Yusuf Hamied Department of Chemistry

Publications by Professor Sir Alan Fersht FRS

Characterization of the p53-rescue drug CP-31398 in vitro and in living cells
TM Rippin, VJN Bykov, SMV Freund, G Selivanova, KG Wiman, AR Fersht
Oncogene
(2002)
21
(doi: 10.1038/sj.onc.1205362)
Max Ferdinand Perutz OM FRS - Obituary
AR Fersht
NATURE STRUCTURAL BIOLOGY
(2002)
9
(doi: 10.1038/nsb0402-245)
A structural double-mutant cycle: estimating the strength of a buried salt bridge in barnase
CK Vaughan, P Harryson, AM Buckle, AR Fersht
Acta Crystallographica Section D, Structural Biology
(2002)
58
(doi: 10.1107/s0907444902001567)
Protein folding and unfolding at atomic resolution
AR Fersht, V Daggett
Cell
(2002)
108
(doi: 10.1016/s0092-8674(02)00620-7)
Cooperativity in ATP hydrolysis by GroEL is increased by GroES.
TE Gray, AR Fersht
FEBS Letters
(2002)
292
(doi: 10.1016/0014-5793(91)80878-7)
Folding of the yeast prion protein Ure2: Kinetic evidence for folding and unfolding intermediates
D Galani, AR Fersht, S Perrett
Journal of Molecular Biology
(2002)
315
(doi: 10.1006/jmbi.2001.5234)
A peptide that binds and stabilizes p53 core domain:: Chaperone strategy for rescue of oncogenic mutants
A Friedler, LO Hansson, DB Veprintsev, SMV Freund, TM Rippin, PV Nikolova, MR Proctor, S Rüdiger, AR Fersht
Proceedings of the National Academy of Sciences of the United States of America
(2002)
99
(doi: 10.1073/pnas.241629998)
Loss of a metal-binding site in gelsolin leads to familial amyloidosis-Finnish type
SL Kazmirski, RL Isaacson, C An, A Buckle, CM Johnson, V Daggett, AR Fersht
Nature Structural & Molecular Biology
(2002)
9
(doi: 10.1038/nsb745)
New Look and New Outlook
WA Hendrickson, C-I Brändén, AR Fersht
Structure
(2002)
10
(doi: 10.1016/s0969-2126(01)00704-3)
Measurement of barnase refolding rate constants under denaturing conditions
JM Sanz, AR Fersht
FEBS Lett
(2001)
344
(doi: 10.1016/0014-5793(94)00384-X)
Hydrolysis of small peptide substrates parallels binding of chymotrypsin inhibitor 2 for mutants of subtilisin BPN'.
J Eder, M Rheinnecker, AR Fersht
FEBS letters
(2001)
335
(doi: 10.1016/0014-5793(93)80417-S)
Protein folding and stability: the pathway of folding of barnase
AR Fersht
FEBS letters
(2001)
325
(doi: 10.1016/0014-5793(93)81405-o)
Protein folding and stability: the pathway of folding of barnase
AR Fersht
FEBS Letters
(2001)
325
(doi: 10.1016/0014-5793(93)81405-O)
Modification of the amino acid specificity of tyrosyl‐tRNA synthetase by protein engineering
G de Prat Gay, HW Duckworth, AR Fersht
FEBS Lett
(2001)
318
(doi: 10.1016/0014-5793(93)80014-l)
Ultrafast folding of WW domains without structured aromatic clusters in the denatured state.
N Ferguson, CM Johnson, M Macias, H Oschkinat, A Fersht
Proceedings of the National Academy of Sciences of the United States of America
(2001)
98
(doi: 10.1073/pnas.221467198)
Using flexible loop mimetics to extend Phi-value analysis to secondary structure interactions
N Ferguson, JR Pires, F Toepert, CM Johnson, YP Pan, R Volkmer-Engert, J Schneider-Mergener, V Daggett, H Oschkinat, A Fersht
Proceedings of the National Academy of Sciences
(2001)
98
(doi: 10.1073/pnas.221467398)
The catalytic activity of the inactive conformation of δ‐chymotrypsin
AR Fersht
FEBS Lett
(2001)
29
(doi: 10.1016/0014-5793(73)80039-0)
Stability and solvation of Thr/Ser to Ala and Gly mutations at the N-cap of alpha-helices.
YW Chen, AR Fersht
FEBS Letters
(2001)
347
(doi: 10.1016/0014-5793(94)00574-5)
Rescuing the function of mutant p53.
AN Bullock, AR Fersht
Nature Reviews Cancer
(2001)
1
(doi: 10.1038/35094077)
[Folding mechanism and folding rate].
T Ikura, AR Fersht
Protein (Tokyo)
(2001)
46
Yusuf Hamied Department of Chemistry
Lensfield Road
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CB2 1EW
T: +44 (0) 1223 336300
enquiries@ch.cam.ac.uk
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