Curriculum Vitae et Studiorum Tiziana Bellini

Born: Barbona (Padova) October 11, 1954.
Citizenship: Italian
Home Address: Ferrara, via Lyda Borelli 6
Work Address: Department of Biomedical and Specialty Surgical Sciences Section: Medical Biochemistry,Molecular Biology and Genetics School of Medicine University of Ferrara,,
address :via L.Borsari 46, I-44100 Ferrara

Languages known: Italian, English, French
1978, MS, Degree in Biological Sciences best marks and honors, University of Ferrara
Previous positions
1978-1982 Doctoral Fellow Department of Biochemistry and Molecular Biology University of Ferrara
1982-1990 Post Doctoral fellow Department of Biochemistry and Molecolar Biology University of Ferrara
1990,-2005 Assistant Professor of Biochemistry Department of Biochemistry and Molecolar Biology University of Ferrara

Present position
Associate professor in Biochemistry
Department of Biochemistry and Molecular Biology University of Ferrara

Membership of Scientific Societies
Ordine Nazionale dei Biologi dal 1981
Società Italiana di Biochimica dal 1979
Associazione Italiana di Calorimetria e Analisi Termica dal 2000

1980-present: Course of Biochemistry of Central Nervous System in Postgraduate School of Neurology, and in Postgraduate School of Psichiatry, University of Ferrara, School of Medicine
1995-present: Course of Medical Chemistry and Biochemistry, Postgraduate School of Nurse,Obstetrics, University of Ferrara, School of Medicine 1997-Present:
Course of Chemistry and propedeutical Biochemistry, School of Medicine, University of Ferrara
Relator of thesis and Tutor phd
Author of 138 pubblications. (on peer-review Journal with Impact Factor)

-Vice coordinator of the degree course in Medicine and Surgery
-Chairman of the Joint Committee of the School of Medicine
-Educational Dean of Degree Course in Medicine and Surgery
-Deputy Rector of Teaching BioMed Area

Research areas

Enzyme structure and function;
The research on the catalytic mechanism of 6-phosphogluconate dehydrogenase was used as a model for multistep enzyme reaction.
This enzyme was investigated with different techniques: fluorescence and UV spectroscopy, kinetics,chemical modifications (in the early years) and site-directed mutagenesis, affinity labelling, substrate analogues. (Biochem.J. 183, 297-302, (1979))( J.Biol.Chem. 256, 10778-10780, (1981)).
These studies lead to the identification of a half-site reactivity of the ternary complex, and to a model of catalytic mechanism with alternating sites ( J.Biol.Chem. 256, 451-455, (1981)).The knowledge of this enzyme has been applied in recent years to study specific inhibitors suitable as drug against the parasite Trypanosoma brucei (Biochem.J. 227, 305-310 (1985)).

Myelin Basic Protein; Purification and interaction with cellular membranes
Myelin Basic Protein, one of the major membrane protein component of the central nervous system, was purified from very limited amounts of human white matter obtained during surgery (Neuroscience Letters,18, S 333, (1984))( J.Neurochem. 46, 1644-1646, (1986)). The MBP was used to probe the molecular mechanism of human lymphocytes activation (Biochem.Biophys.Res.Comm. 141, 524-527 (1986))
(Rivista di Neurologia, 57, 125-126, (1987))( Bioscience Rep. 10, 55-59 (1990)).

- Studies of functional domains of Sendai virus proteins
The study of the hemagglutinin-neuraminidase from Sendai virus has revealed an inhibition of the neuraminidase activity by the fusogenic protein (Biochem. Biophys. Res. Comm 201, 988-993 (1994)) and the activation of fusogenic protein by the binding to the neuraminidase of a substrate analogue (Biochem. Biophys. Res. Comm 208, 36-41 (1995)). Studies of the neuraminidase activity evidenced an interaction hemagglutinin with the hydrophobic heptad repeat of the fusogenic protein.We show that the binding of the F protein to HN, induced by the binding to HN of a substrate or a substrate analogue, causes
A conformational change which activates the F protein Other results suggest that the paramyxovirus neuraminidases have the folding properties of a two-domain protein.

Role of matrix metalloproteases in physiological and pathological conditions;
Proteomic studies of gelatinases and their activity in biological (Ital. J.Biochem.54 147 200 We employed a sensitive activity assay system to measure active matrix metalloproteinase-9 levels in serum and cerebrospinal fluid (CSF). (Mult. Scler. 12: 1-2 (2006)).Our study indicate that CSF and serum levels of active MMP-9 may represent a potential surrogate biomarker for monitoring MS disease activity (Mult Scler. Jun;12(3):294-301 (2006)). The MMP-9 assay was used to assess the different fluid replacement therapy in colon surgery (Anesthesiology. Jan;106(1):85-91 (2007)).

Anderson-Fabry disease
Biochemical studies to the people with cerebrovascular desease in Ferrara