Michele Vendruscolo

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Michele Vendruscolo
Michele Vendruscolo.jpg
Michele Vendruscolo in 2019
Born (1966-07-23) 23 July 1966 (age 55)
Udine, Italy
Alma materPhysics, University of Trieste, Italy(E.N.S., 1992)
Known forProtein folding and misfolding
Awards
Scientific career
FieldsPhysics, chemistry, neuroscience
InstitutionsDepartment of Chemistry, University of Cambridge
Doctoral advisorAmos Maritan
Other academic advisorsEytan Domany, Chris Dobson
Websitewww-vendruscolo.ch.cam.ac.uk

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]

Education[]

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]

Research and career[]

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]

Awards and honors[]

References[]

  1. ^ Jump up to: a b "Citation metrics, Scopus". Retrieved 30 September 2019.
  2. ^ Jump up to: a b c d "CV details within the election to the Academia Europaea".
  3. ^ "professorship at the University of Cambridge". Retrieved 30 September 2019.
  4. ^ "Director of Chemistry of Health and co-director of the Centre for Misfolding Diseases". Retrieved 30 September 2019.
  5. ^ 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.
  6. ^ 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.
  7. ^ 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.
  8. ^ 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.
  9. ^ "Membership to EMBO Young Investigator Program to Michele Vendruscolo".
  10. ^ "Soft Matter & Biophysical Chemistry Award to Michele Vendruscolo".
  11. ^ "Membership to Academia Europaea to Michele Vendruscolo".
  12. ^ https://www.iop.org/about/awards/bilateral/occhialini/medallists/page_38497.html
  13. ^ "Rita and John Cornforth Award to Chris Dobson, Michele Vendruscolo and Tuomas Knowles".

External links[]

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