Yusuf Hamied Department of Chemistry

Publications by Professor Sir Alan Fersht FRS

Intrinsically disordered p53 and its complexes populate compact conformations in the gas phase.
K Pagel, E Natan, Z Hall, AR Fersht, CV Robinson
Angew Chem Int Ed Engl
(2012)
52
(doi: 10.1002/anie.201203047)
Halogen-Enriched Fragment Libraries as Leads for Drug Rescue of Mutant p53
R Wilcken, X Liu, MO Zimmermann, TJ Rutherford, AR Fersht, AC Joerger, FM Boeckler
Journal of the American Chemical Society
(2012)
134
(doi: 10.1021/ja301056a)
Long-Range Modulation of Chain Motions within the Intrinsically Disordered Transactivation Domain of Tumor Suppressor p53
JK Lum, H Neuweiler, AR Fersht
J Am Chem Soc
(2012)
134
(doi: 10.1021/ja2078619)
Nonnative Interactions in the FF Domain Folding Pathway from an Atomic Resolution Structure of a Sparsely Populated Intermediate: An NMR Relaxation Dispersion Study
DM Korzhnev, RM Vernon, TL Religa, AL Hansen, D Baker, AR Fersht, LE Kay
J Am Chem Soc
(2011)
133
(doi: 10.1021/ja203686t)
Combination of Markov State Models and Kinetic Networks for the Analysis of Molecular Dynamics Simulations of Peptide Folding
IH Radford, AR Fersht, G Settanni
The Journal of Physical Chemistry B
(2011)
115
(doi: 10.1021/jp112158w)
Acetylation of lysine 120 of p53 endows DNA-binding specificity at effective physiological salt concentration
E Arbely, E Natan, T Brandt, MD Allen, DB Veprintsev, CV Robinson, JW Chin, AC Joerger, AR Fersht
Proceedings of the National Academy of Sciences
(2011)
108
(doi: 10.1073/pnas.1105028108)
Electrocatalytic Monitoring of Metal Binding and Mutation-Induced Conformational Changes in p53 at Picomole Level
E Paleček, V Ostatná, H Černocká, AC Joerger, AR Fersht
J Am Chem Soc
(2011)
133
(doi: 10.1021/ja201006s)
Interaction of the p53 DNA-binding domain with its n-terminal extension modulates the stability of the p53 tetramer.
E Natan, C Baloglu, K Pagel, SMV Freund, N Morgner, CV Robinson, AR Fersht, AC Joerger
Journal of molecular biology
(2011)
409
(doi: 10.1016/j.jmb.2011.03.047)
Malleability of folding intermediates in the homeodomain superfamily.
W Banachewicz, TL Religa, RD Schaeffer, V Daggett, AR Fersht
Proc Natl Acad Sci U S A
(2011)
108
(doi: 10.1073/pnas.1101752108)
Φ‐Value Analysis of Protein Folding Transition States
N Ferguson, AR Fersht
(2011)
1
(doi: 10.1002/9783527634026.ch4)
Electron microscopy studies on the quaternary structure of p53 reveal different binding modes for p53 tetramers in complex with DNA
NA Drake, RM Blench, SJ Armitage, CS Bristow, KH White
Proc Natl Acad Sci U S A
(2010)
108
(doi: 10.1073/pnas.1012231108)
Folding of the Pit1 homeodomain near the speed limit
W Banachewicz, CM Johnson, AR Fersht
Proceedings of the National Academy of Sciences
(2010)
108
(doi: 10.1073/pnas.1017832108)
Electron microscopy studies on the quaternary structure of p53 reveal different binding modes for p53 tetramers in complex with DNA.
R Melero, S Rajagopalan, M Lázaro, AC Joerger, T Brandt, DB Veprintsev, G Lasso, D Gil, SHW Scheres, JM Carazo, AR Fersht, M Valle
Proc Natl Acad Sci U S A
(2010)
108
(doi: 10.1073/pnas.1015520107)
A single-molecule characterization of p53 search on DNA.
A Tafvizi, F Huang, AR Fersht, LA Mirny, AM van Oijen
Proc Natl Acad Sci U S A
(2010)
108
(doi: 10.1073/pnas.1016020107)
Time-resolved small-angle X-ray scattering study of the folding dynamics of barnase.
T Konuma, T Kimura, S Matsumoto, Y Goto, T Fujisawa, AR Fersht, S Takahashi
J Mol Biol
(2010)
405
(doi: 10.1016/j.jmb.2010.11.052)
Kinetics of chain motions within a protein-folding intermediate
H Neuweiler, W Banachewicz, AR Fersht
Proceedings of the National Academy of Sciences
(2010)
107
(doi: 10.1073/pnas.1011666107)
Stabilization of mutant p53 via alkylation of cysteines and effects on DNA binding
JL Kaar, N Basse, AC Joerger, E Stephens, TJ Rutherford, AR Fersht
Protein Sci
(2010)
19
(doi: 10.1002/pro.507)
Single-molecule characterization of oligomerization kinetics and equilibria of the tumor suppressor p53
S Rajagopalan, F Huang, AR Fersht
Nucleic Acids Research
(2010)
39
(doi: 10.1093/nar/gkq800)
Phosphotriesterase variants with high methylphosphonatase activity and strong negative trade-off against phosphotriesters
L Briseño-Roa, CM Timperley, AD Griffiths, AR Fersht
Protein Eng Des Sel
(2010)
24
(doi: 10.1093/protein/gzq076)
Carboxyl pKa Values and Acid Denaturation of BBL
E Arbely, TJ Rutherford, H Neuweiler, TD Sharpe, N Ferguson, AR Fersht
J Mol Biol
(2010)
403
(doi: 10.1016/j.jmb.2010.08.052)
Yusuf Hamied Department of Chemistry
Lensfield Road
Cambridge
CB2 1EW
T: +44 (0) 1223 336300
enquiries@ch.cam.ac.uk
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