Michele_Vendruscolo
Michele Vendruscolo
Italian British physicist
Michele Vendruscolo (born in Udine, 23 July 1966) is an Italian British physicist working in the UK, noted for his theoretical and experimental work on protein folding, misfolding and aggregation.[1]
Michele Vendruscolo | |
|---|---|
Michele Vendruscolo in 2019 | |
| Born | (1966-07-23) 23 July 1966 (age 57) Udine, Italy |
| Alma mater | Physics, University of Trieste, Italy(E.N.S., 1992) |
| Known for | Protein folding and misfolding |
| Awards | |
| Scientific career | |
| Fields | Physics, chemistry, neuroscience |
| Institutions | Department of Chemistry, University of Cambridge |
| Doctoral advisor | Amos Maritan |
| Other academic advisors | Eytan Domany, Chris Dobson |
| Website | www-vendruscolo |
Vendruscolo is a graduate in physics of the University of Trieste (Italy).[2] He received a Master of Science (MSc) and a PhD in condensed matter physics at the International School for Advanced Studies in Trieste, Italy.[2] He then worked as a postdoctoral researcher, at the Weizmann Institute, Israel with Eytan Domany as a supervisor (1996–1998) and at the University of Oxford (1999–2001) under the supervision of Chris Dobson.[2]
He was appointed as an independent academic at the University of Cambridge as a Royal Society University Research Fellow (2001), as a Lecturer (2006), and then as a Reader (2008) in Theoretical Chemical Biology.[2] He is now Professor of Biophysics at the same university.[3] He is also Director of Chemistry of Health, and Co-Director of the Centre for Misfolding Diseases at the University of Cambridge.[4]
Vendruscolo provided contributions in the field of protein folding, misfolding and aggregation.[1] He introduced the approach of simulating complex protein structures in transient or otherwise undetectable states (transition states, transient intermediates, transient aggregates, etc.) using exploitable experimental data as restraints.[5][6] He edited computational programs able to predict essential characteristics of protein folding and protein aggregation.[7] In a collaboration with other scholars he dissected the process of Amyloid fibril formation in its microscopic steps and computed programs to analyse experimental kinetic time courses and study effects of Small molecules and other agents.[8]
- Election to EMBO Young Investigator program, European Molecular Biology Organization, 2008[9]
- Soft Matter & Biophysical Chemistry Award, Royal Society of Chemistry, 2013[10]
- Election to member of Academia Europaea, 2017[11]
- Awarded Giuseppe Occhialini Medal and Prize, 2017[12]
- Rita and John Cornforth Award, Royal Society of Chemistry, 2019[13]
- "Citation metrics, Scopus". Retrieved 30 September 2019.
- "professorship at the University of Cambridge". Retrieved 30 September 2019.
- "Director of Chemistry of Health and co-director of the Centre for Misfolding Diseases". Retrieved 30 September 2019.
- Cavalli A, Salvatella X, Dobson CM, Vendruscolo M (5 June 2007). "Protein structure determination from NMR chemical shifts". PNAS. 104 (23): 9615–20. Bibcode:2007PNAS..104.9615C. doi:10.1073/pnas.0610313104. PMC 1887584. PMID 17535901.
- Lindorff-Larsen K, Best RB, Depristo MA, Dobson CM, Vendruscolo M (13 January 2005). "Simultaneous determination of protein structure and dynamics". Nature. 433 (7022): 128–32. Bibcode:2005Natur.433..128L. doi:10.1038/nature03199. PMID 15650731. S2CID 15105531.
- Tartaglia GG, Pawar AP, Campioni S, Dobson CM, Chiti F, Vendruscolo M (4 July 2008). "Prediction of aggregation-prone regions in structured proteins". Journal of Molecular Biology. 380 (2): 425–36. doi:10.1016/j.jmb.2008.05.013. PMID 18514226. S2CID 16410867.
- Knowles TP, Vendruscolo M, Dobson CM (June 2014). "The amyloid state and its association with protein misfolding diseases". Nature Reviews Molecular Cell Biology. 15 (6): 384–96. doi:10.1038/nrm3810. PMID 24854788. S2CID 46357173.
- "Occhialini medal recipients". www.iop.org. Archived from the original on 9 March 2011.
