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SBSC Dipartimento di Scienze Biomediche Sperimentali e Cliniche

CV del Prof. Massimo Stefani


Massimo Stefani was born in Pisa, on 31/7/1950 and graduated in Biological Sciences at the University of Firenze. Since 1/8/1981 he was researcher at the Department of Biochemistry of the University of Firenze. In 1990 he won a public competition for Full Professor of Biochemistry at the University of Siena. Since 1993 he is full professor of Biochemistry at the University of Firenze (Department of Biochemical Sciences, since 2013 Department of Biomedical Experimental and Clinical Sciences).

His scientific interests have formerly been focused on the study of the structure-function relationships of phosphomonohydrolases, notably acylphosphatases and low Mr phosphotyrosine protein phosphatases. He has formerly organized the laboratory of chemical synthesis of peptides at the Department of Biochemical Sciences of the University of Firenze. His efforts have been principally dedicated to the study of molecular biology issues such as protein folding, misfolding and aggregation of model proteins such as acylphosphatase, HypF-N, beta2 microglobulin Abeta peptides, amylin and prion proteins and to the investigation of the molecular mechanisms underlying amyloid aggregation and the cell biology of aggregate cytotoxicity on living systems. More recently, he focussed his research on the molecular and cellular basis of the protective effects of plant polyphenols, particularly oleuropein aglycone against amyloid diseases. The results of his researches have been reported in over 180 scientific papers published in outstanding international journals and widely cited (around 10000 total citations, over 6000 citations of the 10 most cited articles, ISI data), for an HI value of 46 (ISI). He has deposited three patents (Nr. MI2008A000514 of 27.03.08, PCT Nr. EP2009/053596 of 23/02/2011 and Nr. FI2011A000034 of 02/03/2011) for the use of oleuropein aglycone and its derivatives in the treatment of type II diabetes mellitus and Alzheimer’s disease.

He has collaborated, and presently collaborates with many foreign and Italian researchers, notably Prof. C.M. Dobson, University of Cambridge, Dr. R. Melki, CNRS, Paris, Prof.  Ayouni E.A.  Centre de Biotecnologie de Borj-Cédria, Hammam-Lif, Tunisie, Prof. P. Nordlund, University of Stockholm, Prof. V. Bellotti, University of Pavia, Prof. P. Pucci, University of Napoli, Prof. M. Bolognesi, University of Milano, Prof. A. Gliozzi/A Relini, University of Genova, Prof. P. Viglino, University of Udine, Prof. P. Polverino de Laureto, University of Padoa, Prof. A. Nataliello, University of Milan. He has been, and presently is, responsible of research projects granted by CNR and MIUR (PRIN and FIIRB) as well as partner in projects CNR, UE and MURST PRIN. He has been Director of the Italian Research Center on the Molecular Basis of Neurodegeneration (CIMN) and member of the Centro Interuniversitario di Medicina Molecolare e Biofisica Applicata (CIMMBA) and of the  Centro per lo Studio a Livello Molecolare e Clinico di Malattie Croniche, Infiammatorie, Degenerative Neoplastiche per Sviluppo Nuove Terapie (DENOthe) of the University of Florence. He is leader of a group associated to the Italian CIB and the Italian INBB.

He has been  reviewer of domestic projects (Italian MIUR 2004), member of the referee board of the Italian MIUR (2006) and many foreign projects for granting institutions. He has been president of the ASN Commission  (05/E1) of the Italian MIUR for the year 2014/15. He has been referee of many qualified scientific journal and project evaluator for several international scientific institutions. He has been Executive Editor of the Italian Journal of Biochemistry and member of the Editorial Board of International Journal of Biological Chemistry, Current Proteomics, The Open Biology Journal, Genes & Diseases, International Journal of Medicine and Clinical Research, Archive of Biochemistry and World Journal of Biological Chemistry (WJBC); Editor of the Special Issue on Protein Folding, Misfolding and Aggregation of the Open Biology Journal (2009). He is, or has been, member of the Società Italiana di Biochimica e Biologia Molecolare, the Protein Society, and the ASBMB.

He organized the international meeting HFSP/EU “Protein Phosphatases” and was Co-organizer and member of the Scientific Committee of the V European Symposium of the Protein Society, co-organizer of the EMBO Workshop and Advanced FEBS Course on “Structure of Amyloid Aggregates, Mechanisms of Formation and Dysfunction”, member of the organizing committee of the 53° Congress of the Società Italiana di Biochimica e Biologia Molecolare, of the scientific committee of the Meeting Proteine 2010 and 2012 of the Società Italiana di Biochimica e Biologia Molecolare and of the XII International Symposium on Amyloidoses (Rome, 2010). He has participated as invited speaker or chair to many national and international meetings, including:

  • XVI meeting of the Protein workgroup, SIBBM, L’Aquila, 6-8 Giugno 2002
  • Nature-Avensis Horizon Symposium “protein folding and disease”, Carzago di Calvagese della Riviera, 3-5 Ottobre 2002
  • I MEETING ON THE MOLECULAR MECHANISMS of neurodegeneration, Milano 2-4 Maggio 2003
  • INF MEETING, “Convegno Nazionale per la Ricerca Multidisciplinare in Fisica della Materia” Genova, 8-10 Giugno 2004
  • XVII Congresso Nazionale della Società Italiana di Biofisica pura e applicata, Pisa, 23-25 Settembre 2004
  • XXXV Congresso Nazionale della società italiana di neurologia, Genova 25-29 Settembre 2004
  • 6° Convegno FISV Riva del Garda, 30 Settembre 3 Ottobre 2004
  • NATIONAL CONGRESS PROTEINE 2006, Novara June 1-3 2006.
  • 1st HAMLET Meeting, Lund, August 31st-September 1st 2006.
  • INBB, VII Convegno Nazionale su Scienze della vita, Rome, October 19-20 2006.
  • III Meeting on the Molecular Mechanisms of Neurodegeneration, Milan, May 19-21 2007.
  • IV Meeting on the Molecular Mechanisms of Neurodegeneration, Milan, May 8-10 2009.
  • II HAMLET Symposiun, Lund 11-14 Maggio 2009.
  • National Congress of the Italian Society for Neurosciences, Milan, October 2-5, 2009
  • Workshop on Molecular Basis of Amyloid Diseases, Helsinki, November 19-20 2009.
  • National Congress PROTEINE 2010, Parma, 8-10 April 2010.
  • XII International Symposium on Amyloidosis, Rome, April 18-20 2010.
  • Department of Molecular Biochemistry and Biophysics Seminars, Umea May 18 2010.
  • Jacques Monod Conference, Roscoff, June 5-9 2010.
  • Italian Congress Proteine 2012, Chieti 25-26 Settembre 2012.
  • XXI Congresso Nazionale SIBPA, Ferrara, 17-20 Settembre 2012.
  • International Conference on new Therapies for Dementia, Firenze, 27 Settembre 2014
  • Ettore Majorana Fundation, “Nutraceuticals”, Erice, 26-30 Settembre 2015
  • Festival dell’innovazione in sanità pubblica. Pisa, 25-28 Ottobre 2017


ORCID Identifier:                                


25 Most relevant publications

  • The crystal structure of a low molecular weight phosphotyrosine protein phosphatase (X.D. Su, N. Taddei, M. Stefani, G. Ramponi, and P. Nordlund) Nature (1994) 6490: 575-578.
  • Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding (F. Chiti, N. Taddei, P.M. White, M. Bucciantini, F. Magherini, M. Stefani & C.M. Dobson) Nat. Struct. Biol. (1999) 6:1005-1009.
  • Designing conditions for in vitro formation of amyloid protofilaments and fibrils (F. Chiti, P. Webster, N. Taddei, A. Clark, M. Stefani, G. Ramponi & C.M. Dobson) Proc. Natl. Acad. Sci. USA (1999) 96:3590-94.
  • Studies on the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases (F. Chiti, M. Calamai, N. Taddei, M. Stefani, G. Ramponi & C.M. Dobson) Proc. Natl. Acad Sci. USA (2002) 4:16419-26.
  • Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases (M. Bucciantini, E. Giannoni, F. Chiti, F. Baroni, L. Formigli, J. Zurdo, N. Taddei, G. Ramponi, C.M. Dobson & M. Stefani) Nature (2002) 416: 507-511.
  • Kinetic partitioning of protein folding and aggregation (F. Chiti, N. Taddei, F. Baroni, C. Capanni, M. Stefani, G. Ramponi & C.M. Dobson) Nat. Struct. Biol. (2002) 9:137-143.
  • Rationalization of the effects of mutations on peptide and protein aggregation rates (F. Chiti, M. Stefani, N. Taddei, G. Ramponi & C.M. Dobson) Nature (2003) 424: 805-808.
  • Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution (M. Stefani & C.M. Dobson) J. Mol. Med. (2003) 81:678-699.
  • Pre-fibrillar amyloid protein aggregates share common features of cytotoxicity. (M. Bucciantini, G. Calloni, F. Chiti, L. Formigli, D. Nosi, C.M. Dobson & M. Stefani) J. Biol. Chem. (2004) 279:31374-31382.
  • Monitoring the process of HypF fibrillization and liposome permeabilization by protofibrils (A. Relini, S. Torrassa, R. Rolandi, A. Gliozzi, C. Rosano, C., Canale, M. Bolognesi, G. Plakoutsi, M. Bucciantini, F. Chiti. & M. Stefani) J. Mol. Biol. (2004) 338: 943-957.
  • Patterns of cell death triggered in two different cell lines by HypF-N pre-fibrillar aggregates (M. Bucciantini, S. Rigacci, A. Berti, L. Pieri, C. Cecchi, D. Nosi, L. Formigli, F. Chiti & M. Stefani) FASEB J. (2005) 19:437-439.
  • Different cell lines are variously affected by the exposure to amyloid pre-fibrillar aggregates (C. Cecchi, S. Baglioni, C. Fiorillo, A. Pensalfini, G. Liguri, D. Nosi, S. Rigacci, M. Bucciantini & M. Stefani) J. Cell Sci. (2005) 118:3459-3470.
  • The yeast prion Ure2p native-like assemblies are toxic to mammalian cells regardless to their aggregation state (L. Pieri, M. Bucciantini, D. Nosi, L. Formigli, J. Savistchenko, R. Melki & M. Stefani) J. Biol. Chem. (2006) 281:15337-15344.
  • Prefibrillar amyloid aggregates could be generic toxins in higher organisms (S. Baglioni, F. Casamenti, M. Bucciantini, L.M. Luheshi, N. Taddei, F. Chiti, C.M. Dobson & M. Stefani) J. Neurosci. (2006) 26:8160-8167. .
  • Biological function in a non-native partially folded state of a protein. (F. Bemporad, J. Gsponer, H.I. Hopearuoho, G. Plakoutsi, G. Stati, M. Stefani, N. Taddei, M. Vendruscolo & F. Chiti) EMBO J. (2008) 27:1525-35.
  • Synthetic lipid vesicles recruit native-like aggregates and affect the aggregation process of the prion ure2p; insights on vesicle permeabilization and charge selectivity (L. Pieri, M. Bucciantini, P. Guasti, J. Savistchenko, R. Melki & M. Stefani) Biophys. J. (2009) 96:3319-3330.
  • Aberrant protein oligomer structures are causatively linked to cellular dysfunction (S. Campioni, B. Mannini, A. Pensalfini, M. Zampagni, C. Parrini, E. Evangelisti, A. Relini, M. Stefani, C.M. Dobson, C. Cecchi & F. Chiti) Nat. Chem. Biol. (2010) 6:140-147.
  • Toxic effects of amyloid fibrils on cell membranes: the importance of ganglioside GM1 (M. Bucciantini, D. Nosi, M. Forzan, E. Russo, M. Calamai, L. Pieri, L. Formigli, F. Quercioli, S. Soria, F. Pavone, J. Savistchenko, R. Melki & M. Stefani) FASEB J. (2012) 26:818-31.
  • Structural features and cytotoxicity of amyloid oligomers: implications in Alzheimer’s disease and other diseases with amyloid deposits. (M. Stefani) Progress Neurobiol. (2012) 99:226-45.
  • The polyphenol oleuropein aglycone protects TgCRND8 mice against Aß plaque pathology (C, Grossi, S. Rigacci, S. Ambrosini, T. Ed Dami, I. Luccarini, C. Traini, P. Failli, A. Berti, F. Casamenti & M. Stefani) (2013) PLoS One 8:e717023.
  • Amyloid aggregation: role of biological membranes and the aggregate-membrane system (M. Bucciantini, S. Rigacci & M. Stefani) J. Phys. Chem. Lett. (2014) 5:517-27.
  • Oleuropein aglycone induces autophagy in exposed cells: a mechanistic study (S. Rigacci, C. Miceli, C. Nediani, A. Berti and M. Stefani) Oncotarget (2015) 6:35344-57.
  • Binding affinity of amyloid oligomers to cellular membranes is a generic indicator of cellular dysfunction in protein misfolding diseases (E. Evangelisti, R. Cascella, M. Becatti, G. Marrazza, C.M. Dobson, F. Chiti, M. Stefani and C. Cecchi) Sci. Rep. (2016) 6:32721. 92.
  • Biochemical and electrophysiological modifications in cardiac myocytes exposed to amyloid aggregates of wild-type transthyretin (L. Sartiani, M. Bucciantini, V. Spinelli, M. Leri, A. Natalello, D. Nosi, S. Doglia, A. Relini, A. Penco, S. Giorgetti, E. Gerace, G. Mannaioni, V. Bellotti, S. Rigacci, E. Cerbai and M. Stefani) Biophys. J. (2016) 111:2024-38.
  • An FTIR microspectroscopy study of the structural and biochemical perturbations induced by natively folded and aggregated transthyretin in HL-1 cardiomyocytes. (D. Ami, P. Mereghetti, A. Nataliello, M. Leri, S.M. Doglia, V. Bellotti, M. Stefani and M. Bucciantini) Sci. Rep. (2018) 8:12508
ultimo aggiornamento: 28-Feb-2019
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