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Asociația Ad Astra anunță lansarea proiectului Premiilor Ad Astra 2022 (link aici), care își propune identificarea și popularizarea modelelor de succes, a rezultatelor excepționale ale cercetătorilor români din țară și din afara ei. Regulamentul de participare se poate gasi aici, iar  pagina de inscriere se poate accesa aici.

Asociatia Ad Astra a cercetatorilor romani lanseaza BAZA DE DATE A CERCETATORILOR ROMANI DIN DIASPORA. Scopul acestei baze de date este aceea de a stimula colaborarea dintre cercetatorii romani de peste hotare dar si cu cercetatorii din Romania. Cercetatorii care doresc sa fie nominalizati in aceasta baza de date sunt rugati sa trimita un email la

Stefana Maria Petrescu


Institutul de Biochimie, Bucuresti, .

E-mail: trimite un mesaj.

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Nascut(a) in: 1955

Interese: plierea proteinelor, degradarea proteinelor, vaccin anti-melanom, glicoproteine

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Dr Stefana-M. Petrescu is Director of the Institute of Biochemistry of the Romanian Academy. She graduated from the University of Bucharest, obtained the PhD at the Institute of Biochemistry and has followed postdoctoral studies in the Department of Biochemistry at the University of Oxford. She has been President of the Romanian Society of Biochemistry and Molecular Biology and in the Board of the society for the last 10 years. Dr. Petrescu is a member of the American Society for Biochemistry and Molecular Biology and of American Chemical Society. She is author of 125 scientific papers and Editor of the Romanian Journal of Biochemistry.

Dr Petrescu’s research aims to understand the mechanisms by which glycans regulate the folding and degradation pathways associated with the glycoprotein maturation in mammalian cells. She developed methods for glycoform characterisation based on protein sugar recognition. The interest in sugar interaction with lectins led her to the investigation of glycan mediated recognition of glycoproteins by chaperone systems and the quality control of glycoprotein folding. Tyrosinase related proteins were chosen as model systems for glycoprotein folding due to the extreme complexity of the process along the maturation pathway. Since tyrosinase regulates melanogenesis in melanocytes and melanoma cells, the cell biology of these two cell types is the major focus of her research group. Dr Petrescu’s research has been funded by the Wellcome Trust and the University of Oxford for the past 14 years.

Dr. Petrescu has been granted the Award Emil Racovita of the Romanian Academy for the work on tyrosinase folding in 2002. She was elected member of MSR Corpus Christi College Oxford in recognition of her scientific merits. In 2002 was elected in the in the working group Women in science of the Federation of the European Biochemical Societies.

Publicații selectate:

* PETRESCU A.J., BUTTERS T.D., PETRESCU S.M., PLATT F.M., DWEK R.A., WORMALD M.R., The solution NMR structure of Glc3Man9 unit in Glc3Man7GlcNAc2, Embo Journal, 16, 1997.

* ZAPUN A., PETRESCU S.M., RUDD P.M., DWEK R.A., THOMAS D.Y., BERGERON J.J.M., Conformation - independent binding of monoglucosylated ribonuclease B to calnexin, Cell, 88, 1997.

* BRANZA-NICHITA N, NEGROIU G, PETRESCU A-J, DWEK R.A., WORMALD, M, PLATT F.M., PETRESCU S.M, Tyrosinase folding and copper loading in vivo: a crucial role for calnexin and alpha-glucosidase II, Biochem.Biophys.Res.Communications, 261, 1999.

* PETRESCU SM., BRANZA-NICHITA N., NEGROIU G., PETRESCU AJ., DWEK RA., Tyrosinase and glycoprotein folding: roles of chaperones that recognize glycans, Biochemistry, 39, 2000.

* Petrescu Stefana, Glycosylation and glycoprotein folding, The Wellcome Trust Review, 2000.

* Negroiu G, Dwek RA, PETRESCU SM, The inhibition of early N-glycan processing targets TRP-2 to degradation in B16 melanoma cell, Journal Biological Chemistry, 278, 2003.

* PETRESCU S.M., Popescu C.I., Petrescu A.J., Dwek R.A., The Glycosylation of Tyrosinase in melanoma cells and the effect on antigen presentation, Kluwer Press, J.S.Axford, Glycobiology and Medicine, chapter 17, 2004.

* Popescu CI, Paduraru C, Dwek RA, PETRESCU SM, Soluble tyrosinase is an ER- associated degradation substrate retained in the ER by calreticulin and BIP and not calnexin, Journal Biological Chemistry, 280(14), 2005.

* Popescu CI, Mares A, Zdrentu L, Zitzmann N, Dwek RA, Petrescu SM., Productive folding of tyrosinase ectodomain is controlled by the transmembrane anchor, Journal Biological Chemistry, 281, 2006.