Yusuf Hamied Department of Chemistry

Publications by Professor Sir Alan Fersht FRS

[Folding mechanism and folding rate].
T Ikura, AR Fersht
Protein (Tokyo)
(2001)
46
Experimental assignment of the structure of the transition state for the association of barnase and barstar11Edited by B. Honig
C Frisch, AR Fersht, G Schreiber
Journal of molecular biology
(2001)
308
(doi: 10.1006/jmbi.2001.4577)
Structure of the C-terminal sterile alpha-motif (SAM) domain of human p73 alpha.
WK Wang, M Bycroft, NW Foster, AM Buckle, AR Fersht, YW Chen
Acta Crystallographica Section D, Structural Biology
(2001)
57
(doi: 10.1107/S0907444901002529)
Protein folding from a highly disordered denatured state: The folding pathway of chymotrypsin inhibitor 2 at atomic resolution
SL Kazmirski, KB Wong, SM Freund, YJ Tan, AR Fersht, V Daggett
Proceedings of the National Academy of Sciences
(2001)
98
(doi: 10.1073/pnas.071054398)
Ligand-independent assembly of recombinant human CD1 by using oxidative refolding chromatography.
MM Altamirano, A Woolfson, A Donda, A Shamshiev, L Briseño-Roa, NW Foster, DB Veprintsev, G De Libero, AR Fersht, C Milstein
Proc Natl Acad Sci U S A
(2001)
98
(doi: 10.1073/pnas.041596598)
The Binding of Bis-ANS to the Isolated GroEL Apical Domain Fragment Induces the Formation of a Folding Intermediate with Increased Hydrophobic Surface Not Observed in Tetradecameric GroEL
AL Smoot, M Panda, BT Brazil, AM Buckle, AR Fersht, PM Horowitz
Biochemistry
(2001)
40
(doi: 10.1021/bi001822b)
Preface
CM Dobson, R John Ellis, AR Fersht
Philosophical Transactions of the Royal Society B Biological Sciences
(2001)
356
(doi: 10.1098/rstb.2000.0757)
Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation (vol 97, pg 13518, 2000)
U Mayor, CM Johnson, V Daggett, AR Fersht
P NATL ACAD SCI USA
(2001)
98
Structure on the move
WA Hendrickson, C-I Brändén, AR Fersht
Structure
(2001)
9
(doi: 10.1016/s0969-2126(00)00562-1)
From minichaperone to GroEL 3: Properties of an active single-ring mutant of GroEL
J Chatellier, F Hill, NW Foster, P Goloubinoff, AR Fersht
Journal of molecular biology
(2000)
304
(doi: 10.1006/jmbi.2000.4278)
From minichaperone to GroEL 2: Importance of avidity of the multisite ring structure
J Chatellier, F Hill, AR Fersht
Journal of molecular biology
(2000)
304
(doi: 10.1006/jmbi.2000.4277)
From Minichaperone to GroEL 1: Information on GroEL-Polypeptide Interactions from Crystal Packing of Minichaperones†
Q Wang, AM Buckle, AR Fersht
Journal of molecular biology
(2000)
304
(doi: 10.1006/jmbi.2000.4276)
A kinetically significant intermediate in the folding of barnase.
AR Fersht
Proceedings of the National Academy of Sciences of the United States of America
(2000)
97
(doi: 10.1073/pnas.260502597)
Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation
U Mayor, CM Johnson, V Daggett, AR Fersht
Proc Natl Acad Sci U S A
(2000)
97
(doi: 10.1073/pnas.250473497)
Biophysical characterization of elongin C from Saccharomyces cerevisiae (vol 39, pg 11137, 2000)
A Buchberger, MJ Howard, SMV Freund, M Proctor, PJG Butler, AR Fersht, M Bycroft
BIOCHEMISTRY
(2000)
39
(doi: 10.1021/bi005115u)
The deleterious effect of polyglutamine aggregation in cell models of Huntington's disease.
DC Rubinsztein, J Carmichael, J Rankin, J Chatellier, A Woolfson, A Wyttenbach, C Milstein, AR Fersht
AMERICAN JOURNAL OF HUMAN GENETICS
(2000)
67
Elucidating the mechanism of familial amyloidosis-Finnish type: NMR studies of human gelsolin domain 2
SL Kazmirski, MJ Howard, RL Isaacson, AR Fersht
Proceedings of the National Academy of Sciences of the United States of America
(2000)
97
(doi: 10.1073/pnas.180310097)
Conversion of two-state to multi-state folding kinetics on fusion of two protein foldons11Edited by J. Karn
K Inaba, N Kobayashi, AR Fersht
Journal of Molecular Biology
(2000)
302
(doi: 10.1006/jmbi.2000.4024)
Biophysical characterization of elongin C from Saccharomyces cerevisiae.
A Buchberger, MJ Howard, SM Freund, M Proctor, PJ Butler, AR Fersht, M Bycroft
Biochemistry
(2000)
39
(doi: 10.1021/bi0008231)
Bacterial and yeast chaperones reduce both aggregate formation and cell death in mammalian cell models of Huntington's disease.
J Carmichael, J Chatellier, A Woolfson, C Milstein, AR Fersht, DC Rubinsztein
Proceedings of the National Academy of Sciences of the United States of America
(2000)
97
(doi: 10.1073/pnas.170280697)
Yusuf Hamied Department of Chemistry
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