Alan Fersht
Alan Fersht
Emeritus Group Leader, MRC Laboratory of Molecular Biology, University of Cambridge
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Cited by
Cited by
Enzyme Structure and Mechanism
A Fersht
WH Freeman, New York, NY, 1977
Structure and mechanism in protein science: a guide to enzyme catalysis and protein folding
A Fersht
Macmillan, 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
Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition
SE Jackson, AR Fersht
Biochemistry 30 (43), 10428-10435, 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
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
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
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
Rescuing the function of mutant p53
AN Bullock, AR Fersht
Nature Reviews Cancer 1 (1), 68-76, 2001
Structural Biology of the Tumor Suppressor p53
A Joerger, AR Fersht
Annual Review of Biochemistry 77, 557-582, 2008
Nucleation mechanisms in protein folding
AR Fersht
Current opinion in structural biology 7 (1), 3-9, 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
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
Rapid, electrostatically assisted association of proteins
G Schreiber, AR Fersht
Nature structural biology 3 (5), 427-431, 1996
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
The hydrogen bond in molecular recognition
AR Fersht
Trends in Biochemical Sciences 12, 301-304, 1987
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
The p53 pathway: origins, inactivation in cancer, and emerging therapeutic approaches
AC Joerger, AR Fersht
Annual review of biochemistry 85, 375-404, 2016
Protein folding and unfolding at atomic resolution
AR Fersht, V Daggett
Cell 108 (4), 573-582, 2002
Is there a unifying mechanism for protein folding?
V Daggett, AR Fersht
Trends in biochemical sciences 28 (1), 18-25, 2003
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