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Aminobenzothiazole derivatives stabilize the thermolabile p53 cancer mutant Y220C and show anticancer activity in p53-Y220C cell lines.

Baud MGJ, Bauer MR, Verduci L, Dingler FA, Patel KJ, Horil Roy D, Joerger AC, Fersht AR.

Eur J Med Chem. 2018 May 25;152:101-114. doi: 10.1016/j.ejmech.2018.04.035. Epub 2018 Apr 21.


The curcumin analog HO-3867 selectively kills cancer cells by converting mutant p53 protein to transcriptionally active wildtype p53.

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 JJ, Jones LJ, Tomás AR, Cunha AC, Selvendiran K, Hansen LA, Fersht AR, Hideg K, Gogna R, Kuppusamy P.

J Biol Chem. 2018 Mar 23;293(12):4262-4276. doi: 10.1074/jbc.RA117.000950. Epub 2018 Jan 30.


Mutant p53 as a therapeutic target for the treatment of triple-negative breast cancer: Preclinical investigation with the anti-p53 drug, PK11007.

Synnott NC, Bauer MR, Madden S, Murray A, Klinger R, O'Donovan N, O'Connor D, Gallagher WM, Crown J, Fersht AR, Duffy MJ.

Cancer Lett. 2018 Feb 1;414:99-106. doi: 10.1016/j.canlet.2017.09.053. Epub 2017 Oct 22.


Structures of closed and open conformations of dimeric human ATM.

Baretić D, Pollard HK, Fisher DI, Johnson CM, Santhanam B, Truman CM, Kouba T, Fersht AR, Phillips C, Williams RL.

Sci Adv. 2017 May 10;3(5):e1700933. doi: 10.1126/sciadv.1700933. eCollection 2017 May.


Multisite aggregation of p53 and implications for drug rescue.

Wang G, Fersht AR.

Proc Natl Acad Sci U S A. 2017 Mar 28;114(13):E2634-E2643. doi: 10.1073/pnas.1700308114. Epub 2017 Mar 14.


Design of a molecular support for cryo-EM structure determination.

Martin TG, Bharat TA, Joerger AC, Bai XC, Praetorius F, Fersht AR, Dietz H, Scheres SH.

Proc Natl Acad Sci U S A. 2016 Nov 22;113(47):E7456-E7463. Epub 2016 Nov 7.


2-Sulfonylpyrimidines: Mild alkylating agents with anticancer activity toward p53-compromised cells.

Bauer MR, Joerger AC, Fersht AR.

Proc Natl Acad Sci U S A. 2016 Sep 6;113(36):E5271-80. doi: 10.1073/pnas.1610421113. Epub 2016 Aug 22.


An in silico algorithm for identifying stabilizing pockets in proteins: test case, the Y220C mutant of the p53 tumor suppressor protein.

Bromley D, Bauer MR, Fersht AR, Daggett V.

Protein Eng Des Sel. 2016 Sep;29(9):377-90. doi: 10.1093/protein/gzw035. Epub 2016 Aug 8.


Harnessing Fluorine-Sulfur Contacts and Multipolar Interactions for the Design of p53 Mutant Y220C Rescue Drugs.

Bauer MR, Jones RN, Baud MG, Wilcken R, Boeckler FM, Fersht AR, Joerger AC, Spencer J.

ACS Chem Biol. 2016 Aug 19;11(8):2265-74. doi: 10.1021/acschembio.6b00315. Epub 2016 Jun 21.


The p53 Pathway: Origins, Inactivation in Cancer, and Emerging Therapeutic Approaches.

Joerger AC, Fersht AR.

Annu Rev Biochem. 2016 Jun 2;85:375-404. doi: 10.1146/annurev-biochem-060815-014710. Epub 2016 May 4. Review.


Exploiting Transient Protein States for the Design of Small-Molecule Stabilizers of Mutant p53.

Joerger AC, Bauer MR, Wilcken R, Baud MGJ, Harbrecht H, Exner TE, Boeckler FM, Spencer J, Fersht AR.

Structure. 2015 Dec 1;23(12):2246-2255. doi: 10.1016/j.str.2015.10.016.


Experimental and Theoretical Evaluation of the Ethynyl Moiety as a Halogen Bioisostere.

Wilcken R, Zimmermann MO, Bauer MR, Rutherford TJ, Fersht AR, Joerger AC, Boeckler FM.

ACS Chem Biol. 2015 Dec 18;10(12):2725-32. doi: 10.1021/acschembio.5b00515. Epub 2015 Oct 1.


Deconvoluting Protein (Un)folding Structural Ensembles Using X-Ray Scattering, Nuclear Magnetic Resonance Spectroscopy and Molecular Dynamics Simulation.

Nasedkin A, Marcellini M, Religa TL, Freund SM, Menzel A, Fersht AR, Jemth P, van der Spoel D, Davidsson J.

PLoS One. 2015 May 6;10(5):e0125662. doi: 10.1371/journal.pone.0125662. eCollection 2015.


Propagation of aggregated p53: Cross-reaction and coaggregation vs. seeding.

Wang G, Fersht AR.

Proc Natl Acad Sci U S A. 2015 Feb 24;112(8):2443-8. doi: 10.1073/pnas.1500262112. Epub 2015 Feb 9.


Mechanism of initiation of aggregation of p53 revealed by Φ-value analysis.

Wang G, Fersht AR.

Proc Natl Acad Sci U S A. 2015 Feb 24;112(8):2437-42. doi: 10.1073/pnas.1500243112. Epub 2015 Feb 9.


Profile of Martin Karplus, Michael Levitt, and Arieh Warshel, 2013 nobel laureates in chemistry.

Fersht AR.

Proc Natl Acad Sci U S A. 2013 Dec 3;110(49):19656-7. doi: 10.1073/pnas.1320569110. Epub 2013 Nov 25. No abstract available.


MDMX contains an autoinhibitory sequence element.

Bista M, Petrovich M, Fersht AR.

Proc Natl Acad Sci U S A. 2013 Oct 29;110(44):17814-9. doi: 10.1073/pnas.1317398110. Epub 2013 Oct 14.


Reply to Campos and Muñoz: Why phosphate is a bad buffer for guanidinium chloride titrations.

Fersht AR, Petrovich M.

Proc Natl Acad Sci U S A. 2013 Apr 2;110(14):E1244-5. No abstract available.


Small molecule induced reactivation of mutant p53 in cancer cells.

Liu X, Wilcken R, Joerger AC, Chuckowree IS, Amin J, Spencer J, Fersht AR.

Nucleic Acids Res. 2013 Jul;41(12):6034-44. doi: 10.1093/nar/gkt305. Epub 2013 Apr 29.


Don't waste good methods on bad buffers and ambiguous data.

Huang F, Johnson CM, Petrovich M, Fersht AR.

Proc Natl Acad Sci U S A. 2013 Jan 29;110(5):E331-2. doi: 10.1073/pnas.1217840110. Epub 2013 Jan 17. No abstract available.


Evaluating Drosophila p53 as a model system for studying cancer mutations.

Herzog G, Joerger AC, Shmueli MD, Fersht AR, Gazit E, Segal D.

J Biol Chem. 2012 Dec 28;287(53):44330-7. doi: 10.1074/jbc.M112.417980. Epub 2012 Nov 7.


Stability of p53 homologs.

Brandt T, Kaar JL, Fersht AR, Veprintsev DB.

PLoS One. 2012;7(10):e47889. doi: 10.1371/journal.pone.0047889. Epub 2012 Oct 24.


Chemical physics of protein folding.

Wolynes PG, Eaton WA, Fersht AR.

Proc Natl Acad Sci U S A. 2012 Oct 30;109(44):17770-1. doi: 10.1073/pnas.1215733109. Epub 2012 Oct 29. No abstract available.


Lithocholic acid is an endogenous inhibitor of MDM4 and MDM2.

Vogel SM, Bauer MR, Joerger AC, Wilcken R, Brandt T, Veprintsev DB, Rutherford TJ, Fersht AR, Boeckler FM.

Proc Natl Acad Sci U S A. 2012 Oct 16;109(42):16906-10. doi: 10.1073/pnas.1215060109. Epub 2012 Oct 3.


Sequence-dependent sliding kinetics of p53.

Leith JS, Tafvizi A, Huang F, Uspal WE, Doyle PS, Fersht AR, Mirny LA, van Oijen AM.

Proc Natl Acad Sci U S A. 2012 Oct 9;109(41):16552-7. doi: 10.1073/pnas.1120452109. Epub 2012 Sep 25.


Domain-domain interactions in full-length p53 and a specific DNA complex probed by methyl NMR spectroscopy.

Bista M, Freund SM, Fersht AR.

Proc Natl Acad Sci U S A. 2012 Sep 25;109(39):15752-6. Epub 2012 Sep 12.


Kinetic mechanism of p53 oncogenic mutant aggregation and its inhibition.

Wilcken R, Wang G, Boeckler FM, Fersht AR.

Proc Natl Acad Sci U S A. 2012 Aug 21;109(34):13584-9. doi: 10.1073/pnas.1211550109. Epub 2012 Aug 6.


First-order rate-determining aggregation mechanism of p53 and its implications.

Wang G, Fersht AR.

Proc Natl Acad Sci U S A. 2012 Aug 21;109(34):13590-5. doi: 10.1073/pnas.1211557109. Epub 2012 Aug 6.


Intrinsically disordered p53 and its complexes populate compact conformations in the gas phase.

Pagel K, Natan E, Hall Z, Fersht AR, Robinson CV.

Angew Chem Int Ed Engl. 2013 Jan 2;52(1):361-5. doi: 10.1002/anie.201203047. Epub 2012 Jul 9.


Halogen-enriched fragment libraries as leads for drug rescue of mutant p53.

Wilcken R, Liu X, Zimmermann MO, Rutherford TJ, Fersht AR, Joerger AC, Boeckler FM.

J Am Chem Soc. 2012 Apr 18;134(15):6810-8. doi: 10.1021/ja301056a. Epub 2012 Apr 5.


Long-range modulation of chain motions within the intrinsically disordered transactivation domain of tumor suppressor p53.

Lum JK, Neuweiler H, Fersht AR.

J Am Chem Soc. 2012 Jan 25;134(3):1617-22. doi: 10.1021/ja2078619. Epub 2012 Jan 12.


Nonnative interactions in the FF domain folding pathway from an atomic resolution structure of a sparsely populated intermediate: an NMR relaxation dispersion study.

Korzhnev DM, Vernon RM, Religa TL, Hansen AL, Baker D, Fersht AR, Kay LE.

J Am Chem Soc. 2011 Jul 20;133(28):10974-82. doi: 10.1021/ja203686t. Epub 2011 Jun 28.


Combination of Markov state models and kinetic networks for the analysis of molecular dynamics simulations of peptide folding.

Radford IH, Fersht AR, Settanni G.

J Phys Chem B. 2011 Jun 9;115(22):7459-71. doi: 10.1021/jp112158w. Epub 2011 May 9.


Acetylation of lysine 120 of p53 endows DNA-binding specificity at effective physiological salt concentration.

Arbely E, Natan E, Brandt T, Allen MD, Veprintsev DB, Robinson CV, Chin JW, Joerger AC, Fersht AR.

Proc Natl Acad Sci U S A. 2011 May 17;108(20):8251-6. doi: 10.1073/pnas.1105028108. Epub 2011 Apr 27.


Electrocatalytic monitoring of metal binding and mutation-induced conformational changes in p53 at picomole level.

Paleček E, Ostatná V, Černocká H, Joerger AC, Fersht AR.

J Am Chem Soc. 2011 May 11;133(18):7190-6. doi: 10.1021/ja201006s. Epub 2011 Apr 14.


Interaction of the p53 DNA-binding domain with its n-terminal extension modulates the stability of the p53 tetramer.

Natan E, Baloglu C, Pagel K, Freund SM, Morgner N, Robinson CV, Fersht AR, Joerger AC.

J Mol Biol. 2011 Jun 10;409(3):358-68. doi: 10.1016/j.jmb.2011.03.047. Epub 2011 Mar 30.


Malleability of folding intermediates in the homeodomain superfamily.

Banachewicz W, Religa TL, Schaeffer RD, Daggett V, Fersht AR.

Proc Natl Acad Sci U S A. 2011 Apr 5;108(14):5596-601. doi: 10.1073/pnas.1101752108. Epub 2011 Mar 21.


Folding of the Pit1 homeodomain near the speed limit.

Banachewicz W, Johnson CM, Fersht AR.

Proc Natl Acad Sci U S A. 2011 Jan 11;108(2):569-73. doi: 10.1073/pnas.1017832108. Epub 2010 Dec 27.


Electron microscopy studies on the quaternary structure of p53 reveal different binding modes for p53 tetramers in complex with DNA.

Melero R, Rajagopalan S, Lázaro M, Joerger AC, Brandt T, Veprintsev DB, Lasso G, Gil D, Scheres SH, Carazo JM, Fersht AR, Valle M.

Proc Natl Acad Sci U S A. 2011 Jan 11;108(2):557-62. doi: 10.1073/pnas.1015520107. Epub 2010 Dec 22.


A single-molecule characterization of p53 search on DNA.

Tafvizi A, Huang F, Fersht AR, Mirny LA, van Oijen AM.

Proc Natl Acad Sci U S A. 2011 Jan 11;108(2):563-8. doi: 10.1073/pnas.1016020107. Epub 2010 Dec 22.


Time-resolved small-angle X-ray scattering study of the folding dynamics of barnase.

Konuma T, Kimura T, Matsumoto S, Goto Y, Fujisawa T, Fersht AR, Takahashi S.

J Mol Biol. 2011 Feb 4;405(5):1284-94. doi: 10.1016/j.jmb.2010.11.052. Epub 2010 Dec 10.


Kinetics of chain motions within a protein-folding intermediate.

Neuweiler H, Banachewicz W, Fersht AR.

Proc Natl Acad Sci U S A. 2010 Dec 21;107(51):22106-10. doi: 10.1073/pnas.1011666107. Epub 2010 Dec 6.


Single-Molecule characterization of oligomerization kinetics and equilibria of the tumor suppressor p53.

Rajagopalan S, Huang F, Fersht AR.

Nucleic Acids Res. 2011 Mar;39(6):2294-303. doi: 10.1093/nar/gkq800. Epub 2010 Nov 18.


Phosphotriesterase variants with high methylphosphonatase activity and strong negative trade-off against phosphotriesters.

Briseño-Roa L, Timperley CM, Griffiths AD, Fersht AR.

Protein Eng Des Sel. 2011 Jan;24(1-2):151-9. doi: 10.1093/protein/gzq076. Epub 2010 Oct 30.


Stabilization of mutant p53 via alkylation of cysteines and effects on DNA binding.

Kaar JL, Basse N, Joerger AC, Stephens E, Rutherford TJ, Fersht AR.

Protein Sci. 2010 Dec;19(12):2267-78. doi: 10.1002/pro.507.


A transient and low-populated protein-folding intermediate at atomic resolution.

Korzhnev DM, Religa TL, Banachewicz W, Fersht AR, Kay LE.

Science. 2010 Sep 10;329(5997):1312-6. doi: 10.1126/science.1191723.


Carboxyl pK(a) values and acid denaturation of BBL.

Arbely E, Rutherford TJ, Neuweiler H, Sharpe TD, Ferguson N, Fersht AR.

J Mol Biol. 2010 Oct 22;403(2):313-27. doi: 10.1016/j.jmb.2010.08.052. Epub 2010 Sep 15.


Refolding the engrailed homeodomain: structural basis for the accumulation of a folding intermediate.

McCully ME, Beck DA, Fersht AR, Daggett V.

Biophys J. 2010 Sep 8;99(5):1628-36. doi: 10.1016/j.bpj.2010.06.040.


The human peripheral subunit-binding domain folds rapidly while overcoming repulsive Coulomb forces.

Arbely E, Neuweiler H, Sharpe TD, Johnson CM, Fersht AR.

Protein Sci. 2010 Sep;19(9):1704-13. doi: 10.1002/pro.453.


Highest paraoxonase turnover rate found in a bacterial phosphotriesterase variant.

Briseño-Roa L, Oliynyk Z, Timperley CM, Griffiths AD, Fersht AR.

Protein Eng Des Sel. 2011 Jan;24(1-2):209-11. doi: 10.1093/protein/gzq046. Epub 2010 Jul 22.


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