Fabrizio_Chiti

Fabrizio Chiti

Fabrizio Chiti

Italian biochemist


Fabrizio Chiti (born in Florence, 7 July 1971) is an Italian biochemist noted for his work on Protein aggregation and amyloid.[1]

Quick Facts Born, Alma mater ...

Education

Chiti 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

He 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


References

  1. "Citation metrics, Scopus". Retrieved 5 October 2019.
  2. 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.
  3. 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.
  4. 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.
  5. 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.
  6. 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.

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