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 over 100 publications in international peer-reviewed journals. These include more than 70 papers published since he became group leader at the end of 2002. A list of 20 relevant publications appears below.

 

• Mannini B, Cascella R, Zampagni M, van Waarde-Verhagen M, Meehan S, Roodveldt C, Campioni S, Boninsegna M, Penco A, Relini A, Kampinga HH, Dobson CM, Wilson MR, Cecchi C, Chiti F (2012). Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers. Proc. Natl. Acad. Sci. USA 109, 12479-12484.
  

• Motamedi-Shad N, Garfagnini T, Penco A, Relini A, Fogolari F, Corazza A, Esposito G, Bemporad F, Chiti F (2012). Rapid oligomer formation of human muscle acylphosphatase induced by heparan sulfate. Nature Struct. Mol. Biol. 19, 547-554.
  

• De Simone A, Dhulesia A, Soldi G, Vendruscolo M, Hsu ST, Chiti F, Dobson CM (2011). Experimental free energy surfaces reveal the mechanisms of maintenance of protein solubility. Proc. Natl. Acad. Sci. USA. 108, 21057-21062.
  

• Belli M, Ramazzotti M, Chiti F (2011). Prediction of amyloid aggregation in vivo. EMBO Rep. 12, 657-663.
  

• Campioni S, Mannini B, Zampagni M, Pensalfini A, Parrini C, Evangelisti E, Relini A, Stefani M, Dobson CM, Cecchi C, Chiti F (2010). 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. EMBO J. 27, 1525-1535.
  

• Soldi G, Bemporad F, Chiti F (2008). The Degree of Structural Protection at the Edge β-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 vivo Analysis of the Intrinsic Determinants of Amyloid β Pathogenicity. PloS Biol. 5, e290.
  

• Monsellier E and Chiti F (2007). "Prevention of amyloid-like aggregation as a driving force of protein evolution". EMBO Reports 8, 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. Acc. Chem. Research 39, 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. USA 102, 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.
  

• Bucciantini M, Giannoni E, Chiti F, Baroni F, Formigli L, Zurdo J, Taddei N, Ramponi G, Dobson CM 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 CM (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 CM (2000). Mutational analysis of the propensity for amyloid formation by a globular protein. EMBO J. 19, 1441-1449.
  

• Chiti F, Webster M, Taddei N, Clark A, Stefani M, Ramponi G and Dobson CM (1999). Designing conditions for in vitro formation of amyloid fibrils. Proc. Natl. Acad. Sci.USA 96, 3590-3594.

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