Fabrizio Chiti

Italian biochemist From Wikipedia, the free encyclopedia

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

Born (1971-07-07) 7 July 1971 (age 54)
Florence, Italy
AlmamaterBiological Sciences, University of Florence, Italy(E.N.S., 1995)
Awards
Quick facts Born, Alma mater ...
Fabrizio Chiti
Fabrizio Chiti in 2015
Born (1971-07-07) 7 July 1971 (age 54)
Florence, Italy
Alma materBiological Sciences, University of Florence, Italy(E.N.S., 1995)
Known forProtein aggregation and amyloid
Awards
Scientific career
FieldsBiophysics, Biochemistry
InstitutionsDepartment of Experimental and Clinical Biomedical Sciences, University of Florence
Doctoral advisorChris Dobson
Other academic advisorsGiampietro Ramponi, Chris Dobson
Websitewww.sbsc.unifi.it/vp-209-gruppo-chiti.html
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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

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