DANIEL OSCAR CICERO: CURRICULUM VITAE ET STUDIORUM

D A N IE L O S C A R C IC E R O : C U R R IC U L U M V IT A E E T S T U D IO R U M TITOLI ACCADEMICI
1990
PhD in CHIMICA, Universidad de Buenos Aires, Argentina
1986
Laurea in CHIMICA, Universidad de Buenos Aires, Argentina
ESPERIENZA PROFESSIONALE ED ACCADEMICA
2010 Direttore del Laboratorio di Risonanza Magnetica Nucleare, Fundación Instituto Leloir,
Buenos Aires, Argentina.
2004 Professore Associato, Dipartimento di Scienze e Tecnologie Chimiche, Facoltà di Scienze
MM.FF.NN., Università di Roma “Tor Vergata”, Italy
2001-2004
Ricercatore, Dipartimento di Scienze e Tecnologie Chimiche, Facoltà di Scienze
MM.FF.NN., Università di Roma “Tor Vergata”, Italy
1992-2001
Ricercatore, Merck Research Laboratories-IRBM, Pomezia, Italy
1990-1992
Studente Post-dottorale, Merck Research Laboratories-IRBM, Pomezia, Italy
1986-1989
Assistente docente, Organic Chemistry Department, Facultad de Ciencias Exactas y
Naturales, Universidad de Buenos Aires, Argentina
ESPERIENZA DIDATTICA
Fisica I e II, corso di laurea in Farmacia e Biochimica, Facoltà di Farmacia e Biochimica, Università di
Buenos Aires
Chimica Organica per Scienze Biologiche, corso di laurea in Biologia, Facoltà di Scienze, Università di
Buenos Aires
Chimica Organica II, corso di laurea in Chimica, Facoltà di Scienze, Università di Buenos Aires
Chimica Generale, corso di laurea in Biotecnologie, Università di Roma “Tor Vergata”
Laboratorio di Organica II, corso di laurea in Chimica, Università di Roma “Tor Vergata”
Chimica Organica III, corso di laurea in Chimica, Università di Roma “Tor Vergata”
Spettroscopia NMR delle Molecole Organiche, corso di laurea in Chimica, Università di Roma “Tor
Vergata”
COMPETENZE SCIENTIFICHE
Uso della Risonanza Magnetica Nucleare per studiare la struttura, dinamica e interazione delle
biomolecole, particolarmente proteine e acidi nucleici. Scoperta di nuovi enzimi con potenziali applicazioni
biotecnologiche.
FINANZIAMENTI OTTENUTI
2013 “NMR Screening to select and improve potential therapeutic compounds for the treatment of
Freidreich’s Ataxia, CNCCS – Italy.
2011 “Search, characterization and evaluation of the biotechnological potential of enzymes active
at low temperature from Antarctic organisms” PID-2011-006. Agencia Nacional de Promoción Científica y
Tecnológica, Argentina
2011 “Using Nuclear Magnetic Resonance to explore key mechanisms of hepatitis C virus proteins”
PICT-2009-0099. Agencia Nacional de Promoción Científica y Tecnológica, Argentina
2008 “Fortalecimiento de las Áreas Estratégicas de Estructura de Biomoléculas y Neurociencias”
IP-PRH07-72. Agencia Nacional de Promoción Científica y Tecnológica, Argentina
2007 “Biomolecular Nuclear Magnetic Resonance Unit” PME06-76. Agencia Nacional de Promoción
Científica y Tecnológica, Argentina
2006 “Lotta al cancro da Papilloma virus umano ceppo HPV16. Uno studio di spettroscopia NMR
del meccanismo molecolare di regolazione di E2 della trascrizione virale.” Ministero degli Affari Esteri,
Italy.
2005 “Structural studies of NS3 protease and complexes” IRBM-Merck, Italy.
PUBBLICAZIONI SCIENTIFICHE
E’ autore di 90 pubblicazioni su riviste internazionali, con più di 1000 citazioni. L’indice-h di Daniel Oscar
Cicero è di 18, misurato tramite Scopus. Si consegnano le più importanti.
Structural characterization by NMR of the natively unfolded extracellular domain of b-dystroglycan:
towards the identification of the binding epitope for a-dystroglycan. M. Bozzi, M. Bianchi, F. Sciandra,
M. Paci, B. Giardina, A. Brancaccio and D.O. Cicero, Biochemistry, 42, 13717-13724 (2003).
Conformations of Laulimalide in DMSO-d6. P. Thepchatri, D.O. Cicero, E. Monteagudo, A. K. Ghosh, B.
Cornett, E. R. Weeks and J. P. Snyder, J. Am. Chem. Soc., 127, 12838-12846 (2005).
Molecular basis for phosphorylation dependent PEST mediated protein turnover M. M. García-Alai, M.
Gallo, M. Salame, D. E. Wetzler, A. A. Mcbride, M. Paci, D.O. Cicero, and G. De Prat-Gay. Structure,
14, 309-19 (2006).
NMR dynamic studies suggest that allosteric activation regulates ligand binding in chicken liver bile acid
binding protein. L. Ragona, M. Catalano, M. Luppi, D.O. Cicero, T. Eliseo, J. Foote, F. Fogolari, L.
Zetta, and H. Molinari. J. Biol. Chem. 281, 9697-709 (2006).
Structural basis for the interaction of the myosin light chain Mlc1p with the myosin v Myo2p IQ motifs. M.
Pennestri, S. Melino, G.M. Contessa, E. Caroli Casavola, M. Paci, A. Ragnini-Wilson and D.O. Cicero, J.
Biol. Chem., 282, 667-679 (2007).
Relationship among ligand conformations in solution, in the solid state, and at the Hsp90 binding site:
geldanamycin and radicicol. P. Thepchatri, T. Eliseo, D.O. Cicero, D. Myles and J.P. Snyder, J. Am.
Chem. Soc., 129, 3127-3134 (2007).
The Papillomavirus E2 DNA binding domain. G. de Prat-Gay, K. Gaston and D.O. Cicero, Frontiers in
Biosciences, 13, 6006-6021 (2008).
Binding of a non-covalent inhibitor exploiting the S’ region stabilizes the hepatitis C virus NS3 protease
conformation in the absence of the cofactor. M. Gallo, M. Pennestri, M.J. Bottomley, G. Barbato, T.
Eliseo, M. Paci, F. Narjes, R. De Francesco, V. Summa, U. Koch, R. Bazzo and D.O. Cicero, J. Mol.
Biol.,385, 1142-1155 (2009).
Indirect DNA readout on the protein side: Coupling between histidine protonation, global structure
cooperativity, dynamics and DNA binding of the human papillomavirus type 16 E2C domain. T. Eliseo,
I.E. Sánchez, A.D. Nadra, M. Dellarole, M. Paci, G. de Prat Gay and D.O. Cicero. J. Mol. Biol., 388,
327-344 (2009).
The discodermolide hairpin structure flows from conformationally stable modular motifs. A.S. Jogalekar,
F.H. Kriel, Q. Shi, B. Cornett, D.O. Cicero and J.P. Snyder. J. Med. Chem., 53, 155-165 (2010).
Structural characterization of the Hepatitis C virus NS3 protease from genotype 3a: the basis of the
genotype 1b vs. 3a inhibitor potency shift. M. Gallo, M.J. Bottomely, M. Pennestri, T. Eliseo, M. Paci,
U. Koch, R. Bazzo, V. Summa, A. Carfi, D.O. Cicero, Virology, 405, 424-438 (2010).
Draft genome sequence of Bizionia argentinensis, isolated from Antarctic surface water. E. Lanzarotti, L.
Pellizza, A. Bercovich, M. Foti, S. Coria, S. Vazquez, L. Ruberto, E. Hernández, R. Dias, W. Mac
Cormack, D.O. Cicero, C. Smal, M. Nicolas, A. Ribeiro Vasconcelos, M. Marti and A. Turjanski. J.
Bacteriol., 193, 6797-8 (2011).
1
H,
15
N and
13
C chemical shift assignments of the BA42 protein of the psychrophilic bacteria Bizionia
argentinensis sp. nov. C. Smal, M. Aran, E. Lanzarotti, M. Papouchado, M. Foti, M. A. Marti, S. H.
Coria, S. C. Vazquez, A. Bercovich, W. P. Mac Cormack, A. G. Turjanski, M. Gallo, D. O. Cicero. Biomol.
NMR Assign., 6, 181-183 (2012).
The β-scaffold of the LOV domain of the Brucella light activated histidine kinase is a key element for
signal transduction. J. Rinaldi, M. Gallo, S. Klinke, G. Paris, H.R. Bonomi, R.A. Bogomolni, D.O. Cicero,
F.A. Goldbaum. J. Mol. Biol.,420, 112-127 (2012).
DANIEL OSCAR CICERO: CURRICULUM VITAE ET STUDIORUM
EDUCATION
1990
PhD in CHEMISTRY, Universidad de Buenos Aires, Argentina
1986
B.S. degree in CHEMISTRY, Universidad de Buenos Aires, Argentina
PROFESSIONAL AND ACADEMIC EXPERIENCE
2010
2004
2001-2004
1992-2001
1990-1992
1986-1989
Director of the Nuclear Magnetic Resonance Laboratory, Fundación Instituto Leloir,
Buenos Aires, Argentina.
Associate Professor, Dipartimento di Scienze e Tecnologie Chimiche, Facoltà di
Scienze MM.FF.NN., Università di Roma “Tor Vergata”, Italy
Senior Research Fellow, Dipartimento di Scienze e Tecnologie Chimiche, Facoltà di
Scienze MM.FF.NN., Università di Roma “Tor Vergata”, Italy
Research Fellow, Merck Research Laboratories-IRBM, Pomezia, Italy
Postdoctoral Fellow, Merck Research Laboratories-IRBM, Pomezia, Italy
Teacher Assistant, Organic Chemistry Department, Facultad de Ciencias Exactas y
Naturales, Universidad de Buenos Aires, Argentina
TEACHING EXPERIENCE
Physics I and II. Undergraduate courses, Physics Department, Facultad de Farmacia y Bioquímica,
Universidad de Buenos Aires.
Organic Chemistry for Biological Sciences. Undergraduate course, Organic Chemistry Department, Facultad
de Ciencias Exactas y Naturales, Universidad de Buenos Aires.
Organic Chemistry II. Undergraduate course, Organic Chemistry Department, Facultad de Ciencias Exactas y
Naturales, Universidad de Buenos Aires.
General Chemistry. Undergraduate course, Department of Chemistry, Facoltà di Scienze MM.FF.NN.,
Università di Roma “Tor Vergata”
Organic Chemistry II. Undergraduate course, Department of Chemistry, Facoltà di Scienze MM.FF.NN.,
Università di Roma “Tor Vergata”
Organic Chemistry III. Undergraduate course, Department of Chemistry, Facoltà di Scienze MM.FF.NN.,
Università di Roma “Tor Vergata”
NMR Spectroscopy. Undergraduate course, Department of Chemistry, Facoltà di Scienze MM.FF.NN.,
Università di Roma “Tor Vergata”
TECHNICAL SKILLS AND COMPETENCES
Use of Nuclear Magnetic Resonance to study the structure, dynamics and interaction of biomolecules,
mainly proteins and nucleic acids. Discovery of new enzymes with potential biotechnological application.
PUBLICATIONS
He is the author of 90 papers published in international peer reviewed journals, with more than 1100
citations. The h-index of Daniel Oscar Cicero is 18 as evaluated from Scopus. The most relevant
publications are listed.
Structural characterization by NMR of the natively unfolded extracellular domain of b-dystroglycan:
towards the identification of the binding epitope for a-dystroglycan. M. Bozzi, M. Bianchi, F. Sciandra,
M. Paci, B. Giardina, A. Brancaccio and D.O. Cicero, Biochemistry, 42, 13717-13724 (2003).
Conformations of Laulimalide in DMSO-d6. P. Thepchatri, D.O. Cicero, E. Monteagudo, A. K. Ghosh, B.
Cornett, E. R. Weeks and J. P. Snyder, J. Am. Chem. Soc., 127, 12838-12846 (2005).
Molecular basis for phosphorylation dependent PEST mediated protein turnover M. M. García-Alai, M.
Gallo, M. Salame, D. E. Wetzler, A. A. Mcbride, M. Paci, D.O. Cicero, and G. De Prat-Gay. Structure,
14, 309-19 (2006).
NMR dynamic studies suggest that allosteric activation regulates ligand binding in chicken liver bile acid
binding protein. L. Ragona, M. Catalano, M. Luppi, D.O. Cicero, T. Eliseo, J. Foote, F. Fogolari, L.
Zetta, and H. Molinari. J. Biol. Chem. 281, 9697-709 (2006).
Structural basis for the interaction of the myosin light chain Mlc1p with the myosin v Myo2p IQ motifs. M.
Pennestri, S. Melino, G.M. Contessa, E. Caroli Casavola, M. Paci, A. Ragnini-Wilson and D.O. Cicero, J.
Biol. Chem., 282, 667-679 (2007).
Relationship among ligand conformations in solution, in the solid state, and at the Hsp90 binding site:
geldanamycin and radicicol. P. Thepchatri, T. Eliseo, D.O. Cicero, D. Myles and J.P. Snyder, J. Am.
Chem. Soc., 129, 3127-3134 (2007).
The Papillomavirus E2 DNA binding domain. G. de Prat-Gay, K. Gaston and D.O. Cicero, Frontiers in
Biosciences, 13, 6006-6021 (2008).
Binding of a non-covalent inhibitor exploiting the S’ region stabilizes the hepatitis C virus NS3 protease
conformation in the absence of the cofactor. M. Gallo, M. Pennestri, M.J. Bottomley, G. Barbato, T.
Eliseo, M. Paci, F. Narjes, R. De Francesco, V. Summa, U. Koch, R. Bazzo and D.O. Cicero, J. Mol.
Biol.,385, 1142-1155 (2009).
Indirect DNA readout on the protein side: Coupling between histidine protonation, global structure
cooperativity, dynamics and DNA binding of the human papillomavirus type 16 E2C domain. T. Eliseo,
I.E. Sánchez, A.D. Nadra, M. Dellarole, M. Paci, G. de Prat Gay and D.O. Cicero. J. Mol. Biol., 388,
327-344 (2009).
The discodermolide hairpin structure flows from conformationally stable modular motifs. A.S. Jogalekar,
F.H. Kriel, Q. Shi, B. Cornett, D.O. Cicero and J.P. Snyder. J. Med. Chem., 53, 155-165 (2010).
Structural characterization of the Hepatitis C virus NS3 protease from genotype 3a: the basis of the
genotype 1b vs. 3a inhibitor potency shift. M. Gallo, M.J. Bottomely, M. Pennestri, T. Eliseo, M. Paci,
U. Koch, R. Bazzo, V. Summa, A. Carfi, D.O. Cicero, Virology, 405, 424-438 (2010).
Draft genome sequence of Bizionia argentinensis, isolated from Antarctic surface water. E. Lanzarotti, L.
Pellizza, A. Bercovich, M. Foti, S. Coria, S. Vazquez, L. Ruberto, E. Hernández, R. Dias, W. Mac
Cormack, D.O. Cicero, C. Smal, M. Nicolas, A. Ribeiro Vasconcelos, M. Marti and A. Turjanski. J.
Bacteriol., 193, 6797-8 (2011).
1
H,
15
N and 13C chemical shift assignments of the BA42 protein of the psychrophilic bacteria Bizionia
argentinensis sp. nov. C. Smal, M. Aran, E. Lanzarotti, M. Papouchado, M. Foti, M. A. Marti, S. H.
Coria, S. C. Vazquez, A. Bercovich, W. P. Mac Cormack, A. G. Turjanski, M. Gallo, D. O. Cicero. Biomol.
NMR Assign., 6, 181-183 (2012).
The β-scaffold of the LOV domain of the Brucella light activated histidine kinase is a key element for
signal transduction. J. Rinaldi, M. Gallo, S. Klinke, G. Paris, H.R. Bonomi, R.A. Bogomolni, D.O. Cicero,
F.A. Goldbaum. J. Mol. Biol.,420, 112-127 (2012).