N
Niccolò Taddei
Researcher at University of Florence
Publications - 115
Citations - 10277
Niccolò Taddei is an academic researcher from University of Florence. The author has contributed to research in topics: Acylphosphatase & Protein folding. The author has an hindex of 44, co-authored 113 publications receiving 9630 citations. Previous affiliations of Niccolò Taddei include University of Cambridge.
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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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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.
Journal ArticleDOI
Kinetic partitioning of protein folding and aggregation.
Fabrizio Chiti,Niccolò Taddei,Fabiana Baroni,Cristina Capanni,Massimo Stefani,Giampietro Ramponi,Christopher M. Dobson,Christopher M. Dobson +7 more
TL;DR: Dissection of the protein into six peptides corresponding to different regions of the sequence indicates that the kinetic partitioning between aggregation and folding can be attributed to the intrinsic conformational preferences of the denatured polypeptide chain.
Journal ArticleDOI
Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding.
Fabrizio Chiti,Niccolò Taddei,Paul White,Monica Bucciantini,Francesca Magherini,Massimo Stefani,Christopher M. Dobson +6 more
TL;DR: Comparison of the rates of folding of AcP and four other proteins with the same topology, including ADA2h, supports the concept that the average distance in sequence between interacting residues (that is, the contact order) is an important determinant of the rate of protein folding.