Fabrizio Chiti

Associate Professor at Department of Biochemistry
University of Florence
fabrizio.chiti@unifi.it

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Publications

Fabrizio Chiti is author of 92 publications in international peer-reviewed journals. These include 61 papers published since he became group leader at the end of 2002. A list of 20 relevant publications appears below.

 

• Campioni S, Mannini B, Zampagni M, Pensalfini A, Parrini C, Evangelisti E, Relini A, Stefani M, Dobson CM, Cecchi C, Chiti F. (2009). A causative link between the structure of aberrant protein oligomers and their toxicity. Nature Chem. Biol.6, 140-147.
• Chiti F and Dobson CM (2009). Amyloid formation by globular proteins under native conditions. Nature Chem. Biol. 5, 15-22.
• Chiti F and Bellotti V (2008). Amyloidogenesis in its biological environment: challenging a fundamental issue in protein misfolding diseases. Curr. Op. Struct. Biol.18, 771-779.
• Calloni G, Lendel C, Campioni S, Giannini S, Gliozzi A, Relini A, Vendruscolo M, Dobson CM, Salvatella X, Chiti F. (2008). Structure and dynamics of a partially folded protein are decoupled from its mechanism of aggregation. J. Am. Chem. Soc.130, 13040-13050.
• Bemporad F, Gsponer J, Hopeharuoho HI, Plakoutsi G, Stati G, Stefani M, Taddei N, Vendruscolo M, Chiti F (2008). Biological function in a non-native partially folded state of a protein. EMBOJ. 27, 1525-1535.
• Soldi G, Bemporad F, Chiti F (2008). The Degree of Structural Protection at the Edge b-Strands Determines the Pathway of Amyloid Formation in Globular Proteins. J. Am. Chem. Soc. 130, 4295-302.
• Luheshi LM, Tartaglia GG, Brorsson AC, Pawar AP, Watson IA, Vendruscolo M, Lomas DA, Dobson CM, Crowther DC (2007). Systematic in vivoAnalysis of the Intrinsic Determinants of Amyloid b Pathogenicity. PloS Biol.5, e290.
• Monsellier E and Chiti F (2007). "Prevention of amyloid-like aggregation as a driving force of protein evolution". EMBO Reports8, 737-742.
• Bemporad F, Calloni G, Campioni S, Plakoutsi G, Taddei N and Chiti F (2006). Invited review titled Sequence and Structural Determinants of amyloid fibril formation. Accounts of Chemical Research39, 620-627.
• Chiti F and Dobson CM (2006). Protein misfolding, functional amyloid, and human disease. Ann. Rev. Biochem. 75, 333-366.
• Fowler SB, Poon S, Muff R, Chiti F, Dobson CM, Zurdo J. (2005). Rational design of aggregation-resistant bioactive peptides: reengineering human calcitonin. Proc. Natl. Acad. Sci. USA102, 10105-10110.
• Chiti F, Stefani M, Taddei N, Ramponi G, Dobson CM. (2003). Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 424, 805-808.
• Chiti F, Calamai M, Taddei N, Stefani M, Ramponi G, Dobson CM. (2002). Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases. Proc. Natl. Acad. Sci. USA99, 16419-16426.
• Bucciantini M., Giannoni E., Chiti F., Baroni F., Formigli L., Zurdo J., Taddei N., Ramponi G., Dobson C.M. and Stefani M. (2002). Inherent toxicity of aggregates implies a common origin for protein misfolding diseases. Nature 416, 507-511.
• Chiti F., Taddei N., Baroni F., Capanni C., Stefani M., Ramponi G. and Dobson C.M. (2002). Kinetic partitioning of protein folding and aggregation. Nature Struct. Biol.9, 137-143.
• Chiti F., Taddei N., Bucciantini M., White P., Ramponi G. and Dobson C.M. (2000). Mutational analysis of the propensity for amyloid formation by a globular protein. EMBO J.19, 1441-1449.
• Hamada D., Chiti F., Guijarro J.I., Kataoka M., Taddei N. and Dobson C.M. (2000). Evidence concerning rate-limiting steps in protein folding from the effects of trifluoroethanol. Nature Struct. Biol.7, 58-61.
• Chiti F., Webster M., Taddei N., Clark, A., Stefani M., Ramponi G. and Dobson C.M. (1999). Designing conditions for in vitro formation of amyloid fibrils. Proc. Natl. Acad. Sci.USA96, 3590-3594.
• Chiti F., Taddei N., White P.M., Bucciantini M., Magherini F., Stefani M. and Dobson C.M. (1999). Mutational analysis of acylphosphatase reveals the importance of topology and contact order in protein folding. Nature Struct. Biol. 6, 1005-1009.
• Chiti F., Taddei N., Webster P., Hamada D., Fiaschi T., Ramponi G. and Dobson C.M. (1999). Acceleration of the folding of acylphosphatase by stabilisation of local secondary structure. Nature Struct. Biol.6, 380-387.