M
Massimo Stefani
Researcher at University of Florence
Publications - 179
Citations - 15811
Massimo Stefani is an academic researcher from University of Florence. The author has contributed to research in topics: Acylphosphatase & Protein aggregation. The author has an hindex of 55, co-authored 175 publications receiving 14733 citations. Previous affiliations of Massimo Stefani include University of Cambridge & University of Pavia.
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Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases.
Monica Bucciantini,Elisa Giannoni,Fabrizio Chiti,Fabrizio Chiti,Fabiana Baroni,Lucia Formigli,Jesús Zurdo,Niccolò Taddei,Giampietro Ramponi,Christopher M. Dobson,Massimo Stefani +10 more
TL;DR: This finding provides added evidence that avoidance of protein aggregation is crucial for the preservation of biological function and suggests common features in the origins of this family of protein deposition diseases.
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Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution
TL;DR: The 'new view' of these diseases suggests that other degenerative conditions could have similar underlying origins to those of the amyloidoses, and suggests some intriguing new factors that could be of great significance in the evolution of biological molecules and the mechanisms that regulate their behaviour.
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Rationalization of the effects of mutations on peptide and protein aggregation rates.
TL;DR: It is shown that the intrinsic effects of specific mutations on the rates of aggregation of unfolded polypeptide chains can be correlated to a remarkable extent with changes in simple physicochemical properties such as hydrophobicity, secondary structure propensity and charge.
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Designing conditions for in vitro formation of amyloid protofilaments and fibrils
Fabrizio Chiti,Paul Webster,Niccolò Taddei,Anne Clark,Massimo Stefani,Giampietro Ramponi,Christopher M. Dobson +6 more
TL;DR: The results indicate that formation of amyloid occurs when the native fold of a protein is destabilized under conditions in which noncovalent interactions, and in particular hydrogen bonding, within the polypeptide chain remain favorable.
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A causative link between the structure of aberrant protein oligomers and their toxicity
Silvia Campioni,Benedetta Mannini,Mariagioia Zampagni,Anna Pensalfini,Anna Pensalfini,Claudia Parrini,Elisa Evangelisti,Annalisa Relini,Massimo Stefani,Christopher M. Dobson,Cristina Cecchi,Fabrizio Chiti +11 more
TL;DR: It is suggested that structural flexibility and hydrophobic exposure are primary determinants of the ability of oligomeric assemblies to cause cellular dysfunction and its consequences, such as neurodegeneration.