Alan Fersht

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Andreas C. JoergerStructural Genomics Consortium (SGC), Institute of Pharmaceutical Chemistry, Goethe UniversityVerified email at pharmchem.uni-frankfurt.de
Valerie D. DaggettProfessor of Bioengineering, University of WashingtonVerified email at uw.edu
Christopher M JohnsonMRC Laboratory of Molecular BiologyVerified email at mrc-lmb.cam.ac.uk
Dmitry VeprintsevProfessor of Molecular and Cellular Pharmacology, University of NottinghamVerified email at nottingham.ac.uk
Andreas MatouschekThe University of Texas at AustinVerified email at austin.utexas.edu
Ashley BuckleReplayVerified email at replay.bio
Gideon schreiberweizmann or hadassah or cambridgeVerified email at weizmann.ac.il
Prof. Assaf FriedlerInstitute of Chemistry, The Hebrew University of JerusalemVerified email at mail.huji.ac.il
Javier sanchoprofessor of biochemistry, universidad de zaragozaVerified email at unizar.es
Paul J. CarterGenentechVerified email at gene.com
Dr S.E. JacksonUniversity of CambridgeVerified email at cam.ac.uk
Jane ClarkeVerified email at cam.ac.uk
Ugo MayorUniversity of the Basque Country UPV/EHU & IkerbasqueVerified email at ehu.eus
Frank M. BoecklerUniv. Professor, Lab for Molecular Design & Pharm. Biophysics, Eberhard Karls University TuebingenVerified email at uni-tuebingen.de
Tim SharpeUniversity of BaselVerified email at unibas.ch
Robin LeatherbarrowImperial College LondonVerified email at imperial.ac.uk
Matthias R. BauerNovartis Institutes for BioMedical ResearchVerified email at novartis.com
Gonzalo de Prat GayHead, Protein Structure-Function and Engineering Lab, Fundación Instituto Leloir-CONICET, ArgentinaVerified email at leloir.org.ar
Kam-Bo WONGProfessor, School of Life Sciences, The Chinese University of Hong KongVerified email at cuhk.edu.hk
Jean ChatellierProtein Engineering Center, Medical Research Council (Cambridge, UK)Verified email at kybora.com

Alan Fersht

Emeritus Group Leader, MRC Laboratory of Molecular Biology, University of Cambridge

Verified email at cam.ac.uk - Homepage

protein folding misfolding p53 and cancer


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Enzyme Structure and Mechanism A Fersht WH Freeman, New York, NY, 1977	6467	1977
Structure and mechanism in protein science: a guide to enzyme catalysis and protein folding A Fersht Macmillan, 1999	5732	1999
Hydrogen bonding and biological specificity analysed by protein engineering AR Fersht, JP Shi, J Knill-Jones, DM Lowe, AJ Wilkinson, DM Blow, ... Nature 314 (6008), 235-238, 1985	1348	1985
Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition SE Jackson, AR Fersht Biochemistry 30 (43), 10428-10435, 1991	1156	1991
Awakening guardian angels: drugging the p53 pathway CJ Brown, S Lain, CS Verma, AR Fersht, DP Lane Nature Reviews Cancer 9 (12), 862-873, 2009	1120	2009
The folding of an enzyme: I. Theory of protein engineering analysis of stability and pathway of protein folding AR Fersht, A Matouschek, L Serrano Journal of molecular biology 224 (3), 771-782, 1992	1070	1992
The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for … LS Itzhaki, DE Otzen, AR Fersht Journal of molecular biology 254 (2), 260-288, 1995	971	1995
Mapping the transition state and pathway of protein folding by protein engineering A Matouschek, JT Kellis Jr, L Serrano, AR Fersht Nature 340 (6229), 122-126, 1989	898	1989
Rescuing the function of mutant p53 AN Bullock, AR Fersht Nature Reviews Cancer 1 (1), 68-76, 2001	839	2001
Structural Biology of the Tumor Suppressor p53 A Joerger, AR Fersht Annual Review of Biochemistry 77, 557-582, 2008	822	2008
Nucleation mechanisms in protein folding AR Fersht Current opinion in structural biology 7 (1), 3-9, 1997	778	1997
Energetics of protein-protein interactions: Analysis ofthe Barnase-Barstar interface by single mutations and double mutant cycles G Schreiber, AR Fersht Journal of molecular biology 248 (2), 478-486, 1995	732	1995
The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus) PJ Carter, G Winter, AJ Wilkinson, AR Fersht Cell 38 (3), 835-840, 1984	714	1984
Rapid, electrostatically assisted association of proteins G Schreiber, AR Fersht Nature structural biology 3 (5), 427-431, 1996	698	1996
The p53 pathway: origins, inactivation in cancer, and emerging therapeutic approaches AC Joerger, AR Fersht Annual review of biochemistry 85 (1), 375-404, 2016	674	2016
Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications. AR Fersht Proceedings of the National Academy of Sciences 92 (24), 10869-10873, 1995	674	1995
PRIMA-1 reactivates mutant p53 by covalent binding to the core domain JMR Lambert, P Gorzov, DB Veprintsev, M Söderqvist, D Segerbäck, ... Cancer cell 15 (5), 376-388, 2009	667	2009
The hydrogen bond in molecular recognition AR Fersht Trends in Biochemical Sciences 12, 301-304, 1987	657	1987
Protein folding and unfolding at atomic resolution AR Fersht, V Daggett Cell 108 (4), 573-582, 2002	634	2002
Is there a unifying mechanism for protein folding? V Daggett, AR Fersht Trends in biochemical sciences 28 (1), 18-25, 2003	614	2003

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