties that are essential for ITCH inhibition. Treating a panel of breast, prostate and bladder cancer cell lines with clomipramine, or its homologs, we found that they reduce cancer cell growth, and synergize with gemcitabine or mitomycin in killing cancer cells by blocking autophagy. 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