研究领域

Biological

Our major research programme concerns the folding, stability and activity of proteins. We apply a broad multi-disciplinary approach that combines methods and ideas of molecular biology and physical-organic chemistry. We use techniques including protein engineering, DNA cloning, sequencing and mutagenesis, cell culture, gene and peptide synthesis, spectroscopy, rapid reaction techniques, multi-dimensional NMR (we have a 500, 600, 700 and an 800 MHz spectrometers) and x-ray protein crystallography. Current major projects include: protein folding, misfolding and disease; drug discovery; and structure-activity relationships of proteins involved in cancer and disease. Although now emeritus, I am still fully active in research with long term funding, including an MRC Programme Grant.

近期论文

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Mechanism of initiation of aggregation of p53 revealed by Φ-value analysis G Wang, AR Fersht – Proceedings of the National Academy of Sciences of the United States of America (2015) 112, 201500243 (DOI: 10.1073/pnas.1500243112) Propagation of aggregated p53: Cross-reaction and coaggregation vs. seeding. G Wang, AR Fersht – Proceedings of the National Academy of Sciences of the United States of America (2015) 112, 201500262 (DOI: 10.1073/pnas.1500262112) Profile of Martin Karplus, Michael Levitt, and Arieh Warshel, 2013 nobel laureates in chemistry. AR Fersht – Proceedings of the National Academy of Sciences of the United States of America (2013) 110, 19656 (DOI: 10.1073/pnas.1320569110) MDMX contains an autoinhibitory sequence element. M Bista, M Petrovich, AR Fersht – Proceedings of the National Academy of Sciences of the United States of America (2013) 110, 17814 (DOI: 10.1073/pnas.1317398110) Small molecule induced reactivation of mutant p53 in cancer cells. X Liu, R Wilcken, AC Joerger, IS Chuckowree, J Amin, J Spencer, AR Fersht – Nucleic acids research (2013) 41, 6034 (DOI: 10.1093/nar/gkt305) HEFLibs: Chemical probes for detecting halogen bonding in fragment-based lead discovery R Wilcken, AC Joerger, AR Fersht, FM Boeckler – ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY (2013) 245 Don't waste good methods on bad buffers and ambiguous data. F Huang, CM Johnson, M Petrovich, AR Fersht – Proceedings of the National Academy of Sciences of the United States of America (2013) 110, E331 (DOI: 10.1073/pnas.1217840110) 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 (2013) 52, 361 (DOI: 10.1002/anie.201203047) Reply to Campos and Munoz: Why phosphate is a bad buffer for guanidinium chloride titrations. AR Fersht, M Petrovich – Proceedings of the National Academy of Sciences of the United States of America (2013) 110, E1244 (DOI: 10.1073/pnas.1303286110) Evaluating Drosophila p53 as a model system for studying cancer mutations. G Herzog, AC Joerger, MD Shmueli, AR Fersht, E Gazit, D Segal – J Biol Chem (2012) 287, 44330 (DOI: 10.1074/jbc.m112.417980)Chemical physics of protein folding PG Wolynes, WA Eaton, AR Fersht – Proceedings of the National Academy of Sciences of the United States of America (2012) 109, 17770 (DOI: 10.1073/pnas.1215733109) Lithocholic acid is an endogenous inhibitor of MDM4 and MDM2 SM Vogel, MR Bauer, AC Joerger, R Wilcken, T Brandt, DB Veprintsev, TJ Rutherford, AR Fersht, FM Boeckler – Proceedings of the National Academy of Sciences of the United States of America (2012) 109, 16906 (DOI: 10.1073/pnas.1215060109) Domain-domain interactions in full-length p53 and a specific DNA complex probed by methyl NMR spectroscopy. M Bista, SM Freund, AR Fersht – Proceedings of the National Academy of Sciences of the United States of America (2012) 109, 15752 (DOI: 10.1073/pnas.1214176109) Sequence-dependent sliding kinetics of p53 JS Leith, A Tafvizi, F Huang, WE Uspal, PS Doyle, AR Fersht, LA Mirny, AM van Oijen – Proceedings of the National Academy of Sciences of the United States of America (2012) 109, 16552 (DOI: 10.1073/pnas.1120452109) First-order rate-determining aggregation mechanism of p53 and its implications. G Wang, AR Fersht – Proceedings of the National Academy of Sciences of the United States of America (2012) 109, 13590 (DOI: 10.1073/pnas.1211557109) Kinetic mechanism of p53 oncogenic mutant aggregation and its inhibition R Wilcken, G Wang, FM Boeckler, AR Fersht – Proceedings of the National Academy of Sciences of the United States of America (2012) 109, 13584 (DOI: 10.1073/pnas.1211550109) 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, 6810 (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 – Journal of the American Chemical Society (2012) 134, 1617 (DOI: 10.1021/ja2078619) Combining simulation and experiment to map protein folding AL Jonsson, AR Fersht, V Daggett – Comprehensive Biophysics (2012) 3, 1 (DOI: 10.1016/B978-0-12-374920-8.00301-5) Stability of p53 Homologs T Brandt, JL Kaar, AR Fersht, DB Veprintsev – PLoS One (2012) 7, e47889 (DOI: 10.1371/journal.pone.0047889)