On weekends, Fabrizio Chiti can be found behind the wheel of his RV, exploring the Italian countryside with his wife and daughter. A decade ago, as an undergraduate at the University of Florence, Chiti never imagined he would be doing science in his home country, let alone in the same department where he became fascinated by proteins. "I was told there were no chances for me," Chiti says. "The opportunities and funding for science were not very good in Florence at that period."
A young Chiti heeded the warning and left for the University of Oxford in 1996 to do his doctoral work with Chris Dobson. Chiti spent three years researching the folding properties of muscle acylphosphatase. Before Chiti's graduation, however, Dobson's interests shifted to protein aggregation, and Chiti was reluctant to follow. "I was deeply involved in protein folding," Chiti says. Dobson wanted his...
Title: Associate professor, Department of Biochemical Science, University of Florence
1. F. Chiti et al., "Designing conditions for in vitro formation of amyloid protofilaments and fibrils," Proc Natl Acad Sci, 96:3590-4, 1999. (Cited in 383 papers) 2. M. Bucciantini et al., "Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases," Nature, 416:507-11, 2002. (Cited in 527 papers) 3. F. Chiti et al., "Rationalization of the effects of mutations on peptide and protein aggregation rates," Nature, 424:805-8, 2003. (Cited in 165 papers)