Alan Roy Fersht - Publications

Affiliations: 
Chemistry University of Cambridge, Cambridge, England, United Kingdom 
Area:
protein engineering, protein folding, and enzyme catalysis
Website:
http://www.ch.cam.ac.uk/person/arf25

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Year Citation  Score
2021 Biancalana M, Natan E, Lenardo MJ, Fersht AR. NF-κB Rel Subunit Exchange on a Physiological Timescale. Protein Science : a Publication of the Protein Society. PMID 34089216 DOI: 10.1002/pro.4134  1
2021 Fersht AR. AlphaFold - A personal perspective on the impact of Machine Learning. Journal of Molecular Biology. 167088. PMID 34087198 DOI: 10.1016/j.jmb.2021.167088  0.01
2020 Bauer MR, Krämer A, Settanni G, Jones RN, Ni X, Khan Tareque R, Fersht AR, Spencer J, Joerger AC. Targeting cavity-creating p53 cancer mutations with small-molecule stabilizers: the Y220X paradigm. Acs Chemical Biology. PMID 31990523 DOI: 10.1021/acschembio.9b00748  1
2019 Fersht AR, Gölitz P, Lehn JM. ChemBioChem@20-Some Reflections. Chembiochem : a European Journal of Chemical Biology. PMID 31769931 DOI: 10.1002/Cbic.201900658  1
2019 Bauer MR, Jones RN, Tareque RK, Springett B, Dingler FA, Verduci L, Patel KJ, Fersht AR, Joerger AC, Spencer J. A structure-guided molecular chaperone approach for restoring the transcriptional activity of the p53 cancer mutant Y220C. Future Medicinal Chemistry. 11: 2491-2504. PMID 31633398 DOI: 10.4155/fmc-2019-0181  1
2019 Gomes S, Bosco B, Loureiro JB, Ramos H, Raimundo L, Soares J, Nazareth N, Barcherini V, Domingues L, Oliveira C, Bisio A, Piazza S, Bauer MR, Brás JP, Almeida MI, ... ... Fersht AR, et al. SLMP53-2 Restores Wild-Type-Like Function to Mutant p53 through Hsp70: Promising Activity in Hepatocellular Carcinoma. Cancers. 11. PMID 31405179 DOI: 10.3390/cancers11081151  1
2019 Fersht AR, Cohen FE. Folding & Design: introduction to a new journal. Folding & Design. 1: i. PMID 9162133 DOI: 10.1016/S1359-0278(96)00001-6  0.08
2018 Baud MGJ, Bauer MR, Verduci L, Dingler FA, Patel KJ, Horil Roy D, Joerger AC, Fersht AR. Aminobenzothiazole derivatives stabilize the thermolabile p53 cancer mutant Y220C and show anticancer activity in p53-Y220C cell lines. European Journal of Medicinal Chemistry. 152: 101-114. PMID 29702446 DOI: 10.1016/j.ejmech.2018.04.035  1
2018 Madan E, Parker TM, Bauer MR, Dhiman A, Pelham CJ, Nagane M, Kuppusamy ML, Holmes M, Holmes TR, Shaik K, Shee K, Kiparoidze S, Smith SD, Park YA, Gomm J, ... ... Fersht AR, et al. The curcumin analog HO-3867 selectively kills cancer cells by converting mutant p53 protein to transcriptionally active wildtype p53. The Journal of Biological Chemistry. PMID 29382728 DOI: 10.1074/jbc.RA117.000950  1
2017 Synnott NC, Bauer MR, Madden S, Murray A, Klinger R, O'Donovan N, O'Connor D, Gallagher WM, Crown J, Fersht AR, Duffy MJ. Mutant p53 as A Therapeutic Target for the Treatment of Triple-Negative Breast Cancer: Preclinical Investigation with the Anti-p53 Drug, PK11007. Cancer Letters. PMID 29069577 DOI: 10.1016/j.canlet.2017.09.053  1
2017 Baretić D, Pollard HK, Fisher DI, Johnson CM, Santhanam B, Truman CM, Kouba T, Fersht AR, Phillips C, Williams RL. Structures of closed and open conformations of dimeric human ATM. Science Advances. 3: e1700933. PMID 28508083 DOI: 10.1126/Sciadv.1700933  1
2017 Wang G, Fersht AR. Multisite aggregation of p53 and implications for drug rescue. Proceedings of the National Academy of Sciences of the United States of America. PMID 28292898 DOI: 10.1073/pnas.1700308114  1
2016 Martin TG, Bharat TA, Joerger AC, Bai XC, Praetorius F, Fersht AR, Dietz H, Scheres SH. Design of a molecular support for cryo-EM structure determination. Proceedings of the National Academy of Sciences of the United States of America. PMID 27821763 DOI: 10.1073/Pnas.1612720113  1
2016 Bauer MR, Joerger AC, Fersht AR. 2-Sulfonylpyrimidines: Mild alkylating agents with anticancer activity toward p53-compromised cells. Proceedings of the National Academy of Sciences of the United States of America. PMID 27551077 DOI: 10.1073/pnas.1610421113  1
2016 Bromley D, Bauer MR, Fersht AR, Daggett V. An in silico algorithm for identifying stabilizing pockets in proteins: test case, the Y220C mutant of the p53 tumor suppressor protein. Protein Engineering, Design & Selection : Peds. PMID 27503952 DOI: 10.1093/Protein/Gzw035  1
2016 Bauer MR, Jones RN, Baud MG, Wilcken R, Boeckler FM, Fersht AR, Joerger AC, Spencer J. Harnessing fluorine-sulfur contacts and multipolar interactions for the design of p53 mutant Y220C rescue drugs. Acs Chemical Biology. PMID 27267810 DOI: 10.1021/Acschembio.6B00315  0.28
2016 Joerger AC, Fersht AR. The p53 Pathway: Origins, Inactivation in Cancer, and Emerging Therapeutic Approaches. Annual Review of Biochemistry. PMID 27145840 DOI: 10.1146/annurev-biochem-060815-014710  1
2015 Joerger AC, Bauer MR, Wilcken R, Baud MG, Harbrecht H, Exner TE, Boeckler FM, Spencer J, Fersht AR. Exploiting Transient Protein States for the Design of Small-Molecule Stabilizers of Mutant p53. Structure (London, England : 1993). 23: 2246-55. PMID 26636255 DOI: 10.1016/J.Str.2015.10.016  1
2015 Wilcken R, Zimmermann MO, Bauer MR, Rutherford TJ, Fersht AR, Joerger AC, Boeckler FM. Experimental and theoretical evaluation of the ethynyl moiety as a halogen bioisostere. Acs Chemical Biology. PMID 26378745 DOI: 10.1021/Acschembio.5B00515  1
2015 González-Arzola K, Díaz-Moreno I, Cano-González A, Díaz-Quintana A, Velázquez-Campoy A, Moreno-Beltrán B, López-Rivas A, De la Rosa MA. Structural basis for inhibition of the histone chaperone activity of SET/TAF-Iβ by cytochrome c. Proceedings of the National Academy of Sciences of the United States of America. 112: 9908-13. PMID 26216969 DOI: 10.1073/pnas.1508040112  1
2015 Nasedkin A, Marcellini M, Religa TL, Freund SM, Menzel A, Fersht AR, Jemth P, van der Spoel D, Davidsson J. Deconvoluting Protein (Un)folding Structural Ensembles Using X-Ray Scattering, Nuclear Magnetic Resonance Spectroscopy and Molecular Dynamics Simulation. Plos One. 10: e0125662. PMID 25946337 DOI: 10.1371/journal.pone.0125662  1
2015 Wang G, Fersht AR. Propagation of aggregated p53: Cross-reaction and coaggregation vs. seeding. Proceedings of the National Academy of Sciences of the United States of America. 112: 2443-8. PMID 25675527 DOI: 10.1073/pnas.1500262112  1
2015 Wang G, Fersht AR. Mechanism of initiation of aggregation of p53 revealed by Φ-value analysis. Proceedings of the National Academy of Sciences of the United States of America. 112: 2437-42. PMID 25675526 DOI: 10.1073/pnas.1500243112  1
2015 Nasedkin A, Marcellini M, Religa TL, Freund SM, Menzel A, Fersht AR, Jemth P, Van Der Spoel D, Davidsson J. Deconvoluting protein (un)folding structural ensembles using X-ray scattering, nuclear magnetic resonance spectroscopy and molecular dynamics simulation Plos One. 10. DOI: 10.1371/journal.pone.0125662  1
2015 Wang G, Fersht AR. Propagation of aggregated p53: Cross-reaction and coaggregation vs. seeding Proceedings of the National Academy of Sciences of the United States of America. 112: 2443-2448. DOI: 10.1073/pnas.1500262112  1
2015 Wang G, Fersht AR. Mechanism of initiation of aggregation of p53 revealed by Φ-value analysis Proceedings of the National Academy of Sciences of the United States of America. 112: 2437-2442. DOI: 10.1073/pnas.1500243112  1
2014 Towse CL, Hopping G, Vulovic I, Daggett V. Nature versus design: the conformational propensities of D-amino acids and the importance of side chain chirality. Protein Engineering, Design & Selection : Peds. 27: 447-55. PMID 25233851 DOI: 10.1093/Protein/Gzu037  1
2013 Fersht AR. Profile of Martin Karplus, Michael Levitt, and Arieh Warshel, 2013 nobel laureates in chemistry. Proceedings of the National Academy of Sciences of the United States of America. 110: 19656-19657. PMID 24277833  1
2013 Bista M, Petrovich M, Fersht AR. MDMX contains an autoinhibitory sequence element Proceedings of the National Academy of Sciences of the United States of America. 110: 17814-17819. PMID 24127580 DOI: 10.1073/pnas.1317398110  1
2013 Fersht AR, Petrovich M. Reply to Campos and Muñoz: Why phosphate is a bad buffer for guanidinium chloride titrations Proceedings of the National Academy of Sciences of the United States of America. 110: E1244-E1245. PMID 23675589 DOI: 10.1073/pnas.1303286110  1
2013 Liu X, Wilcken R, Joerger AC, Chuckowree IS, Amin J, Spencer J, Fersht AR. Small molecule induced reactivation of mutant p53 in cancer cells Nucleic Acids Research. 41: 6034-6044. PMID 23630318 DOI: 10.1093/nar/gkt305  1
2013 Huang F, Johnson CM, Petrovich M, Fersht AR. Don't waste good methods on bad buffers and ambiguous data Proceedings of the National Academy of Sciences of the United States of America. 110: E331-E332. PMID 23329326 DOI: 10.1073/Pnas.1217840110  1
2013 Pagel K, Natan E, Hall Z, Fersht AR, Robinson CV. Intrinsically disordered p53 and its complexes populate compact conformations in the gas phase. Angewandte Chemie (International Ed. in English). 52: 361-5. PMID 22777995 DOI: 10.1002/anie.201203047  1
2012 Herzog G, Joerger AC, Shmueli MD, Fersht AR, Gazit E, Segal D. Evaluating Drosophila p53 as a model system for studying cancer mutations. The Journal of Biological Chemistry. 287: 44330-7. PMID 23135266 DOI: 10.1074/Jbc.M112.417980  1
2012 Brandt T, Kaar JL, Fersht AR, Veprintsev DB. Stability of p53 Homologs Plos One. 7. PMID 23112865 DOI: 10.1371/journal.pone.0047889  1
2012 Wolynes PG, Eaton WA, Fersht AR. Chemical physics of protein folding. Proceedings of the National Academy of Sciences of the United States of America. 109: 17770-1. PMID 23112193 DOI: 10.1073/Pnas.1215733109  1
2012 Vogel SM, Bauer MR, Joerger AC, Wilcken R, Brandt T, Veprintsev DB, Rutherford TJ, Fersht AR, Boeckler FM. Lithocholic acid is an endogenous inhibitor of MDM4 and MDM2 Proceedings of the National Academy of Sciences of the United States of America. 109: 16906-16910. PMID 23035244 DOI: 10.1073/Pnas.1215060109  1
2012 Leith JS, Tafvizi A, Huang F, Uspal WE, Doyle PS, Fersht AR, Mirny LA, van Oijen AM. Sequence-dependent sliding kinetics of p53. Proceedings of the National Academy of Sciences of the United States of America. 109: 16552-7. PMID 23012405 DOI: 10.1073/Pnas.1120452109  1
2012 Bista M, Freund SM, Fersht AR. Domain-domain interactions in full-length p53 and a specific DNA complex probed by methyl NMR spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. 109: 15752-6. PMID 22972749 DOI: 10.1073/pnas.1214176109  1
2012 Markley JL, Akutsu H, Asakura T, Baldus M, Boelens R, Bonvin A, Kaptein R, Bax A, Bezsonova I, Gryk MR, Hoch JC, Korzhnev DM, Maciejewski MW, Case D, Chazin WJ, ... ... Fersht A, et al. In support of the BMRB. Nature Structural & Molecular Biology. 19: 854-60. PMID 22955930 DOI: 10.1038/Nsmb.2371  1
2012 Wilcken R, Wang G, Boeckler FM, Fersht AR. Kinetic mechanism of p53 oncogenic mutant aggregation and its inhibition Proceedings of the National Academy of Sciences of the United States of America. 109: 13584-13589. PMID 22869713 DOI: 10.1073/Pnas.1211550109  1
2012 Wang G, Fersht AR. First-order rate-determining aggregation mechanism of p53 and its implications Proceedings of the National Academy of Sciences of the United States of America. 109: 13590-13595. PMID 22869710 DOI: 10.1073/pnas.1211557109  1
2012 Wilcken R, Liu X, Zimmermann MO, Rutherford TJ, Fersht AR, Joerger AC, Boeckler FM. Halogen-enriched fragment libraries as leads for drug rescue of mutant p53 Journal of the American Chemical Society. 134: 6810-6818. PMID 22439615 DOI: 10.1021/Ja301056A  1
2012 Lum JK, Neuweiler H, Fersht AR. Long-range modulation of chain motions within the intrinsically disordered transactivation domain of tumor suppressor p53 Journal of the American Chemical Society. 134: 1617-1622. PMID 22176582 DOI: 10.1021/ja2078619  1
2012 Jonsson AL, Fersht AR, Daggett V. Combining simulation and experiment to map protein folding Comprehensive Biophysics. 3: 1-18. DOI: 10.1016/B978-0-12-374920-8.00301-5  1
2011 Korzhnev DM, Vernon RM, Religa TL, Hansen AL, Baker D, Fersht AR, Kay LE. Nonnative interactions in the FF domain folding pathway from an atomic resolution structure of a sparsely populated intermediate: an NMR relaxation dispersion study. Journal of the American Chemical Society. 133: 10974-82. PMID 21639149 DOI: 10.1021/Ja203686T  1
2011 Radford IH, Fersht AR, Settanni G. Combination of Markov state models and kinetic networks for the analysis of molecular dynamics simulations of peptide folding. The Journal of Physical Chemistry. B. 115: 7459-71. PMID 21553833 DOI: 10.1021/Jp112158W  1
2011 Arbely E, Natan E, Brandt T, Allen MD, Veprintsev DB, Robinson CV, Chin JW, Joerger AC, Fersht AR. Acetylation of lysine 120 of p53 endows DNA-binding specificity at effective physiological salt concentration. Proceedings of the National Academy of Sciences of the United States of America. 108: 8251-6. PMID 21525412 DOI: 10.1073/Pnas.1105028108  1
2011 Paleček E, Ostatná V, Černocká H, Joerger AC, Fersht AR. Electrocatalytic monitoring of metal binding and mutation-induced conformational changes in p53 at picomole level Journal of the American Chemical Society. 133: 7190-7196. PMID 21491862 DOI: 10.1021/Ja201006S  1
2011 Natan E, Baloglu C, Pagel K, Freund SM, Morgner N, Robinson CV, Fersht AR, Joerger AC. Interaction of the p53 DNA-binding domain with its n-terminal extension modulates the stability of the p53 tetramer. Journal of Molecular Biology. 409: 358-68. PMID 21457718 DOI: 10.1016/j.jmb.2011.03.047  1
2011 Banachewicz W, Religa TL, Schaeffer RD, Daggett V, Fersht AR. Malleability of folding intermediates in the homeodomain superfamily Proceedings of the National Academy of Sciences of the United States of America. 108: 5596-5601. PMID 21422286 DOI: 10.1073/Pnas.1101752108  1
2011 Banachewicz W, Johnson CM, Fersht AR. Folding of the Pit1 homeodomain near the speed limit Proceedings of the National Academy of Sciences of the United States of America. 108: 569-573. PMID 21187427 DOI: 10.1073/Pnas.1017832108  1
2011 Melero R, Rajagopalan S, Lázaro M, Joerger AC, Brandt T, Veprintsev DB, Lasso G, Gil D, Scheres SH, Carazo JM, Fersht AR, Valle M. Electron microscopy studies on the quaternary structure of p53 reveal different binding modes for p53 tetramers in complex with DNA. Proceedings of the National Academy of Sciences of the United States of America. 108: 557-62. PMID 21178074 DOI: 10.1073/Pnas.1015520107  1
2011 Tafvizi A, Huang F, Fersht AR, Mirny LA, van Oijen AM. A single-molecule characterization of p53 search on DNA. Proceedings of the National Academy of Sciences of the United States of America. 108: 563-8. PMID 21178072 DOI: 10.1073/Pnas.1016020107  1
2011 Konuma T, Kimura T, Matsumoto S, Goto Y, Fujisawa T, Fersht AR, Takahashi S. Time-resolved small-angle X-ray scattering study of the folding dynamics of barnase Journal of Molecular Biology. 405: 1284-1294. PMID 21146541 DOI: 10.1016/J.Jmb.2010.11.052  1
2011 Rajagopalan S, Huang F, Fersht AR. Single-molecule characterization of oligomerization kinetics and equilibria of the tumor suppressor p53 Nucleic Acids Research. 39: 2294-2303. PMID 21097469 DOI: 10.1093/Nar/Gkq800  1
2011 Briseño-Roa L, Timperley CM, Griffiths AD, Fersht AR. Phosphotriesterase variants with high methylphosphonatase activity and strong negative trade-off against phosphotriesters. Protein Engineering, Design & Selection : Peds. 24: 151-9. PMID 21037279 DOI: 10.1093/Protein/Gzq076  1
2011 Briseño-Roa L, Oliynyk Z, Timperley CM, Griffiths AD, Fersht AR. Highest paraoxonase turnover rate found in a bacterial phosphotriesterase variant. Protein Engineering, Design & Selection : Peds. 24: 209-11. PMID 20650962 DOI: 10.1093/Protein/Gzq046  1
2011 Wong T, Rutherford T, Freund S, Fersht A. backbone resonance assignments of p53 N-terminal transactivation domain (1-93) Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr17760  1
2011 Melero R, Rajagopalan S, Lázaro M, Joerger AC, Brandt T, Veprintsev DB, Lasso G, Gil D, Scheres SHW, Carazo JM, Fersht AR, Valle M. Electron microscopy studies on the quaternary structure of p53 reveal different binding modes for p53 tetramers in complex with DNA Proceedings of the National Academy of Sciences of the United States of America. 108: 458-462. DOI: 10.1073/pnas.1012231108  1
2011 Radford IH, Fersht AR, Settanni G. Combination of Markov state models and kinetic networks for the analysis of molecular dynamics simulations of peptide folding Journal of Physical Chemistry B. 115: 7459-7471. DOI: 10.1021/jp112158w  1
2011 Ferguson N, Fersht AR. φ- Value Analysis of Protein Folding Transition States Protein Engineering Handbook, Volume 1 & Volume 2. 1: 81-120. DOI: 10.1002/9783527634026.ch4  1
2010 Neuweiler H, Banachewicz W, Fersht AR. Kinetics of chain motions within a protein-folding intermediate Proceedings of the National Academy of Sciences of the United States of America. 107: 22106-22110. PMID 21135210 DOI: 10.1073/Pnas.1011666107  1
2010 Kaar JL, Basse N, Joerger AC, Stephens E, Rutherford TJ, Fersht AR. Stabilization of mutant p53 via alkylation of cysteines and effects on DNA binding Protein Science. 19: 2267-2278. PMID 20878668 DOI: 10.1002/Pro.507  1
2010 Korzhnev DM, Religa TL, Banachewicz W, Fersht AR, Kay LE. A transient and low-populated protein-folding intermediate at atomic resolution. Science (New York, N.Y.). 329: 1312-6. PMID 20829478 DOI: 10.1126/Science.1191723  1
2010 Arbely E, Rutherford TJ, Neuweiler H, Sharpe TD, Ferguson N, Fersht AR. Carboxyl pK(a) values and acid denaturation of BBL. Journal of Molecular Biology. 403: 313-27. PMID 20816989 DOI: 10.1016/J.Jmb.2010.08.052  1
2010 McCully ME, Beck DAC, Fersht AR, Daggett V. Refolding the engrailed homeodomain: Structural basis for the accumulation of a folding intermediate Biophysical Journal. 99: 1628-1636. PMID 20816076 DOI: 10.1016/J.Bpj.2010.06.040  1
2010 Arbely E, Neuweiler H, Sharpe TD, Johnson CM, Fersht AR. The human peripheral subunit-binding domain folds rapidly while overcoming repulsive Coulomb forces Protein Science. 19: 1704-1713. PMID 20662005 DOI: 10.1002/Pro.453  1
2010 van Dieck J, Lum JK, Teufel DP, Fersht AR. S100 proteins interact with the N-terminal domain of MDM2 Febs Letters. 584: 3269-3274. PMID 20591429 DOI: 10.1016/J.Febslet.2010.06.024  1
2010 Joerger AC, Fersht AR. The tumor suppressor p53: from structures to drug discovery. Cold Spring Harbor Perspectives in Biology. 2: a000919. PMID 20516128 DOI: 10.1101/Cshperspect.A000919  1
2010 Rajagopalan S, Andreeva A, Rutherford TJ, Fersht AR. Mapping the physical and functional interactions between the tumor suppressors p53 and BRCA2 Proceedings of the National Academy of Sciences of the United States of America. 107: 8587-8592. PMID 20421506 DOI: 10.1073/Pnas.1003689107  1
2010 Vasbinder JW, Andersson B, Arthur WB, Boasson M, de Boer R, Changeux JP, Domingo E, Eigen M, Fersht A, Frenkel D, Rees M, Groen T, Huber R, Hunt T, Holland J, et al. Transdisciplinary EU science institute needs funds urgently. Nature. 463: 876. PMID 20164899 DOI: 10.1038/463876A  1
2010 Basse N, Kaar JL, Settanni G, Joerger AC, Rutherford TJ, Fersht AR. Toward the Rational Design of p53-Stabilizing Drugs: Probing the Surface of the Oncogenic Y220C Mutant Chemistry and Biology. 17: 46-56. PMID 20142040 DOI: 10.1016/j.chembiol.2009.12.011  1
2010 Van Dieck J, Brandt T, Teufel DP, Veprintsev DB, Joerger AC, Fersht AR. Molecular basis of S100 proteins interacting with the p53 homologs p63 and p73 Oncogene. 29: 2024-2035. PMID 20140014 DOI: 10.1038/onc.2009.490  1
2010 Dodson CA, Ferguson N, Rutherford TJ, Johnson CM, Fersht AR. Engineering a two-helix bundle protein for folding studies. Protein Engineering, Design & Selection : Peds. 23: 357-64. PMID 20130106 DOI: 10.1093/Protein/Gzp080  1
2010 Burge SW, Natan E, Fersht AR. Competition and Complex Formation Between P53, Mdm2 and the P300 Zinc Finger CH3 Biophysical Journal. 98: 652a. DOI: 10.1016/J.Bpj.2009.12.3576  0.01
2009 Brown CJ, Lain S, Verma CS, Fersht AR, Lane DP. Awakening guardian angels: drugging the p53 pathway. Nature Reviews. Cancer. 9: 862-73. PMID 19935675 DOI: 10.1038/Nrc2763  1
2009 Huang F, Rajagopalan S, Settanni G, Marsh RJ, Armoogum DA, Nicolaou N, Bain AJ, Lerner E, Haas E, Ying L, Fersht AR. Multiple conformations of full-length p53 detected with single-molecule fluorescence resonance energy transfer Proceedings of the National Academy of Sciences of the United States of America. 106: 20758-20763. PMID 19933326 DOI: 10.1073/Pnas.0909644106  1
2009 Rajagopalan S, Sade RS, Townsley FM, Fersht AR. Mechanistic differences in the transcriptional activation of p53 by 14-3-3 isoforms Nucleic Acids Research. 38: 893-906. PMID 19933256 DOI: 10.1093/nar/gkp1041  1
2009 Neuweiler H, Johnson CM, Fersht AR. Direct observation of ultrafast folding and denatured state dynamics in single protein molecules Proceedings of the National Academy of Sciences of the United States of America. 106: 18569-18574. PMID 19841261 DOI: 10.1073/Pnas.0910860106  1
2009 van Dieck J, Teufel DP, Jaulent AM, Fernandez-Fernandez MR, Rutherford TJ, Wyslouch-Cieszynska A, Fersht AR. Posttranslational Modifications Affect the Interaction of S100 Proteins with Tumor Suppressor p53 Journal of Molecular Biology. 394: 922-930. PMID 19819244 DOI: 10.1016/j.jmb.2009.10.002  1
2009 Joerger AC, Rajagopalan S, Natan E, Veprintsev DB, Robinson CV, Fersht AR. Structural evolution of p53, p63, and p73: Implication for heterotetramer formation Proceedings of the National Academy of Sciences of the United States of America. 106: 17705-17710. PMID 19815500 DOI: 10.1073/pnas.0905867106  1
2009 Huang F, Ying L, Fersht AR. Direct observation of barrier-limited folding of BBL by single-molecule fluorescence resonance energy transfer Proceedings of the National Academy of Sciences of the United States of America. 106: 16239-16244. PMID 19805287 DOI: 10.1073/pnas.0909126106  1
2009 Wong TS, Rajagopalan S, Freund SM, Rutherford TJ, Andreeva A, Townsley FM, Petrovich M, Fersht AR. Biophysical characterizations of human mitochondrial transcription factor A and its binding to tumor suppressor p53. Nucleic Acids Research. 37: 6765-83. PMID 19755502 DOI: 10.1093/nar/gkp750  1
2009 Khoo KH, Mayer S, Fersht AR. Effects of stability on the biological function of p53. The Journal of Biological Chemistry. 284: 30974-80. PMID 19700401 DOI: 10.1074/jbc.M109.033183  1
2009 Khoo KH, Andreeva A, Fersht AR. Adaptive Evolution of p53 Thermodynamic Stability Journal of Molecular Biology. 393: 161-175. PMID 19683006 DOI: 10.1016/j.jmb.2009.08.013  1
2009 Natan E, Hirschberg D, Morgner N, Robinson CV, Fersht AR. Ultraslow oligomerization equilibria of p53 and its implications Proceedings of the National Academy of Sciences of the United States of America. 106: 14327-14332. PMID 19667193 DOI: 10.1073/pnas.0907840106  1
2009 Di Re M, Sembongi H, He J, Reyes A, Yasukawa T, Martinsson P, Bailey LJ, Goffart S, Boyd-kirkup JD, Wong TS, Fersht AR, Spelbrink JN, Holt IJ. The accessory subunit of mitochondrial DNA polymerase γ determines the DNA content of mitochondrial nucleoids in human cultured cells Nucleic Acids Research. 37: 5701-5713. PMID 19625489 DOI: 10.1093/Nar/Gkp614  1
2009 Rajagopalan S, Andreeva A, Teufel DP, Freund SM, Fersht AR. Interaction between the transactivation domain of p53 and PC4 exemplifies acidic activation domains as single-stranded DNA mimics. The Journal of Biological Chemistry. 284: 21728-37. PMID 19525231 DOI: 10.1074/jbc.M109.006429  1
2009 Khoo KH, Joerger AC, Freund SM, Fersht AR. Stabilising the DNA-binding domain of p53 by rational design of its hydrophobic core. Protein Engineering, Design & Selection : Peds. 22: 421-30. PMID 19515728 DOI: 10.1093/protein/gzp018  1
2009 Neuweiler H, Sharpe TD, Rutherford TJ, Johnson CM, Allen MD, Ferguson N, Fersht AR. The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family. Journal of Molecular Biology. 390: 1060-73. PMID 19445954 DOI: 10.1016/J.Jmb.2009.05.011  1
2009 Lambert JM, Gorzov P, Veprintsev DB, Söderqvist M, Segerbäck D, Bergman J, Fersht AR, Hainaut P, Wiman KG, Bykov VJ. PRIMA-1 reactivates mutant p53 by covalent binding to the core domain. Cancer Cell. 15: 376-88. PMID 19411067 DOI: 10.1016/j.ccr.2009.03.003  1
2009 Teufel DP, Bycroft M, Fersht AR. Regulation by phosphorylation of the relative affinities of the N-terminal transactivation domains of p53 for p300 domains and Mdm2 Oncogene. 28: 2112-2118. PMID 19363523 DOI: 10.1038/onc.2009.71  1
2009 van Dieck J, Fernandez-Fernandez MR, Veprintsev DB, Fersht AR. Modulation of the oligomerization state of p53 by differential binding of proteins of the S100 family to p53 monomers and tetramers Journal of Biological Chemistry. 284: 13804-13811. PMID 19297317 DOI: 10.1074/jbc.M901351200  1
2009 Huang F, Lerner E, Sato S, Amir D, Haas E, Fersht AR. Time-resolved fluorescence resonance energy transfer study shows a compact denatured state of the b domain of protein A Biochemistry. 48: 3468-3476. PMID 19222162 DOI: 10.1021/Bi801890W  1
2009 Burge S, Teufel DP, Townsley FM, Freund SM, Bycroft M, Fersht AR. Molecular basis of the interactions between the p73 N terminus and p300: effects on transactivation and modulation by phosphorylation. Proceedings of the National Academy of Sciences of the United States of America. 106: 3142-7. PMID 19218448 DOI: 10.1073/pnas.0900383106  1
2009 Settanni G, Fersht AR. Downhill versus Barrier-Limited Folding of BBL. 3. Heterogeneity of the Native State of the BBL Peripheral Subunit Binding Domain and Its Implications for Folding Mechanisms Journal of Molecular Biology. 387: 993-1001. PMID 19217911 DOI: 10.1016/j.jmb.2009.02.014  1
2009 Daggett V, Fersht AR. Protein folding and binding: moving into unchartered territory Current Opinion in Structural Biology. 19: 1-2. PMID 19217770 DOI: 10.1016/J.Sbi.2009.01.006  1
2009 Tidow H, Andreeva A, Rutherford TJ, Fersht AR. Solution Structure of the U11-48K CHHC Zinc-Finger Domain that Specifically Binds the 5′ Splice Site of U12-Type Introns Structure. 17: 294-302. PMID 19217400 DOI: 10.1016/J.Str.2008.11.013  1
2009 Neuweiler H, Sharpe TD, Johnson CM, Teufel DP, Ferguson N, Fersht AR. Downhill versus barrier-limited folding of BBL 2: mechanistic insights from kinetics of folding monitored by independent tryptophan probes. Journal of Molecular Biology. 387: 975-85. PMID 19136014 DOI: 10.1016/J.Jmb.2008.12.056  1
2009 Arbely E, Rutherford TJ, Sharpe TD, Ferguson N, Fersht AR. Downhill versus barrier-limited folding of BBL 1: energetic and structural perturbation effects upon protonation of a histidine of unusually low pKa. Journal of Molecular Biology. 387: 986-92. PMID 19136007 DOI: 10.1016/J.Jmb.2008.12.055  1
2009 Lehn JM, Fersht AR. Interfaces: two worlds unite. Chembiochem : a European Journal of Chemical Biology. 10: 4. PMID 19115277 DOI: 10.1002/Cbic.200800740  1
2009 Yu GW, Vaysburd M, Allen MD, Settanni G, Fersht AR. Structure of Human MDM4 N-Terminal Domain Bound to a Single-Domain Antibody Journal of Molecular Biology. 385: 1578-1589. PMID 19084022 DOI: 10.1016/j.jmb.2008.11.043  1
2009 Wong TS, Rajagopalan S, Townsley FM, Freund SM, Petrovich M, Loakes D, Fersht AR. Physical and functional interactions between human mitochondrial single-stranded DNA-binding protein and tumour suppressor p53. Nucleic Acids Research. 37: 568-81. PMID 19066201 DOI: 10.1093/nar/gkn974  1
2009 Fersht AR. Abstract IA-8: p53: From structure to drug discovery Cancer Research. 69. DOI: 10.1158/0008-5472.Fbcr09-Ia-8  0.01
2009 Huang F, Ying L, Neuweiler H, Fersht AR. Reply to Campos et al.: Direct observation versus ambiguous kinetics and thermodynamics Proceedings of the National Academy of Sciences of the United States of America. 106: e140. DOI: 10.1073/pnas.0913321107  1
2009 Fersht A. The most influential journals: Impact factor and eigenfactor Proceedings of the National Academy of Sciences of the United States of America. 106: 6883-6884. DOI: 10.1073/Pnas.0903307106  1
2009 Sharpe TD, Ferguson N, Johnson CM, Fersht AR. Corrigendum to "Conservation of Transition State Structure in Fast Folding Peripheral Subunit-Binding Domains" [J. Mol. Biol. 383 (2008) 224-237] (DOI:10.1016/j.jmb.2008.06.081) Journal of Molecular Biology. 387: 519. DOI: 10.1016/J.Jmb.2009.01.002  1
2009 Tafvizi A, Leith JS, Huang F, Fersht AR, Mirny L, van Oijen AM. Single-molecule Studies Of p53 Sliding Along DNA Biophysical Journal. 96: 417a. DOI: 10.1016/J.Bpj.2008.12.2128  0.04
2009 Leith JS, Tafvizi A, Huang F, Fersht AR, Mirny L, van Oijen AM. Sequence-Dependent Kinetics of One-Dimensional Diffusion of p53 on DNA Biophysical Journal. 96: 416a. DOI: 10.1016/J.Bpj.2008.12.2125  0.04
2008 Rajagopalan S, Jaulent AM, Wells M, Veprintsev DB, Fersht AR. 14-3-3 activation of DNA binding of p53 by enhancing its association into tetramers Nucleic Acids Research. 36: 5983-5991. PMID 18812399 DOI: 10.1093/nar/gkn598  1
2008 Fernandez-Fernandez MR, Rutherford TJ, Fersht AR. Members of the S100 family bind p53 in two distinct ways Protein Science. 17: 1663-1670. PMID 18694925 DOI: 10.1110/Ps.035527.108  1
2008 Boeckler FM, Joerger AC, Jaggi G, Rutherford TJ, Veprintsev DB, Fersht AR. Targeted rescue of a destabilized mutant of p53 by an in silico screened drug Proceedings of the National Academy of Sciences of the United States of America. 105: 10360-10365. PMID 18650397 DOI: 10.1073/Pnas.0805326105  1
2008 Becker J, Ferguson N, Flinders J, van Rossum BJ, Fersht AR, Oschkinat H. A sequential assignment procedure for proteins that have intermediate line widths in MAS NMR spectra: amyloid fibrils of human CA150.WW2. Chembiochem : a European Journal of Chemical Biology. 9: 1946-52. PMID 18642254 DOI: 10.1002/Cbic.200700706  1
2008 Sharpe TD, Ferguson N, Johnson CM, Fersht AR. Conservation of transition state structure in fast folding peripheral subunit-binding domains. Journal of Molecular Biology. 383: 224-37. PMID 18625240 DOI: 10.1016/J.Jmb.2008.06.081  1
2008 García-Alai MM, Tidow H, Natan E, Townsley FM, Veprintsev DB, Fersht AR. The novel p53 isoform "delta p53" is a misfolded protein and does not bind the p21 promoter site Protein Science. 17: 1671-1678. PMID 18621913 DOI: 10.1110/Ps.036996.108  1
2008 Fersht AR. From the first protein structures to our current knowledge of protein folding: Delights and scepticisms Nature Reviews Molecular Cell Biology. 9: 650-654. PMID 18578032 DOI: 10.1038/nrm2446  1
2008 Tafvizi A, Huang F, Leith JS, Fersht AR, Mirny LA, van Oijen AM. Tumor suppressor p53 slides on DNA with low friction and high stability. Biophysical Journal. 95: L01-3. PMID 18424488 DOI: 10.1529/Biophysj.108.134122  1
2008 Joerger AC, Fersht AR. Structural biology of the tumor suppressor p53. Annual Review of Biochemistry. 77: 557-82. PMID 18410249 DOI: 10.1146/annurev.biochem.77.060806.091238  1
2008 Wells M, Tidow H, Rutherford TJ, Markwick P, Jensen MR, Mylonas E, Svergun DI, Blackledge M, Fersht AR. Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain. Proceedings of the National Academy of Sciences of the United States of America. 105: 5762-7. PMID 18391200 DOI: 10.1073/pnas.0801353105  1
2008 Settanni G, Fersht AR. High temperature unfolding simulations of the TRPZ1 peptide Biophysical Journal. 94: 4444-4453. PMID 18281384 DOI: 10.1529/biophysj.107.122606  1
2008 Schaeffer RD, Fersht A, Daggett V. Combining experiment and simulation in protein folding: closing the gap for small model systems. Current Opinion in Structural Biology. 18: 4-9. PMID 18242977 DOI: 10.1016/J.Sbi.2007.11.007  1
2008 Jemth P, Johnson CM, Gianni S, Fersht AR. Demonstration by burst-phase analysis of a robust folding intermediate in the FF domain Protein Engineering, Design and Selection. 21: 207-214. PMID 18239073 DOI: 10.1093/Protein/Gzm091  1
2008 Veprintsev DB, Fersht AR. Algorithm for prediction of tumour suppressor p53 affinity for binding sites in DNA Nucleic Acids Research. 36: 1589-1598. PMID 18234719 DOI: 10.1093/nar/gkm1040  1
2008 Huang F, Settanni G, Fersht AR. Fluorescence resonance energy transfer analysis of the folding pathway of Engrailed Homeodomain Protein Engineering, Design and Selection. 21: 131-146. PMID 18204045 DOI: 10.1093/protein/gzm069  1
2008 Fernandez-Fernandez MR, Fersht AR. S100B (S100 calcium binding protein B) Atlas of Genetics and Cytogenetics in Oncology and Haematology. DOI: 10.4267/2042/16956  1
2008 Joerger AC, Fersht AR. Structural biology of the tumor suppressor p53 Annual Review of Biochemistry. 77: 557-582. DOI: 10.1146/annurev.biochem.77.060806.091238  1
2008 Daggett V, Fersht A. Message from the Editors Protein Engineering, Design and Selection. 21: 129. DOI: 10.1093/protein/gzn008  1
2008 Guydosh NR, Fersht AR. A Guide to Measuring and Interpreting Φ-values Protein Folding Handbook. 1: 445-453. DOI: 10.1002/9783527619498.ch13  1
2008 Fersht AR, Winter GP. Redesigning Enzymes by Site-Directed Mutagenesis Enzymes in Organic Synthesis. 204-218. DOI: 10.1002/9780470720929.ch14  1
2008 Boeckler F, Joerger A, Jaggi G, Rutherford T, Veprintsev D, Fersht A. Targeted rescue of a destabilized mutant of p53 by ar in silico screened drug Chemtracts. 21: 236-237.  1
2007 Sharpe T, Jonsson AL, Rutherford TJ, Daggett V, Fersht AR. The role of the turn in β-hairpin formation during WW domain folding Protein Science. 16: 2233-2239. PMID 17766370 DOI: 10.1110/Ps.073004907  1
2007 Sot B, Freund SM, Fersht AR. Comparative biophysical characterization of p53 with the pro-apoptotic BAK and the anti-apoptotic BCL-xL. The Journal of Biological Chemistry. 282: 29193-200. PMID 17699158 DOI: 10.1074/jbc.M705544200  1
2007 Korzhnev DM, Religa TL, Lundström P, Fersht AR, Kay LE. The folding pathway of an FF domain: characterization of an on-pathway intermediate state under folding conditions by (15)N, (13)C(alpha) and (13)C-methyl relaxation dispersion and (1)H/(2)H-exchange NMR spectroscopy. Journal of Molecular Biology. 372: 497-512. PMID 17689561 DOI: 10.1016/J.Jmb.2007.06.012  1
2007 Mayer S, Rüdiger S, Ang HC, Joerger AC, Fersht AR. Correlation of Levels of Folded Recombinant p53 in Escherichia coli with Thermodynamic Stability in Vitro Journal of Molecular Biology. 372: 268-276. PMID 17631895 DOI: 10.1016/j.jmb.2007.06.044  1
2007 Sato S, Fersht AR. Searching for Multiple Folding Pathways of a Nearly Symmetrical Protein: Temperature Dependent Φ-Value Analysis of the B Domain of Protein A Journal of Molecular Biology. 372: 254-267. PMID 17628591 DOI: 10.1016/J.Jmb.2007.06.043  1
2007 Tidow H, Melero R, Mylonas E, Freund SM, Grossmann JG, Carazo JM, Svergun DI, Valle M, Fersht AR. Quaternary structures of tumor suppressor p53 and a specific p53 DNA complex. Proceedings of the National Academy of Sciences of the United States of America. 104: 12324-9. PMID 17620598 DOI: 10.1073/Pnas.0705069104  1
2007 Tidow H, Andreeva A, Rutherford TJ, Fersht AR. Solution Structure of ASPP2 N-terminal Domain (N-ASPP2) Reveals a Ubiquitin-like Fold Journal of Molecular Biology. 371: 948-958. PMID 17594908 DOI: 10.1016/j.jmb.2007.05.024  1
2007 Religa TL, Johnson CM, Vu DM, Brewer SH, Dyer RB, Fersht AR. The helix-turn-helix motif as an ultrafast independently folding domain: The pathway of folding of Engrailed homeodomain Proceedings of the National Academy of Sciences of the United States of America. 104: 9272-9277. PMID 17517666 DOI: 10.1073/Pnas.0703434104  1
2007 Teufel DP, Freund SM, Bycroft M, Fersht AR. Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53. Proceedings of the National Academy of Sciences of the United States of America. 104: 7009-14. PMID 17438265 DOI: 10.1073/pnas.0702010104  1
2007 Joerger AC, Fersht AR. Structural biology of the tumor suppressor p53 and cancer-associated mutants. Advances in Cancer Research. 97: 1-23. PMID 17419939 DOI: 10.1016/S0065-230X(06)97001-8  1
2007 Joerger AC, Fersht AR. Structure-function-rescue: the diverse nature of common p53 cancer mutants. Oncogene. 26: 2226-42. PMID 17401432 DOI: 10.1038/sj.onc.1210291  1
2007 Scott KA, Alonso DO, Sato S, Fersht AR, Daggett V. Conformational entropy of alanine versus glycine in protein denatured states. Proceedings of the National Academy of Sciences of the United States of America. 104: 2661-6. PMID 17307875 DOI: 10.1073/Pnas.0611182104  1
2007 Ferguson N, Sharpe TD, Johnson CM, Schartau PJ, Fersht AR. Structural biology: analysis of 'downhill' protein folding. Nature. 445: E14-5; discussion E1. PMID 17301742 DOI: 10.1038/Nature05643  1
2007 Karni-Schmidt O, Friedler A, Zupnick A, McKinney K, Mattia M, Beckerman R, Bouvet P, Sheetz M, Fersht A, Prives C. Energy-dependent nucleolar localization of p53 in vitro requires two discrete regions within the p53 carboxyl terminus. Oncogene. 26: 3878-91. PMID 17237827 DOI: 10.1038/Sj.Onc.1210162  1
2007 Huang F, Sato S, Sharpe TD, Ying L, Fersht AR. Distinguishing between cooperative and unimodal downhill protein folding. Proceedings of the National Academy of Sciences of the United States of America. 104: 123-7. PMID 17200301 DOI: 10.1073/pnas.0609717104  1
2007 Fersht AR, Daggett V. Folding and binding: implementing the game plan Current Opinion in Structural Biology. 17: 1-2. DOI: 10.1016/J.Sbi.2007.01.011  1
2006 Ferguson N, Becker J, Tidow H, Tremmel S, Sharpe TD, Krause G, Flinders J, Petrovich M, Berriman J, Oschkinat H, Fersht AR. General structural motifs of amyloid protofilaments. Proceedings of the National Academy of Sciences of the United States of America. 103: 16248-53. PMID 17060612 DOI: 10.1073/Pnas.0607815103  1
2006 Joerger AC, Ang HC, Fersht AR. Structural basis for understanding oncogenic p53 mutations and designing rescue drugs. Proceedings of the National Academy of Sciences of the United States of America. 103: 15056-61. PMID 17015838 DOI: 10.1073/pnas.0607286103  1
2006 Tidow H, Veprintsev DB, Freund SM, Fersht AR. Effects of oncogenic mutations and DNA response elements on the binding of p53 to p53-binding protein 2 (53BP2). The Journal of Biological Chemistry. 281: 32526-33. PMID 16887812 DOI: 10.1074/jbc.M604725200  1
2006 Sánchez-Puig N, Fersht AR. Characterization of the native and fibrillar conformation of the human Nalpha-acetyltransferase ARD1. Protein Science : a Publication of the Protein Society. 15: 1968-76. PMID 16823041 DOI: 10.1110/Ps.062264006  1
2006 Petrovich M, Jonsson AL, Ferguson N, Daggett V, Fersht AR. Phi-analysis at the experimental limits: mechanism of beta-hairpin formation. Journal of Molecular Biology. 360: 865-81. PMID 16784750 DOI: 10.1016/J.Jmb.2006.05.050  1
2006 Sato S, Religa TL, Fersht AR. Phi-analysis of the folding of the B domain of protein A using multiple optical probes. Journal of Molecular Biology. 360: 850-64. PMID 16782128 DOI: 10.1016/J.Jmb.2006.05.051  1
2006 Ang HC, Joerger AC, Mayer S, Fersht AR. Effects of common cancer mutations on stability and DNA binding of full-length p53 compared with isolated core domains. The Journal of Biological Chemistry. 281: 21934-41. PMID 16754663 DOI: 10.1074/jbc.M604209200  1
2006 Cañadillas JM, Tidow H, Freund SM, Rutherford TJ, Ang HC, Fersht AR. Solution structure of p53 core domain: structural basis for its instability. Proceedings of the National Academy of Sciences of the United States of America. 103: 2109-14. PMID 16461916 DOI: 10.1073/Pnas.0510941103  1
2006 Veprintsev DB, Freund SM, Andreeva A, Rutledge SE, Tidow H, Cañadillas JM, Blair CM, Fersht AR. Core domain interactions in full-length p53 in solution. Proceedings of the National Academy of Sciences of the United States of America. 103: 2115-9. PMID 16461914 DOI: 10.1073/Pnas.0511130103  1
2006 Yu GW, Rudiger S, Veprintsev D, Freund S, Fernandez-Fernandez MR, Fersht AR. The central region of HDM2 provides a second binding site for p53. Proceedings of the National Academy of Sciences of the United States of America. 103: 1227-32. PMID 16432196 DOI: 10.1073/Pnas.0510343103  1
2006 Ferguson N, Sharpe TD, Johnson CM, Fersht AR. The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics. Journal of Molecular Biology. 356: 1237-47. PMID 16406408 DOI: 10.1016/J.Jmb.2005.12.016  1
2006 Briseño-Roa L, Hill J, Notman S, Sellers D, Smith AP, Timperley CM, Wetherell J, Williams NH, Williams GR, Fersht AR, Griffiths AD. Analogues with fluorescent leaving groups for screening and selection of enzymes that efficiently hydrolyze organophosphorus nerve agents. Journal of Medicinal Chemistry. 49: 246-55. PMID 16392809 DOI: 10.1021/Jm050518J  1
2006 Yu GW, Allen MD, Andreeva A, Fersht AR, Bycroft M. Solution structure of the C4 zinc finger domain of HDM2. Protein Science : a Publication of the Protein Society. 15: 384-9. PMID 16385008 DOI: 10.1110/Ps.051927306  1
2005 Fersht A. How and why to publish in PNAS Proceedings of the National Academy of Sciences of the United States of America. 102: 6241-6242. PMID 16576766 DOI: 10.1073/Pnas.0502713102  0.01
2005 Religa TL, Markson JS, Mayor U, Freund SM, Fersht AR. Solution structure of a protein denatured state and folding intermediate. Nature. 437: 1053-6. PMID 16222301 DOI: 10.1038/Nature04054  1
2005 Ferguson N, Sharpe TD, Schartau PJ, Sato S, Allen MD, Johnson CM, Rutherford TJ, Fersht AR. Ultra-fast barrier-limited folding in the peripheral subunit-binding domain family. Journal of Molecular Biology. 353: 427-46. PMID 16168437 DOI: 10.1016/J.Jmb.2005.08.031  1
2005 Salvatella X, Dobson CM, Fersht AR, Vendruscolo M. Determination of the folding transition states of barnase by using ΦI-value-restrained simulations validated by double mutant ΦIJ-values Proceedings of the National Academy of Sciences of the United States of America. 102: 12389-12394. PMID 16116084 DOI: 10.1073/Pnas.0408226102  1
2005 Koch M, Stronge VS, Shepherd D, Gadola SD, Mathew B, Ritter G, Fersht AR, Besra GS, Schmidt RR, Jones EY, Cerundolo V. The crystal structure of human CD1d with and without α-galactosylceramide Nature Immunology. 6: 819-826. PMID 16007090 DOI: 10.1038/Ni1225  1
2005 White GW, Gianni S, Grossmann JG, Jemth P, Fersht AR, Daggett V. Simulation and experiment conspire to reveal cryptic intermediates and a slide from the nucleation-condensation to framework mechanism of folding. Journal of Molecular Biology. 350: 757-75. PMID 15967458 DOI: 10.1016/J.Jmb.2005.05.005  1
2005 Jemth P, Day R, Gianni S, Khan F, Allen M, Daggett V, Fersht AR. The structure of the major transition state for folding of an FF domain from experiment and simulation. Journal of Molecular Biology. 350: 363-78. PMID 15935381 DOI: 10.1016/J.Jmb.2005.04.067  1
2005 Sánchez-Puig N, Veprintsev DB, Fersht AR. Human full-length Securin is a natively unfolded protein Protein Science. 14: 1410-1418. PMID 15929994 DOI: 10.1110/Ps.051368005  1
2005 Friedler A, Veprintsev DB, Freund SM, von Glos KI, Fersht AR. Modulation of binding of DNA to the C-terminal domain of p53 by acetylation. Structure (London, England : 1993). 13: 629-36. PMID 15837201 DOI: 10.1016/J.Str.2005.01.020  1
2005 Weinberg RL, Veprintsev DB, Bycroft M, Fersht AR. Comparative binding of p53 to its promoter and DNA recognition elements Journal of Molecular Biology. 348: 589-596. PMID 15826656 DOI: 10.1016/J.Jmb.2005.03.014  1
2005 Fernandez-Fernandez MR, Veprintsev DB, Fersht AR. Proteins of the S100 family the regulate the oligomerization of p53 tumor suppressor Proceedings of the National Academy of Sciences of the United States of America. 102: 4735-4740. PMID 15781852 DOI: 10.1073/Pnas.0501459102  1
2005 Ferguson N, Day R, Johnson CM, Allen MD, Daggett V, Fersht AR. Simulation and experiment at high temperatures: ultrafast folding of a thermophilic protein by nucleation-condensation. Journal of Molecular Biology. 347: 855-70. PMID 15769475 DOI: 10.1016/J.Jmb.2004.12.061  1
2005 Joerger AC, Ang HC, Veprintsev DB, Blair CM, Fersht AR. Structures of p53 cancer mutants and mechanism of rescue by second-site suppressor mutations. The Journal of Biological Chemistry. 280: 16030-7. PMID 15703170 DOI: 10.1074/Jbc.M500179200  1
2005 Garcia P, Bruix M, Rico M, Ciofi-Baffoni S, Banci L, Ramachandra Shastry MC, Roder H, De Lumley Woodyear T, Johnson CM, Fersht AR, Barker PD. Effects of heme on the structure of the denatured state and folding kinetics of cytochrome b562 Journal of Molecular Biology. 346: 331-344. PMID 15663948 DOI: 10.1016/J.Jmb.2004.11.044  1
2005 Sánchez-Puig N, Veprintsev DB, Fersht AR. Binding of natively unfolded HIF-1α ODD domain to p53 Molecular Cell. 17: 11-21. PMID 15629713 DOI: 10.1016/J.Molcel.2004.11.019  1
2005 Friedler A, Veprintsev DB, Rutherford T, Von Glos KI, Fersht AR. Binding of Rad51 and other peptide sequences to a promiscuous, highly electrostatic binding site in p53 Journal of Biological Chemistry. 280: 8051-8059. PMID 15611070 DOI: 10.1074/Jbc.M411176200  1
2005 Fulton KF, Devlin GL, Jodun RA, Silvestri L, Bottomley SP, Fersht AR, Buckle AM. PFD: A database for the investigation of protein folding kinetics and stability Nucleic Acids Research. 33: D279-D283. PMID 15608196 DOI: 10.1093/Nar/Gki016  1
2005 Religa T, Markson J, Mayor U, Freund S, Fersht A. Solution structure of Engrailed homeodomain L16A mutant Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.2210/Pdb1Ztr/Pdb  1
2005 Joerger AC, Friedler A, Fersht AR. Wild Type p53 conformation, structural consequences of p53 mutations and mechanisms of mutant p53 rescue 25 Years of P53 Research. 377-397. DOI: 10.1007/978-1-4020-2922-6_17  1
2004 Fersht AR. Φ value versus ψ analysis Proceedings of the National Academy of Sciences of the United States of America. 101: 17327-17328. PMID 15583125 DOI: 10.1073/Pnas.0407863101  1
2004 Ferguson N, Schartau PJ, Sharpe TD, Sato S, Fersht AR. One-state downhill versus conventional protein folding. Journal of Molecular Biology. 344: 295-301. PMID 15522284 DOI: 10.1016/J.Jmb.2004.09.069  1
2004 Fersht AR. Relationship of Leffler (Brønsted) α values and protein folding Φ values to position of transition-state structures on reaction coordinates Proceedings of the National Academy of Sciences of the United States of America. 101: 14338-14342. PMID 15383660 DOI: 10.1073/Pnas.0406091101  1
2004 Weinberg RL, Freund SM, Veprintsev DB, Bycroft M, Fersht AR. Regulation of DNA binding of p53 by its C-terminal domain. Journal of Molecular Biology. 342: 801-11. PMID 15342238 DOI: 10.1016/J.Jmb.2004.07.042  1
2004 Weinberg RL, Veprintsev DB, Fersht AR. Cooperative binding of tetrameric p53 to DNA Journal of Molecular Biology. 341: 1145-1159. PMID 15321712 DOI: 10.1016/J.Jmb.2004.06.071  1
2004 Oliynyk Z, Briseño-Roa L, Janowitz T, Sondergeld P, Fersht AR. Designing a metal-binding site in the scaffold of Escherichia coli KDO8PS. Protein Engineering, Design & Selection : Peds. 17: 383-90. PMID 15166313 DOI: 10.1093/Protein/Gzh046  1
2004 Fersht AR, Sato S. Phi-value analysis and the nature of protein-folding transition states. Proceedings of the National Academy of Sciences of the United States of America. 101: 7976-81. PMID 15150406 DOI: 10.1073/Pnas.0402684101  1
2004 Jemth P, Gianni S, Day R, Li B, Johnson CM, Daggett V, Fersht AR. Demonstration of a low-energy on-pathway intermediate in a fast-folding protein by kinetics, protein engineering, and simulation. Proceedings of the National Academy of Sciences of the United States of America. 101: 6450-5. PMID 15096617 DOI: 10.1073/Pnas.0401732101  1
2004 Sato S, Religa TL, Daggett V, Fersht AR. Testing protein-folding simulations by experiment: B domain of protein A. Proceedings of the National Academy of Sciences of the United States of America. 101: 6952-6. PMID 15069202 DOI: 10.1073/Pnas.0401396101  1
2004 Batuwangala T, Shepherd D, Gadola SD, Gibson KJC, Zaccai NR, Fersht AR, Besra GS, Cerundolo V, Jones EY. The Crystal Structure of Human CD1b with a Bound Bacterial Glycolipid Journal of Immunology. 172: 2382-2388. PMID 14764708 DOI: 10.4049/Jimmunol.172.4.2382  1
2004 Schon O, Friedler A, Freund S, Fersht AR. Binding of p53-derived ligands to MDM2 induces a variety of long range conformational changes. Journal of Molecular Biology. 336: 197-202. PMID 14741215 DOI: 10.1016/J.Jmb.2003.11.051  1
2004 Friedler A, DeDecker BS, Freund SM, Blair C, Rüdiger S, Fersht AR. Structural distortion of p53 by the mutation R249S and its rescue by a designed peptide: implications for "mutant conformation". Journal of Molecular Biology. 336: 187-96. PMID 14741214 DOI: 10.1016/J.Jmb.2003.12.005  1
2004 Joerger AC, Allen MD, Fersht AR. Crystal structure of a superstable mutant of human p53 core domain: Insights into the mechanism of rescuing oncogenic mutations Journal of Biological Chemistry. 279: 1291-1296. PMID 14534297 DOI: 10.1074/Jbc.M309732200  1
2004 Zhang S, Rich A, Sussman JL, Fersht AR. Carl-Ivar Brändén 1934–2004 Nature Structural & Molecular Biology. 11: 490-492. DOI: 10.1038/Nsmb0604-490  0.04
2003 Gianni S, Mayor U, Fersht AR. Structural insights in the folding of small single-domain proteins The Italian Journal of Biochemistry. 52: 154-161. PMID 15141482  1
2003 Issaeva N, Friedler A, Bozko P, Wiman KG, Fersht AR, Selivanova G. Rescue of mutants of the tumor suppressor p53 in cancer cells by a designed peptide Proceedings of the National Academy of Sciences of the United States of America. 100: 13303-13307. PMID 14595027 DOI: 10.1073/Pnas.1835733100  1
2003 Gianni S, Guydosh NR, Khan F, Caldas TD, Mayor U, White GW, DeMarco ML, Daggett V, Fersht AR. Unifying features in protein-folding mechanisms. Proceedings of the National Academy of Sciences of the United States of America. 100: 13286-91. PMID 14595026 DOI: 10.1073/Pnas.1835776100  1
2003 Mayor U, Grossmann JG, Foster NW, Freund SM, Fersht AR. The denatured state of Engrailed Homeodomain under denaturing and native conditions. Journal of Molecular Biology. 333: 977-91. PMID 14583194 DOI: 10.1016/J.Jmb.2003.08.062  1
2003 Khan F, Chuang JI, Gianni S, Fersht AR. The kinetic pathway of folding of barnase. Journal of Molecular Biology. 333: 169-86. PMID 14516751 DOI: 10.1016/J.Jmb.2003.08.024  1
2003 Stollar EJ, Mayor U, Lovell SC, Federici L, Freund SM, Fersht AR, Luisi BF. Crystal structures of engrailed homeodomain mutants: implications for stability and dynamics. The Journal of Biological Chemistry. 278: 43699-708. PMID 12923178 DOI: 10.1074/Jbc.M308029200  1
2003 Ferguson N, Berriman J, Petrovich M, Sharpe TD, Finch JT, Fersht AR. Rapid amyloid fiber formation from the fast-folding WW domain FBP28. Proceedings of the National Academy of Sciences of the United States of America. 100: 9814-9. PMID 12897238 DOI: 10.1073/Pnas.1333907100  1
2003 Joerger AC, Mayer S, Fersht AR. Mimicking natural evolution in vitro: An N-acetylneuraminate lyase mutant with an increased dihydrodipicolinate synthase activity Proceedings of the National Academy of Sciences of the United States of America. 100: 5694-5699. PMID 12711733 DOI: 10.1073/pnas.0531477100  1
2003 Friedler A, Veprintsev DB, Hansson LO, Fersht AR. Kinetic instability of p53 core domain mutants. Implications for rescue by small molecules Journal of Biological Chemistry. 278: 24108-24112. PMID 12700230 DOI: 10.1074/jbc.M302458200  1
2003 Mayor U, Guydosh NR, Johnson CM, Grossmann JG, Sato S, Jas GS, Freund SM, Alonso DO, Daggett V, Fersht AR. The complete folding pathway of a protein from nanoseconds to microseconds. Nature. 421: 863-7. PMID 12594518 DOI: 10.1038/Nature01428  1
2003 Ferguson N, Fersht AR. Early events in protein folding Current Opinion in Structural Biology. 13: 75-81. PMID 12581663 DOI: 10.1016/S0959-440X(02)00009-X  1
2003 Daggett V, Fersht AR. Is there a unifying mechanism for protein folding? Trends in Biochemical Sciences. 28: 18-25. PMID 12517448 DOI: 10.1016/S0968-0004(02)00012-9  1
2003 Tang KS, Fersht AR, Itzhaki LS. Sequential unfolding of ankyrin repeats in tumor suppressor p16 Structure. 11: 67-73. PMID 12517341 DOI: 10.1016/S0969-2126(02)00929-2  1
2002 Fersht AR. On the simulation of protein folding by short time scale molecular dynamics and distributed computing Proceedings of the National Academy of Sciences of the United States of America. 99: 14122-14125. PMID 12388785 DOI: 10.1073/pnas.182542699  1
2002 Schon O, Friedler A, Bycroft M, Freund SM, Fersht AR. Molecular mechanism of the interaction between MDM2 and p53. Journal of Molecular Biology. 323: 491-501. PMID 12381304 DOI: 10.1016/S0022-2836(02)00852-5  1
2002 Rudiger S, Freund SM, Veprintsev DB, Fersht AR. CRINEPT-TROSY NMR reveals p53 core domain bound in an unfolded form to the chaperone Hsp90. Proceedings of the National Academy of Sciences of the United States of America. 99: 11085-90. PMID 12163643 DOI: 10.1073/pnas.132393699  1
2002 Hansson LO, Friedler A, Freund S, Rudiger S, Fersht AR. Two sequence motifs from HIF-1alpha bind to the DNA-binding site of p53. Proceedings of the National Academy of Sciences of the United States of America. 99: 10305-9. PMID 12124396 DOI: 10.1073/Pnas.122347199  1
2002 Rippin TM, Freund SM, Veprintsev DB, Fersht AR. Recognition of DNA by p53 core domain and location of intermolecular contacts of cooperative binding. Journal of Molecular Biology. 319: 351-8. PMID 12051912 DOI: 10.1016/S0022-2836(02)00326-1  1
2002 Altamirano MM, Blackburn JM, Aguayo C, Fersht AR. Retraction. Directed evolution of new catalytic activity using the alpha/beta-barrel scaffold. Nature. 417: 468. PMID 12024219 DOI: 10.1038/417468A  1
2002 Rippin TM, Bykov VJ, Freund SM, Selivanova G, Wiman KG, Fersht AR. Characterization of the p53-rescue drug CP-31398 in vitro and in living cells. Oncogene. 21: 2119-29. PMID 11948395 DOI: 10.1038/Sj.Onc.1205362  1
2002 Fersht AR. Max Ferdinand Perutz OM FRS Nature Structural Biology. 9: 245-246. PMID 11914731 DOI: 10.1038/Nsb0402-245  1
2002 Vaughan CK, Harryson P, Buckle AM, Fersht AR. A structural double-mutant cycle: estimating the strength of a buried salt bridge in barnase. Acta Crystallographica. Section D, Biological Crystallography. 58: 591-600. PMID 11914482 DOI: 10.1107/S0907444902001567  1
2002 Fersht AR, Daggett V. Protein folding and unfolding at atomic resolution. Cell. 108: 573-82. PMID 11909527 DOI: 10.1016/S0092-8674(02)00620-7  1
2002 Friedler A, Hansson LO, Veprintsev DB, Freund SM, Rippin TM, Nikolova PV, Proctor MR, Rüdiger S, Fersht AR. A peptide that binds and stabilizes p53 core domain: chaperone strategy for rescue of oncogenic mutants. Proceedings of the National Academy of Sciences of the United States of America. 99: 937-42. PMID 11782540 DOI: 10.1073/Pnas.241629998  1
2002 Galani D, Fersht AR, Perrett S. Folding of the yeast prion protein Ure2: Kinetic evidence for folding and unfolding intermediates Journal of Molecular Biology. 315: 213-227. PMID 11779240 DOI: 10.1006/Jmbi.2001.5234  1
2002 Kazmirski SL, Isaacson RL, An C, Buckle A, Johnson CM, Daggett V, Fersht AR. Loss of a metal-binding site in gelsolin leads to familial amyloidosis-Finnish type. Nature Structural Biology. 9: 112-6. PMID 11753432 DOI: 10.1038/Nsb745  1
2002 Hendrickson WA, Brändén CI, Fersht AR. New look and new outlook Structure. 10: 1. DOI: 10.1016/S0969-2126(01)00704-3  1
2001 Bullock AN, Fersht AR. Rescuing the function of mutant p53 Nature Reviews Cancer. 1: 68-76. PMID 11900253  1
2001 Ferguson N, Pires JR, Toepert F, Johnson CM, Pan YP, Volkmer-Engert R, Schneider-Mergener J, Daggett V, Oschkinat H, Fersht A. Using flexible loop mimetics to extend phi-value analysis to secondary structure interactions. Proceedings of the National Academy of Sciences of the United States of America. 98: 13008-13. PMID 11687614 DOI: 10.1073/Pnas.221467398  1
2001 Ferguson N, Johnson CM, Macias M, Oschkinat H, Fersht A. Ultrafast folding of WW domains without structured aromatic clusters in the denatured state. Proceedings of the National Academy of Sciences of the United States of America. 98: 13002-7. PMID 11687613 DOI: 10.1073/Pnas.221467198  0.01
2001 Ikura T, Fersht AR. Folding mechanism and folding rate Tanpakushitsu Kakusan Koso. Protein, Nucleic Acid, Enzyme. 46: 1553-1559. PMID 11579550  1
2001 Frisch C, Fersht AR, Schreiber G. Experimental assignment of the structure of the transition state for the association of barnase and barstar Journal of Molecular Biology. 308: 69-77. PMID 11302708 DOI: 10.1006/Jmbi.2001.4577  1
2001 Smoot AL, Panda M, Brazil BT, Buckle AM, Fersht AR, Horowitz PM. 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. Biochemistry. 40: 4484-92. PMID 11284705 DOI: 10.1021/Bi001822B  1
2001 Kazmirski SL, Wong KB, Freund SM, Tan YJ, Fersht AR, Daggett V. Protein folding from a highly disordered denatured state: the folding pathway of chymotrypsin inhibitor 2 at atomic resolution. Proceedings of the National Academy of Sciences of the United States of America. 98: 4349-54. PMID 11274353 DOI: 10.1073/Pnas.071054398  1
2001 Wang WK, Bycroft M, Foster NW, Buckle AM, Fersht AR, Chen YW. Structure of the C-terminal sterile α-motif (SAM) domain of human p73α Acta Crystallographica Section D: Biological Crystallography. 57: 545-551. PMID 11264583 DOI: 10.1107/S0907444901002529  1
2001 Karadimitris A, Gadola S, Altamirano M, Brown D, Woolfson A, Klenerman P, Chen JL, Koezuka Y, Roberts IA, Price DA, Dusheiko G, Milstein C, Fersht A, Luzzatto L, Cerundolo V. Human CD1d-glycolipid tetramers generated by in vitro oxidative refolding chromatography. Proceedings of the National Academy of Sciences of the United States of America. 98: 3294-8. PMID 11248072 DOI: 10.1073/Pnas.051604498  1
2001 Altamirano MM, Woolfson A, Donda A, Shamshiev A, Briseño-Roa L, Foster NW, Veprintsev DB, De Libero G, Fersht AR, Milstein C. Ligand-independent assembly of recombinant human CD1 by using oxidative refolding chromatography. Proceedings of the National Academy of Sciences of the United States of America. 98: 3288-93. PMID 11248071 DOI: 10.1073/Pnas.041596598  1
2001 Tanaka N, Nakao S, Chatellier J, Fersht AR. Role of the Conformational Flexibility on the Substrate Recognition of Molecular Chaperone DnaK Seibutsu Butsuri. 41. DOI: 10.2142/Biophys.41.S167_1  1
2001 Dobson CM, Ellis RJ, Fersht AR. Philosophical transactions of the Royal Society of London series B: Preface Philosophical Transactions of the Royal Society B: Biological Sciences. 356: 129-131. DOI: 10.1098/rstb.2000.0757  1
2001 Hendrickson WA, Brändén CI, Fersht AR. Structure on the move Structure. 9: R1. DOI: 10.1016/S0969-2126(00)00562-1  1
2000 Yiu CP, Mateu MG, Fersht AR. Protein folding transition states: elicitation of Hammond effects by 2,2,2-trifluoroethanol. Chembiochem : a European Journal of Chemical Biology. 1: 49-55. PMID 11828398 DOI: 10.1002/1439-7633(20000703)1:1<49::Aid-Cbic49>3.0.Co;2-A  1
2000 Clarke J, Hounslow AM, Bond CJ, Fersht AR, Daggett V. The effects of disulfide bonds on the denatured state of barnase. Protein Science : a Publication of the Protein Society. 9: 2394-404. PMID 11206061 DOI: 10.1110/Ps.9.12.2394  1
2000 Chatellier J, Hill F, Foster NW, Goloubinoff P, Fersht AR. From minichaperone to groel 3: Properties of an active single-ring mutant of groel Journal of Molecular Biology. 304: 897-910. PMID 11124035 DOI: 10.1006/Jmbi.2000.4278  1
2000 Chatellier J, Hill F, Fersht AR. From minichaperone to GroEL 2: Importance of avidity of the multisite ring structure Journal of Molecular Biology. 304: 883-896. PMID 11124034 DOI: 10.1006/Jmbi.2000.4277  1
2000 Wang Q, Buckle AM, Fersht AR. From Minichaperone to GroEL 1: Information on GroEL-polypeptide interactions from crystal packing of minichaperones Journal of Molecular Biology. 304: 873-881. PMID 11124033 DOI: 10.1006/Jmbi.2000.4276  1
2000 Fersht AR. A kinetically significant intermediate in the folding of barnase Proceedings of the National Academy of Sciences of the United States of America. 97: 14121-14126. PMID 11114199 DOI: 10.1073/Pnas.260502597  1
2000 Mayor U, Johnson CM, Daggett V, Fersht AR. Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation. Proceedings of the National Academy of Sciences of the United States of America. 97: 13518-22. PMID 11087839 DOI: 10.1073/Pnas.250473497  1
2000 Kazmirski SL, Howard MJ, Isaacson RL, Fersht AR. Elucidating the mechanism of familial amyloidosis- Finnish type: NMR studies of human gelsolin domain 2. Proceedings of the National Academy of Sciences of the United States of America. 97: 10706-11. PMID 10995458 DOI: 10.1073/Pnas.180310097  1
2000 Inaba K, Kobayashi N, Fersht AR. Conversion of two-state to multi-state folding kinetics on fusion of two protein foldons. Journal of Molecular Biology. 302: 219-233. PMID 10964571 DOI: 10.1006/Jmbi.2000.4024  1
2000 Carmichael J, Chatellier J, Woolfson A, Milstein C, Fersht AR, Rubinsztein DC. Bacterial and yeast chaperones reduce both aggregate formation and cell death in mammalian cell models of Huntington's disease. Proceedings of the National Academy of Sciences of the United States of America. 97: 9701-5. PMID 10920207 DOI: 10.1073/Pnas.170280697  1
2000 Neira JL, Vázquez E, Fersht AR. Stability and folding of the protein complexes of barnase. Febs Journal. 267: 2859-2870. PMID 10806383 DOI: 10.1046/J.1432-1327.2000.01290.X  1
2000 Wang Q, Buckle AM, Fersht AR. Stabilization of GroEL minichaperones by core and surface mutations Journal of Molecular Biology. 298: 917-926. PMID 10801358 DOI: 10.1006/Jmbi.2000.3716  1
2000 Bullock AN, Henckel J, Fersht AR. Quantitative analysis of residual folding and DNA binding in mutant p53 core domain: definition of mutant states for rescue in cancer therapy. Oncogene. 19: 1245-56. PMID 10713666 DOI: 10.1038/Sj.Onc.1203434  1
2000 Wong KB, Clarke J, Bond CJ, Neira JL, Freund SM, Fersht AR, Daggett V. Towards a complete description of the structural and dynamic properties of the denatured state of barnase and the role of residual structure in folding. Journal of Molecular Biology. 296: 1257-82. PMID 10698632 DOI: 10.1006/Jmbi.2000.3523  1
2000 Altamirano MM, Blackburn JM, Aguayo C, Fersht AR. Directed evolution of new catalytic activity using the alpha/beta-barrel scaffold. Nature. 403: 617-22. PMID 10688189 DOI: 10.1038/35001001  1
2000 Fersht AR. Transition-state structure as a unifying basis in protein-folding mechanisms: Contact order, chain topology, stability, and the extended nucleus mechanism Proceedings of the National Academy of Sciences of the United States of America. 97: 1525-1529. PMID 10677494 DOI: 10.1073/Pnas.97.4.1525  0.01
2000 Nikolova PV, Wong KB, DeDecker B, Henckel J, Fersht AR. Mechanism of rescue of common p53 cancer mutations by second-site suppressor mutations. The Embo Journal. 19: 370-8. PMID 10654936 DOI: 10.1093/Emboj/19.3.370  1
2000 Inaba K, Fersht A. Conversion of two-state to multi-state folding kinetics on fusion of two protein foldons Seibutsu Butsuri. 40. DOI: 10.2142/Biophys.40.S10_3  1
2000 Ikura T, Fersht AR. Correlation between folding-mechanism and folding-rate in protein folding Seibutsu Butsuri. 40. DOI: 10.2142/Biophys.40.S10_2  1
2000 Fersht AR, Altamirano MM. Designing new enzymes Biochemical Society Transactions. 28. DOI: 10.1042/Bst028A053B  1
2000 Fersht AR. Protein folding transition states: Elicitation of hammond effects by 2,2,2-trifluoroethanol Chembiochem. 1: 49-55.  1
1999 Chatellier J, Hartley O, Griffiths AD, Fersht AR, Winter G, Riechmann L. Interdomain interactions within the gene 3 protein of filamentous phage. Febs Letters. 463: 371-4. PMID 10606756 DOI: 10.1016/S0014-5793(99)01658-0  1
1999 Wang Q, Buckle AM, Foster NW, Johnson CM, Fersht AR. Design of highly stable functional GroEL minichaperones. Protein Science. 8: 2186-2193. PMID 10548065 DOI: 10.1110/Ps.8.10.2186  1
1999 Durocher D, Henckel J, Fersht AR, Jackson SP. The FHA domain is a modular phosphopeptide recognition motif. Molecular Cell. 4: 387-94. PMID 10518219 DOI: 10.1016/S1097-2765(00)80340-8  1
1999 Isaacson RL, Weeds AG, Fersht AR. Equilibria and kinetics of folding of gelsolin domain 2 and mutants involved in familial amyloidosis-Finnish type. Proceedings of the National Academy of Sciences of the United States of America. 96: 11247-52. PMID 10500162 DOI: 10.1073/Pnas.96.20.11247  1
1999 Kobayashi N, Freund SM, Chatellier J, Zahn R, Fersht AR. NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution. Journal of Molecular Biology. 292: 181-90. PMID 10493867 DOI: 10.1006/Jmbi.1999.3042  1
1999 Tanaka N, Fersht AR. Identification of substrate binding site of GroEL minichaperone in solution. Journal of Molecular Biology. 292: 173-180. PMID 10493866 DOI: 10.1006/Jmbi.1999.3041  1
1999 Chatellier J, Buckle AM, Fersht AR. GroEL recognises sequential and non-sequential linear structural motifs compatible with extended beta-strands and alpha-helices. Journal of Molecular Biology. 292: 163-172. PMID 10493865 DOI: 10.1006/Jmbi.1999.3040  1
1999 Golbik R, Fischer G, Fersht AR. Folding of barstar C40A/C82A/P27A and catalysis of the peptidyl-prolyl cis/trans isomerization by human cytosolic cyclophilin (Cyp18). Protein Science. 8: 1505-1514. PMID 10422840 DOI: 10.1110/Ps.8.7.1505  1
1999 Wong KB, DeDecker BS, Freund SM, Proctor MR, Bycroft M, Fersht AR. Hot-spot mutants of p53 core domain evince characteristic local structural changes. Proceedings of the National Academy of Sciences of the United States of America. 96: 8438-42. PMID 10411893 DOI: 10.1073/Pnas.96.15.8438  1
1999 Arnesano F, Banci L, Bertini I, Faraone-Mennella J, Rosato A, Barker PD, Fersht AR. The solution structure of oxidized Escherichia coli cytochrome b562. Biochemistry. 38: 8657-70. PMID 10393541 DOI: 10.1021/Bi982785F  0.01
1999 Perrett S, Freeman SJ, Butler PJ, Fersht AR. Equilibrium folding properties of the yeast prion protein determinant Ure2. Journal of Molecular Biology. 290: 331-45. PMID 10388576 DOI: 10.1006/Jmbi.1999.2872  1
1999 Killick TR, Freund SM, Fersht AR. Real-time NMR studies on a transient folding intermediate of barstar. Protein Science : a Publication of the Protein Society. 8: 1286-91. PMID 10386878 DOI: 10.1110/Ps.8.6.1286  1
1999 Mateu MG, Fersht AR. Mutually compensatory mutations during evolution of the tetramerization domain of tumor suppressor p53 lead to impaired hetero-oligomerization Proceedings of the National Academy of Sciences of the United States of America. 96: 3595-3599. PMID 10097082 DOI: 10.1073/Pnas.96.7.3595  1
1999 Neira JL, Fersht AR. Acquisition of native-like interactions in C-terminal fragments of barnase. Journal of Molecular Biology. 287: 421-432. PMID 10080903 DOI: 10.1006/Jmbi.1999.2602  1
1999 Otzen DE, Fersht AR. Analysis of protein-protein interactions by mutagenesis: direct versus indirect effects. Protein Engineering. 12: 41-45. PMID 10065709 DOI: 10.1093/Protein/12.1.41  1
1999 Axe DD, Foster NW, Fersht AR. An irregular beta-bulge common to a group of bacterial RNases is an important determinant of stability and function in barnase. Journal of Molecular Biology. 286: 1471-1485. PMID 10064710 DOI: 10.1006/Jmbi.1999.2569  1
1999 Altamirano MM, García C, Possani LD, Fersht AR. Oxidative refolding chromatography: folding of the scorpion toxin Cn5. Nature Biotechnology. 17: 187-191. PMID 10052357 DOI: 10.1038/6192  1
1999 Mateu MG, Sánchez Del Pino MM, Fersht AR. Mechanism of folding and assembly of a small tetrameric protein domain from tumor suppressor p53 Nature Structural Biology. 6: 191-198. PMID 10048932 DOI: 10.1038/5880  1
1999 Tang KS, Guralnick BJ, Wang WK, Fersht AR, Itzhaki LS. Stability and folding of the tumour suppressor protein p16 Journal of Molecular Biology. 285: 1869-1886. PMID 9917418 DOI: 10.1006/Jmbi.1998.2420  1
1999 Neira JL, Fersht AR. Exploring the folding funnel of a polypeptide chain by biophysical studies on protein fragments. Journal of Molecular Biology. 285: 1309-1333. PMID 9887278 DOI: 10.1006/Jmbi.1998.2249  1
1999 Tanaka N, Fersht A. Identification of substrate binding site of GroEL minichaperone in solution Biophysics. 39. DOI: 10.2142/Biophys.39.S157_3  1
1998 Vaughan CK, Buckle AM, Fersht AR. Structural response to mutation at a protein-protein interface. Journal of Molecular Biology. 286: 1487-1506. PMID 10064711 DOI: 10.1006/Jmbi.1998.2559  1
1998 Ben-Zvi AP, Chatellier J, Fersht AR, Goloubinoff P. Minimal and optimal mechanisms for GroE-mediated protein folding Proceedings of the National Academy of Sciences of the United States of America. 95: 15275-15280. PMID 9860959 DOI: 10.1073/Pnas.95.26.15275  1
1998 Nikolova PV, Henckel J, Lane DP, Fersht AR. Semirational design of active tumor suppressor p53 DNA binding domain with enhanced stability. Proceedings of the National Academy of Sciences of the United States of America. 95: 14675-80. PMID 9843948 DOI: 10.1073/Pnas.95.25.14675  1
1998 Chatellier J, Hill F, Lund PA, Fersht AR. In vivo activities of GroEL minichaperones Proceedings of the National Academy of Sciences of the United States of America. 95: 9861-9866. PMID 9707566 DOI: 10.1073/Pnas.95.17.9861  1
1998 Ladurner AG, Itzhaki LS, Daggett V, Fersht AR. Synergy between simulation and experiment in describing the energy landscape of protein folding. Proceedings of the National Academy of Sciences of the United States of America. 95: 8473-8. PMID 9671702 DOI: 10.1073/Pnas.95.15.8473  1
1998 Fersht AR, Shakhnovich EI. Protein folding: think globally, (inter)act locally. Current Biology : Cb. 8: R478-9. PMID 9663379 DOI: 10.1016/S0960-9822(98)70310-0  1
1998 Otzen DE, Fersht AR. Folding of Circular and Permuted Chymotrypsin Inhibitor 2: Retention of the Folding Nucleus† Biochemistry. 37: 8139-8146. PMID 9609709 DOI: 10.1021/Bi980250G  1
1998 Vijayakumar M, Wong KY, Schreiber G, Fersht AR, Szabo AP, Zhou H. Electrostatic enhancement of diffusion-controlled protein-protein association: comparison of theory and experiment on barnase and barstar. Journal of Molecular Biology. 278: 1015-1024. PMID 9600858 DOI: 10.1006/Jmbi.1998.1747  1
1998 Axe DD, Foster NW, Fersht AR. A Search For Single Substitutions That Eliminate Enzymatic Function In A Bacterial Ribonuclease Biochemistry. 37: 7157-7166. PMID 9585527 DOI: 10.1021/Bi9804028  1
1998 Mateu MG, Fersht AR. Nine hydrophobic side chains are key determinants of the thermodynamic stability and oligomerization status of tumour suppressor p53 tetramerization domain Embo Journal. 17: 2748-2758. PMID 9582268 DOI: 10.1093/Emboj/17.10.2748  1
1998 Fersht AR. Sieves in sequence. Science. 280: 541-541. PMID 9575099 DOI: 10.1126/Science.280.5363.541  0.01
1998 Dalby PA, Clarke J, Johnson CM, Fersht AR. Folding intermediates of wild-type and mutants of barnase. II. Correlation of changes in equilibrium amide exchange kinetics with the population of the folding intermediate. Journal of Molecular Biology. 276: 647-56. PMID 9551102 DOI: 10.1006/Jmbi.1997.1547  0.12
1998 Dalby PA, Oliveberg M, Fersht AR. Folding intermediates of wild-type and mutants of barnase. I. use of @f-value analysis and m-values to probe the cooperative nature of the folding pre-equilibrium Journal of Molecular Biology. 276: 625-646. PMID 9551101 DOI: 10.1006/Jmbi.1997.1546  1
1998 Oliveberg M, Tan Y, Silow M, Fersht AR. The Changing Nature of the Protein Folding Transition State: Implications for the Shape of the Free-energy Profile for Folding Journal of Molecular Biology. 277: 933-943. PMID 9545382 DOI: 10.1006/Jmbi.1997.1612  1
1998 Dalby PA, Oliveberg M, Fersht AR. Movement of the Intermediate and Rate Determining Transition State of Barnase on the Energy Landscape with Changing Temperature Biochemistry. 37: 4674-4679. PMID 9521788 DOI: 10.1021/Bi972798D  1
1998 Golbik R, Zahn R, Harding SE, Fersht AR. Thermodynamic stability and folding of GroEL minichaperones. Journal of Molecular Biology. 276: 505-15. PMID 9512719 DOI: 10.1006/Jmbi.1997.1538  0.04
1998 Killick TR, Freund SM, Fersht AR. Real-time NMR studies on folding of mutants of barnase and chymotrypsin inhibitor 2. Febs Letters. 423: 110-2. PMID 9506851 DOI: 10.1016/S0014-5793(98)00075-1  1
1998 Ladurner AG, Itzhaki LS, Fersht AR. Strain in the folding nucleus of chymotrypsin inhibitor 2. Folding & Design. 2: 363-8. PMID 9427010 DOI: 10.1016/S1359-0278(97)00050-3  0.32
1998 Clarke J, Itzhaki LS, Fersht AR. A reply to Englander and Woodward Trends in Biochemical Sciences. 23: 379-381. DOI: 10.1016/S0968-0004(98)01280-8  0.2
1997 Bullock AN, Henckel J, DeDecker BS, Johnson CM, Nikolova PV, Proctor MR, Lane DP, Fersht AR. Thermodynamic stability of wild-type and mutant p53 core domain. Proceedings of the National Academy of Sciences of the United States of America. 94: 14338-42. PMID 9405613 DOI: 10.1073/Pnas.94.26.14338  1
1997 Stenberg G, Fersht AR. Folding of barnase in the presence of the molecular chaperone SecB Journal of Molecular Biology. 274: 268-275. PMID 9398532 DOI: 10.1006/Jmbi.1997.1398  1
1997 Soler‐González AS, Fersht AR. Helix Stability in Barstar Peptides Febs Journal. 249: 724-732. PMID 9395319 DOI: 10.1111/J.1432-1033.1997.T01-1-00724.X  0.01
1997 Bond CJ, Wong KB, Clarke J, Fersht AR, Daggett V. Characterization of residual structure in the thermally denatured state of barnase by simulation and experiment: description of the folding pathway. Proceedings of the National Academy of Sciences of the United States of America. 94: 13409-13. PMID 9391038 DOI: 10.1073/Pnas.94.25.13409  1
1997 Ladurner AG, Fersht AR. Glutamine, alanine or glycine repeats inserted into the loop of a protein have minimal effects on stability and folding rates. Journal of Molecular Biology. 273: 330-7. PMID 9367765 DOI: 10.1006/Jmbi.1997.1304  0.44
1997 Ladurner AG, Itzhaki LS, de Prat Gay G, Fersht AR. Complementation of peptide fragments of the single domain protein chymotrypsin inhibitor 2. Journal of Molecular Biology. 273: 317-29. PMID 9367764 DOI: 10.1006/Jmbi.1997.1303  0.24
1997 Clarke J, Itzhaki LS, Fersht AR. Hydrogen exchange at equilibrium: a short cut for analysing protein-folding pathways? Trends in Biochemical Sciences. 22: 284-7. PMID 9270297 DOI: 10.1016/S0968-0004(97)01087-6  0.16
1997 Nölting B, Golbik R, Soler-González aAS, Fersht AR. Circular Dichroism Of Denatured Barstar Suggests Residual Structure Biochemistry. 36: 9899-9905. PMID 9245422 DOI: 10.1021/Bi962879U  1
1997 Schreiber G, Frisch C, Fersht AR. The role of Glu73 of barnase in catalysis and the binding of barstar. Journal of Molecular Biology. 270: 111-122. PMID 9231905 DOI: 10.1006/Jmbi.1997.1080  1
1997 Neira JL, Itzhaki LS, Otzen DE, Davis B, Fersht AR. Hydrogen exchange in chymotrypsin inhibitor 2 probed by mutagenesis. Journal of Molecular Biology. 270: 99-110. PMID 9231904 DOI: 10.1006/Jmbi.1997.1088  1
1997 Itzhaki LS, Neira JL, Fersht AR. Hydrogen exchange in chymotrypsin inhibitor 2 probed by denaturants and temperature. Journal of Molecular Biology. 270: 89-98. PMID 9231903 DOI: 10.1006/Jmbi.1997.1049  1
1997 Perrett S, Zahn R, Stenberg G, Fersht AR. Importance of electrostatic interactions in the rapid binding of polypeptides to GroEL. Journal of Molecular Biology. 269: 892-901. PMID 9223649 DOI: 10.1006/Jmbi.1997.1081  1
1997 Tan Y, Oliveberg M, Otzen DE, Fersht AR. The rate of isomerisation of peptidyl-proline bonds as a probe for interactions in the physiological denatured state of chymotrypsin inhibitor 2 Journal of Molecular Biology. 269: 611-622. PMID 9217264 DOI: 10.1006/Jmbi.1997.1043  1
1997 Wong KB, Fersht AR, Freund SM. NMR 15N relaxation and structural studies reveal slow conformational exchange in barstar C40/82A. Journal of Molecular Biology. 268: 494-511. PMID 9159486 DOI: 10.1006/Jmbi.1997.0989  1
1997 Pino MMSD, Fersht AR. Nonsequential unfolding of the alpha/beta barrel protein indole-3-glycerol-phosphate synthase. Biochemistry. 36: 5560-5565. PMID 9154940 DOI: 10.1021/Bi963133Z  0.01
1997 Johnson CM, Oliveberg M, Clarke J, Fersht AR. Thermodynamics of denaturation of mutants of barnase with disulfide crosslinks. Journal of Molecular Biology. 268: 198-208. PMID 9149152 DOI: 10.1006/Jmbi.1997.0928  0.01
1997 Neira JL, Itzhaki LS, Ladurner AG, Davis B, de Prat Gay G, Fersht AR. Following co-operative formation of secondary and tertiary structure in a single protein module. Journal of Molecular Biology. 268: 185-97. PMID 9149151 DOI: 10.1006/Jmbi.1997.0932  0.16
1997 Gopalan V, Golbik R, Schreiber G, Fersht AR, Altman S. Fluorescence properties of a tryptophan residue in an aromatic core of the protein subunit of ribonuclease P from Escherichia coli. Journal of Molecular Biology. 267: 765-9. PMID 9135109 DOI: 10.1006/Jmbi.1997.0907  1
1997 Frisch C, Schreiber G, Johnson CM, Fersht AR. Thermodynamics of the interaction of barnase and barstar: changes in free energy versus changes in enthalpy on mutation. Journal of Molecular Biology. 267: 696-706. PMID 9126847 DOI: 10.1006/Jmbi.1997.0892  1
1997 Chène P, Day AG, Fersht AR. Role of isoleucine-164 at the active site of rubisco from Rhodospirillum rubrum. Biochemical and Biophysical Research Communications. 232: 482-486. PMID 9125206 DOI: 10.1006/Bbrc.1997.6318  1
1997 Altamirano MM, Golbik R, Zahn R, Buckle AM, Fersht AR. Refolding chromatography with immobilized mini-chaperones Proceedings of the National Academy of Sciences of the United States of America. 94: 3576-3578. PMID 9108018 DOI: 10.1073/Pnas.94.8.3576  1
1997 Clarke J, Fersht AR. An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway. Folding & Design. 1: 243-54. PMID 9079387 DOI: 10.1016/S1359-0278(96)00038-7  0.08
1997 Neira JL, Davis B, Ladurner AG, Buckle AM, Gay Gde P, Fersht AR. Towards the complete structural characterization of a protein folding pathway: the structures of the denatured, transition and native states for the association/folding of two complementary fragments of cleaved chymotrypsin inhibitor 2. Direct evidence for a nucleation-condensation mechanism. Folding & Design. 1: 189-208. PMID 9079381 DOI: 10.1016/S1359-0278(96)00031-4  0.08
1997 Nölting B, Golbik R, Neira JL, Soler-Gonzalez AS, Schreiber G, Fersht AR. The Folding Pathway of a Protein at High Resolution from Microseconds to Seconds Proceedings of the National Academy of Sciences of the United States of America. 94: 826-830. PMID 9023341 DOI: 10.1073/Pnas.94.3.826  1
1996 Corrales FJ, Fersht AR. Kinetic significance of GroEL14·(GroES7)2 complexes in molecular chaperone activity Folding and Design. 1: 265-273. PMID 9079389 DOI: 10.1016/S1359-0278(96)00040-5  1
1996 Neira JL, Fersht AR. An NMR study on the β-hairpin region of barnase Folding and Design. 1: 231-241. PMID 9079384 DOI: 10.1016/S1359-0278(96)00034-X  1
1996 Zahn R, Buckle AM, Perrett S, Johnson CM, Corrales FJ, Golbik R, Fersht AR. Chaperone activity and structure of monomeric polypeptide binding domains of GroEL. Proceedings of the National Academy of Sciences of the United States of America. 93: 15024-15029. PMID 8986757 DOI: 10.1073/Pnas.93.26.15024  1
1996 Tan Y, Oliveberg M, Fersht AR. Titration properties and thermodynamics of the transition state for folding: comparison of two-state and multi-state folding pathways. Journal of Molecular Biology. 264: 377-389. PMID 8951383 DOI: 10.1006/Jmbi.1996.0647  1
1996 Freund SM, Wong KB, Fersht AR. Initiation sites of protein folding by NMR analysis. Proceedings of the National Academy of Sciences of the United States of America. 93: 10600-3. PMID 8855224 DOI: 10.1073/Pnas.93.20.10600  1
1996 Zahn R, Perrett S, Fersht AR. Conformational states bound by the molecular chaperones GroEL and secB: a hidden unfolding (annealing) activity. Journal of Molecular Biology. 261: 43-61. PMID 8760501 DOI: 10.1006/Jmbi.1996.0440  1
1996 Wong KB, Freund SM, Fersht AR. Cold denaturation of barstar: 1H, 15N and 13C NMR assignment and characterisation of residual structure. Journal of Molecular Biology. 259: 805-18. PMID 8683584 DOI: 10.1006/Jmbi.1996.0359  1
1996 Axe DD, Foster NW, Fersht AR. Active barnase variants with completely random hydrophobic cores. Proceedings of the National Academy of Sciences of the United States of America. 93: 5590-5594. PMID 8643620 DOI: 10.1073/Pnas.93.11.5590  1
1996 Oliveberg M, Fersht AR. A New Approach to the Study of Transient Protein Conformations: The Formation of a Semiburied Salt Link in the Folding Pathway of Barnase Biochemistry. 35: 6795-6805. PMID 8639631 DOI: 10.1021/Bi9529317  1
1996 Oliveberg M, Fersht AR. Thermodynamics of transient conformations in the folding pathway of barnase: reorganization of the folding intermediate at low pH. Biochemistry. 35: 2738-2749. PMID 8611580 DOI: 10.1021/Bi950967T  1
1996 Oliveberg M, Fersht AR. Formation of electrostatic interactions on the protein-folding pathway. Biochemistry. 35: 2726-2737. PMID 8611579 DOI: 10.1021/Bi9509661  1
1996 Daggett V, Li A, Itzhaki LS, Otzen DE, Fersht AR. Structure of the transition state for folding of a protein derived from experiment and simulation. Journal of Molecular Biology. 257: 430-40. PMID 8609634 DOI: 10.1006/Jmbi.1996.0173  1
1996 Buckle AM, Cramer P, Fersht AR. Structural and energetic responses to cavity-creating mutations in hydrophobic cores: observation of a buried water molecule and the hydrophilic nature of such hydrophobic cavities. Biochemistry. 35: 4298-4305. PMID 8605178 DOI: 10.1021/Bi9524676  1
1996 Zahn R, Perrett S, Stenberg G, Fersht AR. Catalysis of Amide Proton Exchange by the Molecular Chaperones GroEL and SecB Science. 271: 642-645. PMID 8571125 DOI: 10.1126/Science.271.5249.642  1
1996 de Prat Gay G, Ruiz-Sanz J, Neira JL, Corrales FJ, Otzen DE, Ladurner AG, Fersht AR. Conformational pathway of the polypeptide chain of chymotrypsin inhibitor-2 growing from its N terminus in vitro. Parallels with the protein folding pathway. Journal of Molecular Biology. 254: 968-79. PMID 7500364 DOI: 10.1006/Jmbi.1995.0669  0.36
1995 Shaw GL, Davis B, Keeler J, Fersht AR. Backbone dynamics of chymotrypsin inhibitor 2: effect of breaking the active site bond and its implications for the mechanism of inhibition of serine proteases. Biochemistry. 34: 2225-33. PMID 7857934 DOI: 10.1021/Bi00007A017  1
1995 Ruiz-Sanz J, Otzen DE, Fersht AR. Protein fragments as models for events in protein folding pathways: protein engineering analysis of the association of two complementary fragments of the barley chymotrypsin inhibitor 2 (CI-2). Biochemistry. 34: 1695-1701. PMID 7849029 DOI: 10.1021/Bi00005A026  1
1995 Ibba M, Johnson CM, Hennecke H, Fersht AR. Increased rates of tRNA charging through modification of the enzyme-aminoacyl-adenylate complex of phenylalanyl-tRNA synthetase Febs Letters. 358: 293-296. PMID 7843418 DOI: 10.1016/0014-5793(94)01454-9  1
1995 Kippen AD, Fersht AR. Analysis of the mechanism of assembly of cleaved barnase from two peptide fragments and its relevance to the folding pathway of uncleaved barnase. Biochemistry. 34: 1464-1468. PMID 7827095 DOI: 10.1021/Bi00004A042  1
1995 Corrales FJ, Fersht AR. The Folding Of Groel-Bound Barnase As A Model For Chaperonin-Mediated Protein Folding Proceedings of the National Academy of Sciences of the United States of America. 92: 5326-5330. PMID 7777506 DOI: 10.1073/Pnas.92.12.5326  1
1995 Fersht AR. Characterizing transition states in protein folding: an essential step in the puzzle. Current Opinion in Structural Biology. 5: 79-84. PMID 7773750 DOI: 10.1016/0959-440X(95)80012-P  0.01
1995 Fersht AR. Mapping the Structures of Transition States and Intermediates in Folding: Delineation of Pathways at High Resolution Philosophical Transactions of the Royal Society B. 348: 11-15. PMID 7770480 DOI: 10.1098/Rstb.1995.0040  0.01
1995 Matthews JM. Exploring the energy surface of protein folding by structure-reactivity relationships and engineered proteins: Observation of hammond behavior for the gross structure of the transition state and anti-hammond behavior for structural elements for unfolding/folding of barnase Biochemistry®. 34: 6805-6814. PMID 7756312 DOI: 10.1021/Bi00020A027  0.01
1995 Johnson CM. Protein stability as a function of denaturant concentration: The thermal stability of barnase in the presence of urea Biochemistry®. 34: 6795-6804. PMID 7756311 DOI: 10.1021/Bi00020A026  0.01
1995 Ruiz-Sanz J, Neira JL, Itzhaki LS, Fersht AR. Folding of a nascent polypeptide chain in vitro: cooperative formation of structure in a protein module. Proceedings of the National Academy of Sciences of the United States of America. 92: 3683-3686. PMID 7731965 DOI: 10.1073/Pnas.92.9.3683  1
1995 Otzen DE, Fersht AR. Side-chain determinants of beta-sheet stability. Biochemistry. 34: 5718-5724. PMID 7727432 DOI: 10.1021/Bi00017A003  1
1995 Martinez JC, Filimonov VV, Mateo PL, Schreiber G, Fersht AR. A calorimetric study of the thermal stability of barstar and its interaction with barnase. Biochemistry. 34: 5224-5233. PMID 7711042 DOI: 10.1021/Bi00015A036  1
1995 First EA, Fersht AR. Analysis of the role of the KMSKS loop in the catalytic mechanism of the tyrosyl-tRNA synthetase using multimutant cycles. Biochemistry. 34: 5030-5043. PMID 7711024 DOI: 10.1021/Bi00015A014  1
1995 Frisch C, Schreiber G, Fersht AR. Characterization of in vitro oxidized barstar Febs Letters. 370: 273-277. PMID 7656992 DOI: 10.1016/0014-5793(95)00839-2  1
1995 Oliveberg M, Arcus VL, Fersht AR. pKA values of carboxyl groups in the native and denatured states of barnase: the pKA values of the denatured state are on average 0.4 units lower than those of model compounds. Biochemistry. 34: 9424-9433. PMID 7626612 DOI: 10.1021/Bi00029A018  1
1995 Perrett S, Clarke J, Hounslow AM, Fersht AR. Relationship between equilibrium amide proton exchange behavior and the folding pathway of barnase. Biochemistry. 34: 9288-98. PMID 7626599 DOI: 10.1021/Bi00029A003  0.04
1995 Matouschek A, Otzen DE, Itzhaki LS, Jackson SE, Fersht AR. Movement of the position of the transition state in protein folding Biochemistry. 34: 13656-13662. PMID 7577956 DOI: 10.1021/Bi00041A047  1
1995 Otzen DE, Rheinnecker M, Fersht AR. Structural factors contributing to the hydrophobic effect: the partly exposed hydrophobic minicore in chymotrypsin inhibitor 2. Biochemistry. 34: 13051-13058. PMID 7548064 DOI: 10.1021/Bi00040A016  1
1995 Tan Y, Oliveberg M, Davis B, Fersht AR. Perturbed pKA-values in the denatured states of proteins. Journal of Molecular Biology. 254: 980-992. PMID 7500365 DOI: 10.1006/Jmbi.1995.0670  1
1995 Arcus VL, Vuilleumier S, Freund SMV, Bycroft M, Fersht AR. A Comparison of the pH, Urea, and Temperature-denatured States of Barnase by Heteronuclear NMR: Implications for the Initiation of Protein Folding Journal of Molecular Biology. 254: 305-321. PMID 7490750 DOI: 10.1006/Jmbi.1995.0618  1
1995 Itzhaki LS, Neira JL, Ruiz-Sanz J, Fersht AR. Search for nucleation sites in smaller fragments of chymotrypsin inhibitor 2. Journal of Molecular Biology. 254: 289-304. PMID 7490749 DOI: 10.1006/Jmbi.1995.0617  1
1995 Itzhaki LS, Otzen DE, Fersht AR. The Structure of the Transition State for Folding of Chymotrypsin Inhibitor 2 Analysed by Protein Engineering Methods: Evidence for a Nucleation-condensation Mechanism for Protein Folding Journal of Molecular Biology. 254: 260-288. PMID 7490748 DOI: 10.1006/Jmbi.1995.0616  1
1995 Nölting B, Golbik R, Fersht AR. Submillisecond events in protein folding Proceedings of the National Academy of Sciences of the United States of America. 92: 10668-10672. PMID 7479862 DOI: 10.1073/Pnas.92.23.10668  1
1995 Eder J, Fersht AR. Pro-sequence-assisted protein folding Molecular Microbiology. 16: 609-614. PMID 7476156 DOI: 10.1111/J.1365-2958.1995.Tb02423.X  1
1995 Clarke J, Hounslow AM, Fersht AR. Disulfide mutants of barnase. II: Changes in structure and local stability identified by hydrogen exchange. Journal of Molecular Biology. 253: 505-13. PMID 7473730 DOI: 10.1006/Jmbi.1995.0569  0.08
1995 Clarke J, Henrick K, Fersht AR. Disulfide mutants of barnase. I: Changes in stability and structure assessed by biophysical methods and X-ray crystallography. Journal of Molecular Biology. 253: 493-504. PMID 7473729 DOI: 10.1006/Jmbi.1995.0568  0.01
1994 Chen YW, Fersht AR, Henrick K. Crystallographic analysis of Phe-->Leu substitution in the hydrophobic core of barnase. Acta Crystallographica Section D-Biological Crystallography. 51: 220-231. PMID 15299323 DOI: 10.1107/S0907444994008851  1
1994 Rheinnecker M, Eder J, Pandey PS, Fersht AR. Variants of subtilisin BPN' with altered specificity profiles. Biochemistry. 33: 221-225. PMID 8286344 DOI: 10.1021/Bi00167A029  1
1994 Harpaz Y, Elmasry N, Fersht AR, Henrick K. Direct observation of better hydration at the N terminus of an alpha-helix with glycine rather than alanine as the N-cap residue Proceedings of the National Academy of Sciences of the United States of America. 91: 311-315. PMID 8278384 DOI: 10.1073/Pnas.91.1.311  1
1994 Buckle AM, Henrick K, Fersht AR. Crystal structural analysis of mutations in the hydrophobic cores of barnase Journal of Molecular Biology. 234: 847-860. PMID 8254677 DOI: 10.1006/Jmbi.1993.1630  1
1994 Jasanoff A, Davis B, Fersht AR. Detection of an intermediate in the folding of the (beta alpha)8-barrel N-(5'-phosphoribosyl)anthranilate isomerase from Escherichia coli. Biochemistry. 33: 6350-5. PMID 8193151 DOI: 10.1021/Bi00186A039  1
1994 Sanz JM, Fersht AR. Measurement of barnase refolding rate constants under denaturing conditions Febs Letters. 344: 216-220. PMID 8187887 DOI: 10.1016/0014-5793(94)00384-X  1
1994 Vuilleumier S, Fersht AR. Insertion in barnase of a loop sequence from ribonuclease T1. Investigating sequence and structure alignments by protein engineering. Febs Journal. 221: 1003-1012. PMID 8181455 DOI: 10.1111/J.1432-1033.1994.Tb18817.X  1
1994 Martinez JC, Harrous ME, Filimonov VV, Mateo PL, Fersht AR. A calorimetric study of the thermal stability of barnase and its interaction with 3'GMP. Biochemistry. 33: 3919-3926. PMID 8142395 DOI: 10.1021/Bi00179A018  1
1994 Kippen AD, Sancho J, Fersht AR. Folding of barnase in parts. Biochemistry. 33: 3778-3786. PMID 8142379 DOI: 10.1021/Bi00178A039  1
1994 Jasanoff A, Fersht AR. Quantitative determination of helical propensities from trifluoroethanol titration curves. Biochemistry. 33: 2129-35. PMID 8117669 DOI: 10.1021/Bi00174A020  1
1994 Buckle AM, Fersht AR. Subsite Binding in an RNase: Structure of a Barnase-Tetranucleotide Complex at 1.76-A Resolution Biochemistry. 33: 1644-1653. PMID 8110767 DOI: 10.1021/Bi00173A005  1
1994 Kippen AD, Arcus VL, Fersht AR. Structural studies on peptides corresponding to mutants of the major alpha-helix of barnase. Biochemistry. 33: 10013-10021. PMID 8060969 DOI: 10.1021/Bi00199A027  1
1994 Buckle AM, Schreiber G, Fersht AR. Protein-Protein Recognition : Crystal Structural Analysis Of A Barnase-Barstar Complex At 2.0-A Resolution Biochemistry. 33: 8878-8889. PMID 8043575 DOI: 10.1021/Bi00196A004  1
1994 Oliveberg M, Vuilleumier S, Fersht AR. Thermodynamic study of the acid denaturation of barnase and its dependence on ionic strength: evidence for residual electrostatic interactions in the acid/thermally denatured state. Biochemistry. 33: 8826-8832. PMID 8038174 DOI: 10.1021/Bi00195A026  1
1994 Yu WC, Fersht AR. Stability and solvation of Thr/Ser to Ala and Gly mutations at the N-cap of α-helices Febs Letters. 347: 304-309. PMID 8034023 DOI: 10.1016/0014-5793(94)00574-5  1
1994 Ruiz-Sanz J, Fersht AR. Generation of a family of protein fragments for structure-folding studies. 2. Kinetics of association of the two chymotrypsin inhibitor-2 fragments. Biochemistry. 33: 7964-7970. PMID 8011659 DOI: 10.1021/Bi00191A025  1
1994 Fersht AR. Generation of a family of protein fragments for structure-folding studies. 1. Folding complementation of two fragments of chymotrypsin inhibitor-2 formed by cleavage at its unique methionine residue. Biochemistry. 33: 7957-7963. PMID 8011658 DOI: 10.1021/Bi00191A024  0.01
1994 Ruiz-Sanz J, Davis B, Fersht AR. The structure of the transition state for the association of two fragments of the barley chymotrypsin inhibitor 2 to generate native-like protein: implications for mechanisms of protein folding. Proceedings of the National Academy of Sciences of the United States of America. 91: 10943-10946. PMID 7971988 DOI: 10.1073/Pnas.91.23.10943  1
1994 Fersht AR. Pathway and Stability of Protein Folding Biochemical Society Transactions. 22: 267-273. PMID 7958305 DOI: 10.1042/Bst0220267  0.01
1994 Jackson SE, Fersht AR. Contribution of residues in the reactive site loop of chymotrypsin inhibitor 2 to protein stability and activity Biochemistry. 33: 13880-13887. PMID 7947796 DOI: 10.1021/Bi00250A042  1
1994 Arcus VL, Vuilleumier S, Freund SMV, Bycroft M, Fersht AR. Toward solving the folding pathway of barnase: the complete backbone 13C, 15N, and 1H NMR assignments of its pH-denatured state Proceedings of the National Academy of Sciences of the United States of America. 91: 9412-9416. PMID 7937780 DOI: 10.1073/Pnas.91.20.9412  1
1994 elMasry NF, Fersht AR. Mutational analysis of the N-capping box of the α-helix of chymotrypsin inhibitor 2 Protein Engineering. 7: 777-782. PMID 7937708 DOI: 10.1093/Protein/7.6.777  0.01
1994 Johnson CM, Fersht AR. Contribution of a proline residue and a salt bridge to the stability of a type I reverse turn in chymotrypsin inhibitor-2 Protein Engineering. 7: 103-108. PMID 7908135 DOI: 10.1093/Protein/7.1.103  1
1994 Schreiber G, Buckle AM, Fersht AR. Stability and function: two constraints in the evolution of barstar and other proteins Structure. 2: 945-951. PMID 7866746 DOI: 10.1016/S0969-2126(94)00096-4  1
1994 Matouschek A, Matthews JM, Johnson CM, Fersht AR. Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions Protein Engineering, Design and Selection. 7: 1089-1095. PMID 7831279 DOI: 10.1093/Protein/7.9.1089  1
1994 Sanz JM, Johnson CM, Fersht AR. The A-state of barnase. Biochemistry. 33: 11189-11199. PMID 7727370 DOI: 10.1021/Bi00203A015  1
1994 Lubienski MJ, Bycroft M, Freund SMV, Fersht AR. Three-dimensional solution structure and 13C assignments of barstar using nuclear magnetic resonance spectroscopy. Biochemistry. 33: 8866-8877. DOI: 10.2210/Pdb1Bta/Pdb  1
1993 Fersht AR. Protein folding and stability: the pathway of folding of barnase Febs Letters. 325: 5-16. PMID 8513892 DOI: 10.1016/0014-5793(93)81405-O  0.01
1993 Avis JM, Fersht AR. Use of binding energy in catalysis: optimization of rate in a multistep reaction. Biochemistry. 32: 5321-6. PMID 8499436 DOI: 10.1021/Bi00071A006  1
1993 Avis JM, Day AG, Garcia GA, Fersht AR. Reaction of modified and unmodified tRNATyr substrates with tyrosyl-tRNA synthetase (Bacillus stearothermophilus) Biochemistry. 32: 5312-5320. PMID 8499435 DOI: 10.1021/Bi00071A005  1
1993 Schreiber G, Fersht AR. Interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering. Biochemistry. 32: 5145-5150. PMID 8494892 DOI: 10.1021/Bi00070A025  1
1993 Day AG, Chene P, Fersht AR. Role of phenylalanine-327 in the closure of loop 6 of ribulosebisphosphate carboxylase/oxygenase from Rhodospirillum rubrum. Biochemistry. 32: 1940-1944. PMID 8448152 DOI: 10.1021/Bi00059A009  1
1993 Rheinnecker M, Baker G, Eder J, Fersht AR. Engineering a novel specificity in subtilisin BPN Biochemistry. 32: 1199-1203. PMID 8448130 DOI: 10.1021/Bi00056A001  1
1993 de Prat Gay G, Duckworth HW, Fersht AR. Modification of the amino acid specificity of tyrosyl-tRNA synthetase by protein engineering. Febs Letters. 318: 167-71. PMID 8440372 DOI: 10.1016/0014-5793(93)80014-L  0.01
1993 Eder J, Rheinnecker M, Fersht AR. Folding of subtilisin BPN': characterization of a folding intermediate Biochemistry. 32: 18-26. PMID 8418836 DOI: 10.1021/Bi00052A004  1
1993 Lubienski MJ, Bycroft M, Jones DNM, Fersht AR. Assignment of the backbone 1H and 15N NMR resonances and secondary structure characterization of barstar. Febs Letters. 332: 81-87. PMID 8405454 DOI: 10.1016/0014-5793(93)80489-H  1
1993 Jones DNM, Bycroft M, Lubienski MJ, Fersht AR. Identification of the barstar binding site of barnase by NMR spectroscopy and hydrogen‐deuterium exchange Febs Letters. 331: 165-172. PMID 8405399 DOI: 10.1016/0014-5793(93)80319-P  1
1993 Vuilleumier S, Sancho J, Loewenthal R, Fersht AR. Circular Dichroism Studies of Barnase and Its Mutants: Characterization of the Contribution of Aromatic Side Chains Biochemistry. 32: 10303-10313. PMID 8399173 DOI: 10.1021/Bi00090A005  1
1993 Serrano L, Day AG, Fersht AR. Step-wise mutation of barnase to binase. A procedure for engineering increased stability of proteins and an experimental analysis of the evolution of protein stability. Journal of Molecular Biology. 233: 305-12. PMID 8377205 DOI: 10.1006/Jmbi.1993.1508  0.01
1993 Eder J, Rheinnecker M, Fersht AR. Folding of subtilisin BPN': role of the pro-sequence. Journal of Molecular Biology. 233: 293-304. PMID 8377204 DOI: 10.1006/Jmbi.1993.1507  1
1993 Matouschek A, Fersht AR. Application of physical organic chemistry to engineered mutants of proteins: Hammond postulate behavior in the transition state of protein folding. Proceedings of the National Academy of Sciences of the United States of America. 90: 7814-7818. PMID 8356089 DOI: 10.1073/Pnas.90.16.7814  1
1993 Loewenthal R, Sancho J, Reinikainen T, Fersht AR. Long-range surface charge-charge interactions in proteins. Comparison of experimental results with calculations from a theoretical method. Journal of Molecular Biology. 232: 574-583. PMID 8345524 DOI: 10.1006/Jmbi.1993.1412  1
1993 Jackson SE, Fersht AR. Contribution of long-range electrostatic interactions to the stabilization of the catalytic transition state of the serine protease subtilisin BPN' Biochemistry. 32: 13909-13916. PMID 8268166 DOI: 10.1021/Bi00213A021  1
1993 Chen YW, Fersht AR, Henrick K. Contribution of buried hydrogen bonds to protein stability. The crystal structures of two barnase mutants Journal of Molecular Biology. 234: 1158-1170. PMID 8263918 DOI: 10.1006/Jmbi.1993.1667  1
1993 Eder J, Rheinnecker M, Fersht AR. Hydrolysis of small peptide substrates parallels binding of chymotrypsin inhibitor 2 for mutants of subtilisin BPN' Febs Letters. 335: 349-352. PMID 8262182 DOI: 10.1016/0014-5793(93)80417-S  1
1993 First EA, Fersht AR. Mutational and kinetic analysis of a mobile loop in tyrosyl-tRNA synthetase. Biochemistry. 32: 13658-13663. PMID 8257699 DOI: 10.1021/Bi00212A034  1
1993 First EA, Fersht AR. Mutation of lysine 233 to alanine introduces positive cooperativity into tyrosyl-tRNA synthetase. Biochemistry. 32: 13651-13657. PMID 8257698 DOI: 10.1021/Bi00212A033  1
1993 First EA, Fersht AR. Involvement of threonine 234 in catalysis of tyrosyl adenylate formation by tyrosyl-tRNA synthetase Biochemistry. 32: 13644-13650. PMID 8257697 DOI: 10.1021/Bi00212A032  1
1993 Sanz JM, Fersht AR. Rationally designing the accumulation of a folding intermediate of barnase by protein engineering. Biochemistry. 32: 13584-13592. PMID 8257694 DOI: 10.1021/Bi00212A026  1
1993 Clarke J, Hounslow AM, Bycroft M, Fersht AR. Local breathing and global unfolding in hydrogen exchange of barnase and its relationship to protein folding pathways. Proceedings of the National Academy of Sciences of the United States of America. 90: 9837-41. PMID 8234322 DOI: 10.1073/Pnas.90.21.9837  0.08
1993 Jackson SE, ElMasry N, Fersht AR. Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: A critical test of the protein engineering method of analysis Biochemistry. 32: 11270-11278. PMID 8218192 DOI: 10.1021/Bi00093A002  1
1993 Jackson SE, Moracci M, elMasry N, Johnson CM, Fersht AR. Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2. Biochemistry. 32: 11259-11269. PMID 8218191 DOI: 10.1021/Bi00093A001  1
1993 Schreiber G, Fersht AR. The refolding of cis- and trans-peptidylprolyl isomers of barstar Biochemistry. 32: 11195-11203. PMID 8218183 DOI: 10.1021/Bi00092A032  1
1993 Meiering EM, Bycroft M, Lubienski MJ, Fersht AR. Structure and dynamics of barnase complexed with 3'-GMP studied by NMR spectroscopy Biochemistry. 32: 10975-10987. PMID 8218163 DOI: 10.1021/Bi00092A006  1
1993 Gray TE, Fersht AR. Refolding of barnase in the presence of GroE. Journal of Molecular Biology. 232: 1197-1207. PMID 8103803 DOI: 10.1006/Jmbi.1993.1471  1
1993 Fersht AR, Jackson SE, Serrano L. Protein stability : experimental data from protein engineering Philosophical Transactions of the Royal Society A. 345: 141-151. DOI: 10.1098/Rsta.1993.0125  1
1993 Fersht AR, Serrano L. Principles of protein stability derived from protein engineering experiments Current Opinion in Structural Biology. 3: 75-83. DOI: 10.1016/0959-440X(93)90205-Y  0.01
1993 Gray TE, Eder J, Bycroft M, Day AG, Fersht AR. Refolding of barnase mutants and pro-barnase in the presence and absence of GroEL. The Embo Journal. 12: 4145-4150. DOI: 10.1002/J.1460-2075.1993.Tb06098.X  1
1992 Willaert K, Loewenthal R, Sancho J, Froeyen M, Fersht A, Engelborghs Y. Determination of the excited-state lifetimes of the tryptophan residues in barnase, via multifrequency phase fluorometry of tryptophan mutants. Biochemistry. 31: 711-716. PMID 1731927 DOI: 10.1021/Bi00118A011  1
1992 Serrano L, Matouschek A, Fersht AR. The folding of an enzyme. VI. The folding pathway of barnase: comparison with theoretical models. Journal of Molecular Biology. 224: 847-59. PMID 1569561 DOI: 10.1016/0022-2836(92)90566-3  0.12
1992 Serrano L, Kellis JT, Cann P, Matouschek A, Fersht AR. The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. Journal of Molecular Biology. 224: 783-804. PMID 1569557 DOI: 10.1016/0022-2836(92)90562-X  0.01
1992 Sancho J, Fersht AR. Dissection of an enzyme by protein engineering. The N and C-terminal fragments of barnase form a native-like complex with restored enzymic activity. Journal of Molecular Biology. 224: 741-747. PMID 1569553 DOI: 10.1016/0022-2836(92)90558-2  1
1992 Serrano L, Neira JL, Sancho J, Fersht AR. Effect of alanine versus glycine in alpha-helices on protein stability. Nature. 356: 453-5. PMID 1557131 DOI: 10.1038/356453A0  0.04
1992 Sancho J, Serrano L, Fersht AR. Histidine residues at the N- and C-termini of alpha-helices: perturbed pKas and protein stability. Biochemistry. 31: 2253-8. PMID 1540580 DOI: 10.1021/Bi00123A006  0.01
1992 Serrano L, Sancho J, Hirshberg M, Fersht AR. Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. Journal of Molecular Biology. 227: 544-59. PMID 1404368 DOI: 10.1016/0022-2836(92)90906-Z  0.01
1991 Loewenthal R, Sancho J, Fersht AR. Fluorescence spectrum of barnase: contributions of three tryptophan residues and a histidine-related pH dependence. Biochemistry. 30: 6775-6779. PMID 2065058 DOI: 10.1021/Bi00241A021  1
1991 Fothergill MD, Fersht AR. Correlations between kinetic and X-ray analyses of engineered enzymes: crystal structures of mutants Cys----Gly-35 and Tyr----Phe-34 of tyrosyl-tRNA synthetase. Biochemistry. 30: 5157-5164. PMID 2036381 DOI: 10.1021/Bi00235A007  0.01
1991 Horovitz A, Serrano L, Fersht AR. COSMIC analysis of the major α-helix of barnase during folding Journal of Molecular Biology. 219: 5-9. PMID 2023260 DOI: 10.1016/0022-2836(91)90852-W  1
1991 Serrano L, Bycroft M, Fersht AR. Aromatic-aromatic interactions and protein stability. Investigation by double-mutant cycles. Journal of Molecular Biology. 218: 465-75. PMID 2010920 DOI: 10.1016/0022-2836(91)90725-L  0.2
1991 Meiering EM, Bycroft M, Fersht AR. Characterization of phosphate binding in the active site of barnase by site-directed mutagenesis and NMR. Biochemistry. 30: 11348-11356. PMID 1958671 DOI: 10.1021/Bi00111A022  1
1991 Jackson SE, Fersht AR. Folding of chymotrypsin inhibitor 2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding Biochemistry. 30: 10436-10443. PMID 1931968 DOI: 10.1021/Bi00107A011  1
1991 Bycroft M, Ludvigsen S, Fersht AR, Poulsen FM. Determination of the three-dimensional solution structure of barnase using nuclear magnetic resonance spectroscopy. Biochemistry. 30: 8697-701. PMID 1888730 DOI: 10.1021/Bi00099A030  0.08
1991 Fersht AR. Surface electrostatic interactions contribute little to stability of barnase Journal of Molecular Biology. 220: 779-788. PMID 1870131 DOI: 10.1016/0022-2836(91)90117-O  1
1991 Fersht AR, Wells TNC. Linear free energy relationships in enzyme binding interactions studied by protein engineering. Protein Engineering. 4: 229-231. PMID 1857710 DOI: 10.1093/Protein/4.3.229  1
1991 Matouschek AT, Fersht AR. Protein engineering in analysis of protein folding pathways and stability Methods in Enzymology. 202: 82-112. PMID 1784198 DOI: 10.1016/0076-6879(91)02008-W  1
1991 Fersht AR, Bycroft M, Horovitz A, Kellis JT, Matouschek A, Serrano L. Pathway and stability of protein folding Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences. 332: 171-176. PMID 1678536 DOI: 10.1098/Rstb.1991.0046  1
1991 Sancho J, Meiering EM, Fersht AR. Mapping transition states of protein unfolding by protein engineering of ligand-binding sites. Journal of Molecular Biology. 221: 1007-1014. PMID 1658330 DOI: 10.1016/0022-2836(91)80188-Z  1
1991 Wells TNC, Knill-Jones JW, Gray TE, Fersht AR. Kinetic and thermodynamic properties of wild-type and engineered mutants of tyrosyl-tRNA synthetase analyzed by pyrophosphate-exchange kinetics. Biochemistry. 30: 5151-5156. PMID 1645192 DOI: 10.1021/Bi00235A006  1
1991 Fersht AR, Matouschek AT, Bycroft M, Kellis JT, Serrano L. Physical-Organic Molecular Biology : Pathway And Stability Of Protein Folding Pure and Applied Chemistry. 63: 187-194. DOI: 10.1351/Pac199163020187  1
1990 Horovitz A, Fersht AR. Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins Journal of Molecular Biology. 214: 613-617. PMID 2388258 DOI: 10.1016/0022-2836(90)90275-Q  1
1990 Bycroft M, Matouschek AT, Kellis JT, Serrano L, Fersht AR. Detection and characterization of a folding intermediate in barnase by NMR Nature. 346: 488-490. PMID 2377210 DOI: 10.1038/346488A0  1
1990 Garcia GA, Leatherbarrow RJ, Eckstein F, Fersht AR. Metal ion dependence of phosphorothioate ATP analogues in the Bacillus stearothermophilus tyrosyl-tRNA synthetase reaction Biochemistry. 29: 1643-1648. PMID 2334722 DOI: 10.1021/Bi00458A041  1
1990 Horovitz A, Serrano L, Avron B, Bycroft M, Fersht AR. Strength and co-operativity of contributions of surface salt bridges to protein stability Journal of Molecular Biology. 216: 1031-1044. PMID 2266554 DOI: 10.1016/S0022-2836(99)80018-7  1
1990 Serrano L, Horovitz A, Avron B, Bycroft M, Fersht AR. Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles Biochemistry®. 29: 9343-9352. PMID 2248951 DOI: 10.1021/Bi00492A006  1
1990 Bycroft M, Sheppard RN, Lau FTK, Fersht AR. Sequential assignment of the 1H nuclear magnetic resonance spectrum of barnase. Biochemistry. 29: 7425-7432. PMID 2223774 DOI: 10.1021/Bi00484A011  1
1990 Longstaff C, Campbell AF, Fersht AR. Recombinant chymotrypsin inhibitor 2: expression, kinetic analysis of inhibition with alpha-chymotrypsin and wild-type and mutant subtilisin BPN', and protein engineering to investigate inhibitory specificity and mechanism. Biochemistry. 29: 7339-47. PMID 2207109 DOI: 10.1021/Bi00483A025  0.01
1990 Ward WHJ, Timms D, Fersht AR. Protein engineering and the study of structure—function relationships in receptors Trends in Pharmacological Sciences. 11: 280-284. PMID 2202140 DOI: 10.1016/0165-6147(90)90009-W  1
1990 Fersht AR, Kellis JT, Matouschek AT, Serrano L. Folding pathway enigma Nature. 343: 602-602. DOI: 10.1038/343602A0  1
1989 Serrano L, Fersht AR. Capping and alpha-helix stability. Nature. 342: 296-9. PMID 2812029 DOI: 10.1038/342296A0  0.04
1989 Wells TNC, Fersht AR. Protection of an unstable reaction intermediate examined with linear free energy relationships in tyrosyl-tRNA synthetase. Biochemistry. 28: 9201-9209. PMID 2690955 DOI: 10.1021/Bi00449A036  1
1989 Kellis JT, Nyberg K, Fersht AR. Energetics of complementary side-chain packing in a protein hydrophobic core. Biochemistry. 28: 4914-4922. PMID 2669964 DOI: 10.1021/Bi00437A058  1
1989 Mossakowska DE, Nyberg K, Fersht AR. Kinetic characterization of the recombinant ribonuclease from Bacillus amyloliquefaciens (barnase) and investigation of key residues in catalysis by site-directed mutagenesis. Biochemistry. 28: 3843-3850. PMID 2665810 DOI: 10.1021/Bi00435A033  1
1989 Fersht AR, Sternberg MJE. Can a simple function for the dielectric response model electrostatic effects in globular proteins Protein Engineering. 2: 527-530. PMID 2664761 DOI: 10.1093/Protein/2.7.527  0.01
1989 Lau FTK, Fersht AR. Dissection of the effector-binding site and complementation studies of Escherichia coli phosphofructokinase using site-directed mutagenesis. Biochemistry. 28: 6841-6847. PMID 2531002 DOI: 10.1021/Bi00443A010  1
1988 Ward WHJ, Fersht AR. Asymmetry of tyrosyl-tRNA synthetase in solution. Biochemistry. 27: 1041-1049. PMID 3365365 DOI: 10.1021/Bi00403A029  1
1988 Ward WHJ, Fersht AR. Tyrosyl-tRNA synthetase acts as an asymmetric dimer in charging tRNA. A rationale for half-of-the-sites activity. Biochemistry. 27: 5525-5530. PMID 3179266 DOI: 10.1021/Bi00415A021  1
1988 Bycroft M, Fersht AR. Assignment of histidine resonances in the 1H NMR (500 MHz) spectrum of subtilisin BPN' using site-directed mutagenesis. Biochemistry. 27: 7390-7394. PMID 3061456 DOI: 10.1021/Bi00419A033  1
1987 Lowe DM, Winter G, Fersht AR. Structure-activity relationships in engineered proteins: characterization of disruptive deletions in the alpha-ammonium group binding site of tyrosyl-tRNA synthetase. Biochemistry. 26: 6038-6043. PMID 3480006 DOI: 10.1021/Bi00393A014  1
1987 Fersht AR, Leatherbarrow RJ, Wells TNC. Structure-activity relationships in engineered proteins: Analysis of use of binding energy by linear free energy relationships Biochemistry. 26: 6030-6038. PMID 3480005 DOI: 10.1021/Bi00393A013  1
1987 Borgford TJ, Gray TE, Brand NJ, Fersht AR. Site-directed mutagenesis reveals transition-state stabilization as a general catalytic mechanism for aminoacyl-tRNA synthetases. Biochemistry. 26: 7246-7250. PMID 3427072 DOI: 10.1021/Bi00397A008  1
1987 Leatherbarrow RJ, Fersht AR. Investigation of transition-state stabilization by residues histidine-45 and threonine-40 in the tyrosyl-tRNA synthetase Biochemistry. 26: 8524-8528. PMID 3126804 DOI: 10.1021/Bi00400A005  1
1987 Fersht AR. Concluding comment:–Fersht Protein Engineering Design & Selection. 1: 446-446. DOI: 10.1093/Protein/1.6.446  0.01
1986 Wells TNC, Fersht AR. Use of binding energy in catalysis analyzed by mutagenesis of the tyrosyl-tRNA synthetase Biochemistry. 25: 1881-1886. PMID 3518794 DOI: 10.1021/Bi00356A007  1
1986 Wells TNC, Ho CK, Fersht AR. Free energy of hydrolysis of tyrosyl adenylate and its binding to wild-type and engineered mutant tyrosyl-tRNA synthetases. Biochemistry. 25: 6603-6608. PMID 3466647 DOI: 10.1021/Bi00369A040  1
1986 Leatherbarrow RJ, Fersht AR. Protein engineering. Protein Engineering. 1: 7-16. PMID 3333843  1
1985 Leatherbarrow RJ, Fersht AR, Winter G. Transition-state stabilization in the mechanism of tyrosyl-tRNA synthetase revealed by protein engineering. Proceedings of the National Academy of Sciences of the United States of America. 82: 7840-4. PMID 3865201 DOI: 10.1073/Pnas.82.23.7840  1
1985 Fersht AR, Wilkinson AJ, Carter P, Winter G. Fine structure-activity analysis of mutations at position 51 of tyrosyl-tRNA synthetase Biochemistry. 24: 5858-5861. PMID 3002425 DOI: 10.1021/Bi00342A025  1
1984 FERSHT AR, SHI J, WILKINSON AJ, BLOW DM, CARTER P, WAYE MMY, WINTER GP. ChemInform Abstract: ANALYSIS OF STRUCTURE-ACTIVITY RELATIONS IN ENZYMES USING PROTEIN ENGINEERING Chemischer Informationsdienst. 15. DOI: 10.1002/Chin.198444371  0.01
1983 Wilkinson AJ, Fersht AR, Blow DM, Winter G. Site-directed mutagenesis as a probe of enzyme structure and catalysis: tyrosyl-tRNA synthetase cysteine-35 to glycine-35 mutation. Biochemistry. 22: 3581-6. PMID 6615786 DOI: 10.1021/Bi00284A007  1
1983 Waye MM, Winter G, Wilkinson AJ, Fersht AR. Deletion mutagenesis using an 'M13 splint': the N-terminal structural domain of tyrosyl-tRNA synthetase (B. stearothermophilus) catalyses the formation of tyrosyl adenylate. The Embo Journal. 2: 1827-9. PMID 6315404 DOI: 10.1002/J.1460-2075.1983.Tb01665.X  1
1983 Cotterill SM, Fersht AR. Direct observation of complexes of ssb and recA proteins with a fluorescent single-stranded deoxyribonucleic acid derivative. Biochemistry. 22: 5878-5881. PMID 6229277 DOI: 10.1021/Bi00294A029  1
1983 Silver MS, Fersht AR. Investigation of binding between recA protein and single-stranded polynucleotides with the aid of a fluorescent deoxyribonucleic acid derivative Biochemistry. 22: 2860-2866. PMID 6223658 DOI: 10.1021/Bi00281A014  1
1983 Cotterill SM, Fersht AR. recA Filaments in solution Biochemistry. 22: 3525-3531. DOI: 10.1021/Bi00283A034  1
1982 Silver MS, Fersht AR. Direct observation of complexes formed between recA protein and a fluorescent single-stranded deoxyribonucleic acid derivative Biochemistry. 21: 6066-6072. PMID 6758843 DOI: 10.1021/Bi00267A007  1
1982 Cotterill SM, Satterthwait AC, Fersht AR. recA protein from Escherichia coli. a very rapid and simple purification procedure: binding of adenosine 5'-triphosphate and adenosine 5'-diphosphate by the homogeneous protein. Biochemistry. 21: 4332-4337. PMID 6751387 DOI: 10.1021/Bi00261A023  1
1981 Fersht AR, Knill-Jones JW. DNA polymerase accuracy and spontaneous mutation rates: frequencies of purine.purine, purine.pyrimidine, and pyrimidine.pyrimidine mismatches during DNA replication Proceedings of the National Academy of Sciences of the United States of America. 78: 4251-4255. PMID 6457301 DOI: 10.1073/Pnas.78.7.4251  1
1980 Fersht AR, Shindler JS, Tsui W. Probing the limits of protein-amino acid side chain recognition with the aminoacyl-tRNA synthetases. Discrimination against phenylalanine by tyrosyl-tRNA synthetases. Biochemistry. 19: 5520-5524. PMID 7006687 DOI: 10.1021/Bi00565A009  0.01
1978 Mulvey RS, Fersht AR. Mechanism of aminoacylation of transfer RNA. A pre-steady-state analysis of the reaction pathway catalyzed by the methionyl-tRNA synthetase of Bacillus stearothermophilus. Biochemistry. 17: 5591-5597. PMID 728419 DOI: 10.1021/Bi00619A002  1
1978 Fersht AR, Gangloff J, Dirheimer G. Reaction pathway and rate-determining step in the aminoacylation of tRNAArg catalyzed by the arginyl-tRNA synthetase from yeast. Biochemistry. 17: 3740-3746. PMID 359044 DOI: 10.1021/Bi00611A011  0.01
1978 Danson MJ, Fersht AR, Perham RN. Rapid intramolecular coupling of active sites in the pyruvate dehydrogenase complex of Escherichia coli: mechanism for rate enhancement in a multimeric structure. Proceedings of the National Academy of Sciences of the United States of America. 75: 5386-90. PMID 214786 DOI: 10.1073/Pnas.75.11.5386  0.04
1977 Fersht AR. Editing mechanisms in protein synthesis. Rejection of valine by the isoleucyl-tRNA synthetase. Biochemistry. 16: 1025-1030. PMID 321008 DOI: 10.1021/Bi00624A034  0.01
1977 Mulvey RS, Fersht AR. Editing mechanisms in aminoacylation of tRNA:ATP consumption and the binding of aminoacyl-tRNA by elongation factor Tu Biochemistry. 16: 4731-4737. PMID 242929 DOI: 10.1021/Bi00640A031  1
1977 Mulvey RS, Fersht AR. Ligand binding stoichiometries, subunit structure, and slow transitions in aminoacyl-tRNA synthetases. Biochemistry. 16: 4005-4013. PMID 199234 DOI: 10.1021/Bi00637A011  1
1976 Mulvey RS, Fersht AR. Subunit interactions in the methionyl-tRNA synthetase of Bacillus stearothermophilus. Biochemistry. 15: 243-249. PMID 1247516 DOI: 10.1021/Bi00647A001  1
1976 Fersht AR, Kaethner MM. Mechanism of aminoacylation of tRNA. Proof of the aminoacyl adenylate pathway for the isoleucyl- and tyrosyl-tRNA synthetases from Escherichia coli K12 Biochemistry. 15: 818-823. PMID 764868 DOI: 10.1021/Bi00649A014  1
1976 Fersht AR, Kaethner MM. Enzyme hyperspecificity. Rejection of threonine by the valyl-tRNA synthetase by misacylation and hydrolytic editing. Biochemistry. 15: 3342-3346. PMID 182209 DOI: 10.1021/Bi00660A026  1
1975 Fersht AR. Demonstration of two active sites on a monomeric aminoacyl-tRNA synthetase. Possible roles of negative cooperativity and half-of-the-sites reactivity in oligomeric enzymes. Biochemistry. 14: 5-12. PMID 1109589 DOI: 10.1021/Bi00672A002  0.01
1975 Fersht AR, Ashford JS, Bruton CJ, Jakes R, Koch GL, Hartley BS. Active site titration and aminoacyl adenylate binding stoichiometry of aminoacyl-tRNA synthetases. Biochemistry. 14: 1-4. PMID 1109585 DOI: 10.1021/Bi00672A001  1
1975 Fersht AR, Jakes R. Demonstration of two reaction pathways for the aminoacylation of tRNA. Application of the pulsed quenched flow technique. Biochemistry. 14: 3350-3356. PMID 1096942 DOI: 10.1021/Bi00686A010  1
1975 Jakes R, Fersht AR. Tyrosyl-tRNA synthetase from Escherichia coli. Stoichiometry of ligand binding and half-of-the-sites reactivity in aminoacylation. Biochemistry. 14: 3344-3350. PMID 1096941 DOI: 10.1021/Bi00686A009  1
1975 Fersht AR, Mulvey RS, Koch GLE. Ligand binding and enzymic catalysis coupled through subunits in tyrosyl-tRNA synthetase. Biochemistry. 14: 13-18. PMID 162826 DOI: 10.1021/Bi00672A003  1
1974 Perutz MF, Fersht AR, Simon SR, Roberts GCK. Influence of globin structure on the state of the heme. II. Allosteric transitions in methemoglobin Biochemistry. 13: 2174-2186. PMID 4857061 DOI: 10.1021/Bi00707A027  1
1974 Fersht AR, Renard M. pH dependence of chymotrypsin catalysis. Appendix: substrate binding to dimeric alpha-chymotrypsin studied by x-ray diffraction and the equilibrium method. Biochemistry. 13: 1416-1426. PMID 4819756 DOI: 10.1021/Bi00704A016  1
1973 Renard M, Fersht AR. Anomalous pH dependence of kcat-KM in enzyme reactions. Rate constants for the association of chymotrypsin with substrates. Biochemistry. 12: 4713-4718. PMID 4773852 DOI: 10.1021/Bi00747A026  1
1973 Fersht AR, Blow DM, Fastrez J. Leaving group specificity in the chymotrypsin-catalyzed hydrolysis of peptides. A stereochemical interpretation. Biochemistry. 12: 2035-41. PMID 4735878 DOI: 10.1021/Bi00735A002  1
1973 Fastrez J, Fersht AR. Demonstration of the acyl-enzyme mechanism for the hydrolysis of peptides and anilides by chymotrypsin. Biochemistry. 12: 2025-2034. PMID 4705984 DOI: 10.1021/Bi00735A001  1
1973 Fastrez J, Fersht AR. Mechanism of chymotrypsin. Structure, reactivity, and nonproductive binding relations Biochemistry. 12: 1067-1074. PMID 4688860 DOI: 10.1021/Bi00730A008  1
1972 Fersht AR, Requena Y. Mechanismus Der Durch Alpha‐Chymotrypsin Katalysierten Hydrolyse Von Amiden, Ph‐Abhaengigkeit Von K(C) Und K(M) (Michaeliskonstante), Kinetischer Nachweis Eines Intermediaerproduktes Cheminform. 3. DOI: 10.1002/Chin.197208118  1
1971 Fersht AR. Acyl-transfer reactions of amides and esters with alcohols and thiols. A reference system for the serine and cysteine proteinases. Concerning the N protonation of amides and amide-imidate equilibria. Journal of the American Chemical Society. 93: 3504-3515. PMID 5560470 DOI: 10.1021/Ja00743A035  0.01
1971 Fersht AR, Requena Y. Free energies of hydrolysis of amides and peptides in aqueous solution at 25.deg. Journal of the American Chemical Society. 93: 3499-3504. PMID 5560469 DOI: 10.1021/Ja00743A034  1
1971 Fersht AR, Requena Y. Mechanism of the -chymotrypsin-catalyzed hydrolysis of amides. pH dependence of k c and K m . Kinetic detection of an intermediate. Journal of the American Chemical Society. 93: 7079-7087. PMID 5133099 DOI: 10.1021/Ja00754A066  1
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