Yusuf Hamied Department of Chemistry

Publications by Professor Sir Alan Fersht FRS

Stabilization of GroEL minichaperones by core and surface mutations
Q Wang, AM Buckle, AR Fersht
Journal of molecular biology
(2000)
298
(doi: 10.1006/jmbi.2000.3716)
Fast-folding proteins.
AR Fersht
ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY
(2000)
219
Towards a complete description of the structural and dynamic properties of the denatured state of barnase and the role of residual structure in folding.
KB Wong, J Clarke, CJ Bond, JL Neira, SM Freund, AR Fersht, V Daggett
Journal of molecular biology
(2000)
296
(doi: 10.1006/jmbi.2000.3523)
Characterization of in vitro oxidized barstar.
C Frisch, G Schreiber, AR Fersht
FEBS Lett
(2000)
370
(doi: 10.1016/0014-5793(95)00839-2)
Quantitative analysis of residual folding and DNA binding in mutant p53 core domain: definition of mutant states for rescue in cancer therapy
AN Bullock, J Henckel, AR Fersht
Oncogene
(2000)
19
(doi: 10.1038/sj.onc.1203434)
Untitled
JM Lehn, AR Fersht
EUROPEAN JOURNAL OF INORGANIC CHEMISTRY
(2000)
Increased rates of tRNA charging through modification of the enzyme‐aminoacyl‐adenylate complex of phenylalanyl‐tRNA synthetase
M Ibba, CM Johnson, H Hennecke, AR Fersht
FEBS Letters
(2000)
358
(doi: 10.1016/0014-5793(94)01454-9)
Transition-state structure as a unifying basis in protein-folding mechanisms: Contact order, chain topology, stability, and the extended nucleus mechanism
AR Fersht
Proceedings of the National Academy of Sciences of the United States of America
(2000)
97
(doi: 10.1073/pnas.97.4.1525)
Directed evolution of new catalytic activity using the alpha/beta-barrel scaffold.
MM Altamirano, JM Blackburn, C Aguayo, AR Fersht
Nature
(2000)
403
(doi: 10.1038/35001001)
Mechanism of rescue of common p53 cancer mutations by second-site suppressor mutations
PV Nikolova, KB Wong, B DeDecker, J Henckel, AR Fersht
The EMBO Journal
(2000)
19
(doi: 10.1093/emboj/19.3.370)
Interdomain interactions within the gene 3 protein of filamentous phage.
J Chatellier, O Hartley, AD Griffiths, AR Fersht, G Winter, L Riechmann
FEBS letters
(2000)
463
(doi: 10.1016/s0014-5793(99)01658-0)
Equilibria and kinetics of folding of gelsolin domain 2 and mutants involved in familial amyloidosis-Finnish type.
RL Isaacson, AG Weeds, AR Fersht
Proceedings of the National Academy of Sciences of the United States of America
(1999)
96
(doi: 10.1073/pnas.96.20.11247)
Formation of Short-Lived Protein Aggregates Directly from the Coil in Two-State Folding
M Silow, YJ Tan, AR Fersht, M Oliveberg
Biochemistry
(1999)
38
(doi: 10.1021/bi9909997)
NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution
N Kobayashi, SM Freund, J Chatellier, R Zahn, AR Fersht
Journal of Molecular Biology
(1999)
292
(doi: 10.1006/jmbi.1999.3042)
Identification of substrate binding site of GroEL minichaperone in solution
N Tanaka, AR Fersht
J Mol Biol
(1999)
292
(doi: 10.1006/jmbi.1999.3041)
GroEL recognises sequential and non-sequential linear structural motifs compatible with extended β-strands and α-helices 1 1Edited by J. Karn
J Chatellier, AM Buckle, AR Fersht
Journal of Molecular Biology
(1999)
292
(doi: 10.1006/jmbi.1999.3040)
The FHA domain is a modular phosphopeptide recognition motif
D Durocher, J Henckel, AR Fersht, SP Jackson
Molecular Cell
(1999)
4
(doi: 10.1016/s1097-2765(00)80340-8)
Hot-spot mutants of p53 core domain evince characteristic local structural changes.
KB Wong, BS DeDecker, SM Freund, MR Proctor, M Bycroft, AR Fersht
Proceedings of the National Academy of Sciences
(1999)
96
(doi: 10.1073/pnas.96.15.8438)
Equilibrium folding properties of the yeast prion protein determinant Ure211Edited by J. Karn
S Perrett, SJ Freeman, PJ Butler, AR Fersht
J Mol Biol
(1999)
290
(doi: 10.1006/jmbi.1999.2872)
The solution structure of oxidized Escherichia coli cytochrome b(562)
F Arnesano, L Banci, I Bertini, J Faraone-Mennella, A Rosato, PD Barker, AR Fersht
Biochemistry
(1999)
38
(doi: 10.1021/bi982785f)
Yusuf Hamied Department of Chemistry
Lensfield Road
Cambridge
CB2 1EW
T: +44 (0) 1223 336300
enquiries@ch.cam.ac.uk
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