Alan Roy Fersht

Affiliations: 
Chemistry University of Cambridge, Cambridge, England, United Kingdom 
Area:
protein engineering, protein folding, and enzyme catalysis
Website:
http://www.ch.cam.ac.uk/person/arf25
Google:
"Alan Fersht"
Bio:

The Copley Medal 2020 was awarded to Sir Alan Fersht for developing and applying "the methods of protein engineering to provide descriptions of protein folding pathways at atomic resolution, revolutionising our understanding of these processes."
https://royalsociety.org/people/alan-fersht-11430/
http://www.nasonline.org/member-directory/members/64214.html

Mean distance: 9.02
 

Parents

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Anthony J. Kirby grad student 1965-1968 Cambridge
William P. Jencks post-doc 1968-1969 Brandeis

Children

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Markus A. Seeliger grad student (Cell Biology Tree)
Alan J. Russell grad student 1987 Imperial College London (BME Tree)
Elizabeth Meiering grad student 1992 Cambridge
Paul A Dalby grad student 1994-1998 Cambridge University UK
Andreas G Ladurner grad student 1994-1998 University of Cambridge and MRC
Javier Sancho post-doc Cambridge University UK (Computational Biology Tree)
Robin John Leatherbarrow post-doc 1984-1985 Imperial College London
Jesus M Sanz post-doc 1992-1994
Assaf Friedler post-doc 2000-2004 Cambridge
Frank M. Boeckler post-doc 2006-2008
Joel L. Kaar post-doc 2008-2010 Cambridge (Neurotree)
M. Eugenio Vazquez research scientist 1998-1998 Cambridge
BETA: Related publications

Publications

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Fersht AR, Cohen FE. (2019) Folding & Design: introduction to a new journal. Folding & Design. 1: i
Baretić D, Pollard HK, Fisher DI, et al. (2017) Structures of closed and open conformations of dimeric human ATM. Science Advances. 3: e1700933
Bromley D, Bauer MR, Fersht AR, et al. (2016) An in silico algorithm for identifying stabilizing pockets in proteins: test case, the Y220C mutant of the p53 tumor suppressor protein. Protein Engineering, Design & Selection : Peds
Bauer MR, Jones RN, Baud MG, et al. (2016) Harnessing fluorine-sulfur contacts and multipolar interactions for the design of p53 mutant Y220C rescue drugs. Acs Chemical Biology
Joerger AC, Bauer MR, Wilcken R, et al. (2015) Exploiting Transient Protein States for the Design of Small-Molecule Stabilizers of Mutant p53. Structure (London, England : 1993). 23: 2246-55
Wilcken R, Zimmermann MO, Bauer MR, et al. (2015) Experimental and theoretical evaluation of the ethynyl moiety as a halogen bioisostere. Acs Chemical Biology
Nasedkin A, Marcellini M, Religa TL, et al. (2015) Deconvoluting Protein (Un)folding Structural Ensembles Using X-Ray Scattering, Nuclear Magnetic Resonance Spectroscopy and Molecular Dynamics Simulation. Plos One. 10: e0125662
Brandt T, Kaar JL, Fersht AR, et al. (2012) Stability of p53 Homologs Plos One. 7
Vogel SM, Bauer MR, Joerger AC, et al. (2012) Lithocholic acid is an endogenous inhibitor of MDM4 and MDM2 Proceedings of the National Academy of Sciences of the United States of America. 109: 16906-16910
Wilcken R, Wang G, Boeckler FM, et al. (2012) Kinetic mechanism of p53 oncogenic mutant aggregation and its inhibition Proceedings of the National Academy of Sciences of the United States of America. 109: 13584-13589
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