Fabrizio Chiti (born in Florence, 7 July 1971) is an Italian biochemist noted for his work on Protein aggregation and amyloid.[1]
Fabrizio Chiti | |
---|---|
Born | Florence, Italy | 7 July 1971
Alma mater | Biological Sciences, University of Florence, Italy(E.N.S., 1995) |
Known for | Protein aggregation and amyloid |
Awards |
|
Scientific career | |
Fields | Biophysics, Biochemistry |
Institutions | Department of Experimental and Clinical Biomedical Sciences, University of Florence |
Doctoral advisor | Chris Dobson |
Other academic advisors | Giampietro Ramponi, Chris Dobson |
Website | www |
Education
editChiti is a graduate in Biological Sciences of the University of Florence (Italy).[2] He attained a PhD degree (D.Phil) in Chemistry in 2000 at the University of Oxford in UK.[2] He then worked as a postdoctoral researcher at the University of Florence, Italy, with Giampietro Ramponi as a supervisor (2000–2002) and at the University of Cambridge, UK, under the supervision of Chris Dobson (2002).[2]
Research and career
editHe was appointed as an Associate (2002) and then Full Professor (2010) at the University of Florence in Biochemistry.[2] Chiti provided contributions in the field of misfolding and aggregation, particularly in the field of amyloid[1] He rationalized how amino acid mutations induce protein aggregation and edited an equation to predict the effect of mutations on the aggregation of an unfolded protein,[3][4] which led to a search by many investigators of algorithms with predictive power on essential aspects of protein aggregation. He also correlated the toxicities of abnormal protein oligomers with specific structural properties of them.[5] His 2006 review with Chris Dobson on protein misfolding, amyloid formation and human disease,[6] later updated as a new report,[7] is a reference paper in the field of amyloid and received, as of October 2019, more than four thousands citations in scientific publications.[1][8]
Awards and honors
edit- Election to EMBO Young Investigator program, European Molecular Biology Organization, 2005[9]
- Election to member of Academia Europaea, 2015[10]
- Jean-Francois LeFèvre Lecture, École supérieure de biotechnologie Strasbourg, 2003[11]
- Maria Teresa Messori Roncaglia ed Eugenio Mari Award, Accademia Nazionale dei Lincei, 2010[12]
References
edit- ^ a b c "Citation metrics, Scopus". Retrieved 5 October 2019.
- ^ a b c d "CV details on the official page of the University of Florence".
- ^ Chiti F, Taddei N, Bucciantini M, White P, Ramponi G, Dobson CM (3 April 2000). "Mutational analysis of the propensity for amyloid formation by a globular protein". EMBO Journal. 19 (7): 1441–9. doi:10.1093/emboj/19.7.1441. PMC 310213. PMID 10747012.
- ^ Chiti F, Stefani M, Taddei N, Ramponi G, Dobson CM (14 August 2003). "Rationalization of the effects of mutations on peptide and protein aggregation rates". Nature. 424 (6950): 805–8. Bibcode:2003Natur.424..805C. doi:10.1038/nature01891. PMID 12917692. S2CID 4421180.
- ^ Campioni S, Mannini B, Zampagni M, Pensalfini A, Parrini C, Evangelisti E, Relini A, Stefani M, Dobson CM, Cecchi C, Chiti F (February 2010). "A causative link between the structure of aberrant protein oligomers and their toxicity". Nature Chemical Biology. 6 (2): 140–7. doi:10.1038/nchembio.283. hdl:2158/382930. PMID 20081829. S2CID 43311039.
- ^ Chiti F, Dobson CM (5 June 2006). "Protein misfolding, functional amyloid, and human disease". Annual Review of Biochemistry. 75: 333–66. doi:10.1146/annurev.biochem.75.101304.123901. PMID 16756495. S2CID 23797549.
- ^ Chiti F, Dobson CM (20 June 2017). "Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade". Annual Review of Biochemistry. 86: 26–68. doi:10.1146/annurev-biochem-061516-045115. hdl:2158/1117236. PMID 28498720.
- ^ "Citations to Fabrizio Chiti, source Google Scholars".
- ^ "Membership to EMBO Young Investigator Program to Fabrizio Chiti".
- ^ "Membership to Academia Europaea to Fabrizio Chiti".
- ^ "Quotation to Jean-Francois LeFèvre Lecture".
- ^ "List of Awards at Academia Nazionale dei Lincei".