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Alan Fersht

This is a preview profile on BiomedExperts - the first literature-based scientific social network. It brings the right researchers together and allows them to collaborate online. Collexis and Dell provide the BiomedExperts network of +1.5 Million pre-calculated profiles free of charge to researchers worldwide.

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Physiology

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Thermodynamics

Disorders

Protein Denaturation

Chemicals & Drugs

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Escherichia coli

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Co-Publications
Name
35
Freund, Stefan
30
Bycroft, Mark
21
Veprintsev, Dmitry
17
Daggett, Valerie
15
Ferguson, Neil
14
Itzhaki, LS
14
Johnson, Christopher
12
Sharpe, Timothy
11
Neira, José
10
Rutherford, Trevor
9
Tidow, Henning
9
De Prat-Gay, Gonzalo
8
Friedler, Assaf
8
Sato, Satoshi
8
Ladurner, AG

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Publications

TOP 3
Di Re M; Sembongi H; He J; Reyes A; Yasukawa T; Martinsson P; Bailey L J; Goffart S; Boyd-Kirkup J D; Wong T S; Fersht A R; Spelbrink J N; Holt I J
The accessory subunit of mitochondrial DNA polymerase gamma determines the DNA content of mitochondrial nucleoids in human cultured cells.
Rajagopalan Sridharan; Andreeva Antonina; Teufel Daniel P; Freund Stefan M; Fersht Alan R
Interaction between the transactivation domain of p53 and PC4 exemplifies acidic activation domains as single-stranded DNA mimics.
Khoo Kian Hoe; Joerger Andreas C; Freund Stefan M V; Fersht Alan R
Stabilising the DNA-binding domain of p53 by rational design of its hydrophobic core.

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All Publications

2009: Di Re M; Sembongi H; He J; Reyes A; Yasukawa T; Martinsson P; Bailey L J; Goffart S; Boyd-Kirkup J D; Wong T S; Fersht A R; Spelbrink J N; Holt I J
The accessory subunit of mitochondrial DNA polymerase gamma determines the DNA content of mitochondrial nucleoids in human cultured cells.
Nucleic acids research 2009;37(17):5701-13.
2009: Rajagopalan Sridharan; Andreeva Antonina; Teufel Daniel P; Freund Stefan M; Fersht Alan R
Interaction between the transactivation domain of p53 and PC4 exemplifies acidic activation domains as single-stranded DNA mimics.
The Journal of biological chemistry 2009;284(32):21728-37.
2009: Khoo Kian Hoe; Joerger Andreas C; Freund Stefan M V; Fersht Alan R
Stabilising the DNA-binding domain of p53 by rational design of its hydrophobic core.
Protein engineering, design & selection : PEDS 2009;22(7):421-30.
2009: Neuweiler Hannes; Sharpe Timothy D; Rutherford Trevor J; Johnson Christopher M; Allen Mark D; Ferguson Neil; Fersht Alan R
The folding mechanism of BBL: Plasticity of transition-state structure observed within an ultrafast folding protein family.
Journal of molecular biology 2009;390(5):1060-73.
2009: Lambert Jeremy M R; Gorzov Petr; Veprintsev Dimitry B; Söderqvist Maja; Segerbäck Dan; Bergman Jan; Fersht Alan R; Hainaut Pierre; Wiman Klas G; Bykov Vladimir J N
PRIMA-1 reactivates mutant p53 by covalent binding to the core domain.
Cancer cell 2009;15(5):376-88.
2009: Teufel D P; Bycroft M; Fersht A R
Regulation by phosphorylation of the relative affinities of the N-terminal transactivation domains of p53 for p300 domains and Mdm2.
Oncogene 2009;28(20):2112-8.
2009: van Dieck Jan; Fernandez-Fernandez Maria R; Veprintsev Dmitry B; Fersht Alan R
Modulation of the oligomerization state of p53 by differential binding of proteins of the S100 family to p53 monomers and tetramers.
The Journal of biological chemistry 2009;284(20):13804-11.
2009: Huang F; Lerner E; Sato S; Amir D; Haas E; Fersht A R
Time-resolved fluorescence resonance energy transfer study shows a compact denatured state of the B domain of protein A.
Biochemistry 2009;48(15):3468-76.
2009: Settanni Giovanni; Fersht Alan R
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 2009;387(4):993-1001.
2009: Neuweiler Hannes; Sharpe Timothy D; Johnson Christopher M; Teufel Daniel P; Ferguson Neil; Fersht Alan R
Downhill versus barrier-limited folding of BBL 2: mechanistic insights from kinetics of folding monitored by independent tryptophan probes.
Journal of molecular biology 2009;387(4):975-85.
2009: Arbely Eyal; Rutherford Trevor J; Sharpe Timothy D; Ferguson Neil; Fersht Alan R
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 2009;387(4):986-92.
2009: Burge Sarah; Teufel Daniel P; Townsley Fiona M; Freund Stefan M V; Bycroft Mark; Fersht Alan R
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 2009;106(9):3142-7.
2009: Daggett Valerie; Fersht Alan R
Protein folding and binding: moving into unchartered territory.
Current opinion in structural biology 2009;19(1):1-2.
2009: Tidow Henning; Andreeva Antonina; Rutherford Trevor J; Fersht Alan R
Solution structure of the U11-48K CHHC zinc-finger domain that specifically binds the 5' splice site of U12-type introns.
Structure (London, England : 1993) 2009;17(2):294-302.
2009: Yu Grace W; Vaysburd Marina; Allen Mark D; Settanni Giovanni; Fersht Alan R
Structure of human MDM4 N-terminal domain bound to a single-domain antibody.
Journal of molecular biology 2009;385(5):1578-89.
2009: Wong Tuck Seng; Rajagopalan Sridharan; Townsley Fiona M; Freund Stefan M; Petrovich Miriana; Loakes David; Fersht Alan R
Physical and functional interactions between human mitochondrial single-stranded DNA-binding protein and tumour suppressor p53.
Nucleic acids research 2009;37(2):568-81.
2009: Lehn Jean-Marie; Fersht Alan R
Interfaces: two worlds unite.
Chembiochem : a European journal of chemical biology 2009;10(1):4.
2008: Rajagopalan Sridharan; Jaulent Agnes M; Wells Mark; Veprintsev Dmitry B; Fersht Alan R
14-3-3 activation of DNA binding of p53 by enhancing its association into tetramers.
Nucleic acids research 2008;36(18):5983-91.
2008: Fernandez-Fernandez Maria Rosario; Rutherford Trevor J; Fersht Alan R
Members of the S100 family bind p53 in two distinct ways.
Protein science : a publication of the Protein Society 2008;17(10):1663-70.
2008: Sharpe Timothy D; Ferguson Neil; Johnson Christopher M; Fersht Alan R
Conservation of transition state structure in fast folding peripheral subunit-binding domains.
Journal of molecular biology 2008;383(1):224-37.
2008: García-Alai Maria M; Tidow Henning; Natan Eviatar; Townsley Fiona M; Veprintsev Dmitry B; Fersht Alan R
The novel p53 isoform "delta p53" is a misfolded protein and does not bind the p21 promoter site.
Protein science : a publication of the Protein Society 2008;17(10):1671-8.
2008: Becker Johanna; Ferguson Neil; Flinders Jeremy; van Rossum Barth-Jan; Fersht Alan R; Oschkinat Hartmut
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 2008;9(12):1946-52.
2008: Fersht Alan R
From the first protein structures to our current knowledge of protein folding: delights and scepticisms.
Nature reviews. Molecular cell biology 2008;9(8):650-4.
2008: Boeckler Frank M; Joerger Andreas C; Jaggi Gaurav; Rutherford Trevor J; Veprintsev Dmitry B; Fersht Alan R
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 2008;105(30):10360-5.
2008: Tafvizi Anahita; Huang Fang; Leith Jason S; Fersht Alan R; Mirny Leonid A; van Oijen Antoine M
Tumor suppressor p53 slides on DNA with low friction and high stability.
Biophysical journal 2008;95(1):L01-3.
2008: Settanni Giovanni; Fersht Alan R
High temperature unfolding simulations of the TRPZ1 peptide.
Biophysical journal 2008;94(11):4444-53.
2008: Wells Mark; Tidow Henning; Rutherford Trevor J; Markwick Phineus; Jensen Malene Ringkjobing; Mylonas Efstratios; Svergun Dmitri I; Blackledge Martin; Fersht Alan R
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 2008;105(15):5762-7.
2008: Jemth Per; Johnson Christopher M; Gianni Stefano; Fersht Alan R
Demonstration by burst-phase analysis of a robust folding intermediate in the FF domain.
Protein engineering, design & selection : PEDS 2008;21(3):207-14.
2008: Veprintsev Dmitry B; Fersht Alan R
Algorithm for prediction of tumour suppressor p53 affinity for binding sites in DNA.
Nucleic acids research 2008;36(5):1589-98.
2008: Huang Fang; Settanni Giovanni; Fersht Alan R
Fluorescence resonance energy transfer analysis of the folding pathway of Engrailed Homeodomain.
Protein engineering, design & selection : PEDS 2008;21(3):131-46.
2008: Joerger Andreas C; Fersht Alan R
Structural biology of the tumor suppressor p53.
Annual review of biochemistry 2008;77():557-82.
2007: Sharpe Tim; Jonsson Amanda L; Rutherford Trevor J; Daggett Valerie; Fersht Alan R
The role of the turn in beta-hairpin formation during WW domain folding.
Protein science : a publication of the Protein Society 2007;16(10):2233-9.
2007: Sot Begona; Freund Stefan M V; Fersht Alan R
Comparative biophysical characterization of p53 with the pro-apoptotic BAK and the anti-apoptotic BCL-xL.
The Journal of biological chemistry 2007;282(40):29193-200.
2007: Korzhnev Dmitry M; Religa Tomasz L; Lundström Patrik; Fersht Alan R; Kay Lewis E
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 2007;372(2):497-512.
2007: Mayer Sebastian; Rüdiger Stefan; Ang Hwee Ching; Joerger Andreas C; Fersht Alan R
Correlation of levels of folded recombinant p53 in escherichia coli with thermodynamic stability in vitro.
Journal of molecular biology 2007;372(1):268-76.
2007: Sato Satoshi; Fersht Alan R
Searching for multiple folding pathways of a nearly symmetrical protein: temperature dependent phi-value analysis of the B domain of protein A.
Journal of molecular biology 2007;372(1):254-67.
2007: Tidow Henning; Andreeva Antonina; Rutherford Trevor J; Fersht Alan R
Solution structure of ASPP2 N-terminal domain (N-ASPP2) reveals a ubiquitin-like fold.
Journal of molecular biology 2007;371(4):948-58.
2007: Tidow Henning; Melero Roberto; Mylonas Efstratios; Freund Stefan M V; Grossmann J Guenter; Carazo José María; Svergun Dmitri I; Valle Mikel; Fersht Alan R
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 2007;104(30):12324-9.
2007: Religa Tomasz L; Johnson Christopher M; Vu Dung M; Brewer Scott H; Dyer R Brian; Fersht Alan R
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 2007;104(22):9272-7.
2007: Teufel Daniel P; Freund Stefan M; Bycroft Mark; Fersht Alan R
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 2007;104(17):7009-14.
2007: Joerger A C; Fersht A R
Structure-function-rescue: the diverse nature of common p53 cancer mutants.
Oncogene 2007;26(15):2226-42.
2007: Scott Kathryn A; Alonso Darwin O V; Sato Satoshi; Fersht Alan R; Daggett Valerie
Conformational entropy of alanine versus glycine in protein denatured states.
Proceedings of the National Academy of Sciences of the United States of America 2007;104(8):2661-6.
2007: Ferguson Neil; Sharpe Timothy D; Johnson Christopher M; Schartau Pamela J; Fersht Alan R
Structural biology: analysis of 'downhill' protein folding.
Nature 2007;445(7129):E14-5; discussion E17-8.
2007: Huang Fang; Sato Satoshi; Sharpe Timothy D; Ying Liming; Fersht Alan R
Distinguishing between cooperative and unimodal downhill protein folding.
Proceedings of the National Academy of Sciences of the United States of America 2007;104(1):123-7.
2007: Joerger Andreas C; Fersht Alan R
Structural biology of the tumor suppressor p53 and cancer-associated mutants.
Advances in cancer research 2007;97():1-23.
2006: Ferguson Neil; Becker Johanna; Tidow Henning; Tremmel Sandra; Sharpe Timothy D; Krause Gerd; Flinders Jeremy; Petrovich Miriana; Berriman John; Oschkinat Hartmut; Fersht Alan R
General structural motifs of amyloid protofilaments.
Proceedings of the National Academy of Sciences of the United States of America 2006;103(44):16248-53.
2006: Joerger Andreas C; Ang Hwee Ching; Fersht Alan R
Structural basis for understanding oncogenic p53 mutations and designing rescue drugs.
Proceedings of the National Academy of Sciences of the United States of America 2006;103(41):15056-61.
2006: Tidow Henning; Veprintsev Dmitry B; Freund Stefan M V; Fersht Alan R
Effects of oncogenic mutations and DNA response elements on the binding of p53 to p53-binding protein 2 (53BP2).
The Journal of biological chemistry 2006;281(43):32526-33.
2006: Sánchez-Puig Nuria; Fersht Alan R
Characterization of the native and fibrillar conformation of the human Nalpha-acetyltransferase ARD1.
Protein science : a publication of the Protein Society 2006;15(8):1968-76.
2006: Ang Hwee Ching; Joerger Andreas C; Mayer Sebastian; Fersht Alan R
Effects of common cancer mutations on stability and DNA binding of full-length p53 compared with isolated core domains.
The Journal of biological chemistry 2006;281(31):21934-41.
2006: Petrovich Miriana; Jonsson Amanda L; Ferguson Neil; Daggett Valerie; Fersht Alan R
Phi-analysis at the experimental limits: mechanism of beta-hairpin formation.
Journal of molecular biology 2006;360(4):865-81.
2006: Sato Satoshi; Religa Tomasz L; Fersht Alan R
Phi-analysis of the folding of the B domain of protein A using multiple optical probes.
Journal of molecular biology 2006;360(4):850-64.
2006: Ferguson Neil; Sharpe Timothy D; Johnson Christopher M; Fersht Alan R
The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics.
Journal of molecular biology 2006;356(5):1237-47.
2006: Cañadillas José Manuel Pérez; Tidow Henning; Freund Stefan M V; Rutherford Trevor J; Ang Hwee Ching; Fersht Alan R
Solution structure of p53 core domain: structural basis for its instability.
Proceedings of the National Academy of Sciences of the United States of America 2006;103(7):2109-14.
2006: Veprintsev Dmitry B; Freund Stefan M V; Andreeva Antonina; Rutledge Stacey E; Tidow Henning; Cañadillas José Manuel Pérez; Blair Caroline M; Fersht Alan R
Core domain interactions in full-length p53 in solution.
Proceedings of the National Academy of Sciences of the United States of America 2006;103(7):2115-9.
2006: Yu Grace W; Allen Mark D; Andreeva Antonina; Fersht Alan R; Bycroft Mark
Solution structure of the C4 zinc finger domain of HDM2.
Protein science : a publication of the Protein Society 2006;15(2):384-9.
2006: Yu Grace W; Rudiger Stefan; Veprintsev Dmitry; Freund Stefan; Fernandez-Fernandez M Rosario; Fersht Alan R
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 2006;103(5):1227-32.
2006: Briseño-Roa Luis; Hill Jim; Notman Stuart; Sellers David; Smith Andy P; Timperley Christopher M; Wetherell Janet; Williams Nichola H; Williams Gareth R; Fersht Alan R; Griffiths Andrew D
Analogues with fluorescent leaving groups for screening and selection of enzymes that efficiently hydrolyze organophosphorus nerve agents.
Journal of medicinal chemistry 2006;49(1):246-55.
2005: Religa T L; Markson J S; Mayor U; Freund S M V; Fersht A R
Solution structure of a protein denatured state and folding intermediate.
Nature 2005;437(7061):1053-6.
2005: Ferguson Neil; Sharpe Timothy D; Schartau Pamela J; Sato Satoshi; Allen Mark D; Johnson Christopher M; Rutherford Trevor J; Fersht Alan R
Ultra-fast barrier-limited folding in the peripheral subunit-binding domain family.
Journal of molecular biology 2005;353(2):427-46.
2005: Salvatella Xavier; Dobson Christopher M; Fersht Alan R; Vendruscolo Michele
Determination of the folding transition states of barnase by using PhiI-value-restrained simulations validated by double mutant PhiIJ-values.
Proceedings of the National Academy of Sciences of the United States of America 2005;102(35):12389-94.
2005: Koch Michael; Stronge Victoria S; Shepherd Dawn; Gadola Stephan D; Mathew Bini; Ritter Gerd; Fersht Alan R; Besra Gurdyal S; Schmidt Richard R; Jones E Yvonne; Cerundolo Vincenzo
The crystal structure of human CD1d with and without alpha-galactosylceramide.
Nature immunology 2005;6(8):819-26.
2005: White George W N; Gianni Stefano; Grossmann J Gunter; Jemth Per; Fersht Alan R; Daggett Valerie
Simulation and experiment conspire to reveal cryptic intermediates and a slide from the nucleation-condensation to framework mechanism of folding.
Journal of molecular biology 2005;350(4):757-75.
2005: Jemth Per; Day Ryan; Gianni Stefano; Khan Faaizah; Allen Mark; Daggett Valerie; Fersht Alan R
The structure of the major transition state for folding of an FF domain from experiment and simulation.
Journal of molecular biology 2005;350(2):363-78.
2005: Sánchez-Puig Nuria; Veprintsev Dmitry B; Fersht Alan R
Human full-length Securin is a natively unfolded protein.
Protein science : a publication of the Protein Society 2005;14(6):1410-8.
2005: Weinberg Richard L; Veprintsev Dmitry B; Bycroft Mark; Fersht Alan R
Comparative binding of p53 to its promoter and DNA recognition elements.
Journal of molecular biology 2005;348(3):589-96.
2005: Friedler Assaf; Veprintsev Dmitry B; Freund Stefan M V; von Glos Karoly I; Fersht Alan R
Modulation of binding of DNA to the C-terminal domain of p53 by acetylation.
Structure (London, England : 1993) 2005;13(4):629-36.
2005: Ferguson Neil; Day Ryan; Johnson Christopher M; Allen Mark D; Daggett Valerie; Fersht Alan R
Simulation and experiment at high temperatures: ultrafast folding of a thermophilic protein by nucleation-condensation.
Journal of molecular biology 2005;347(4):855-70.
2005: Joerger Andreas C; Ang Hwee Ching; Veprintsev Dmitry B; Blair Caroline M; Fersht Alan R
Structures of p53 cancer mutants and mechanism of rescue by second-site suppressor mutations.
The Journal of biological chemistry 2005;280(16):16030-7.
2005: Fernandez-Fernandez Maria Rosario; Veprintsev Dmitry B; Fersht Alan R
Proteins of the S100 family regulate the oligomerization of p53 tumor suppressor.
Proceedings of the National Academy of Sciences of the United States of America 2005;102(13):4735-40.
2005: Friedler Assaf; Veprintsev Dmitry B; Rutherford Trevor; von Glos Karoly I; Fersht Alan R
Binding of Rad51 and other peptide sequences to a promiscuous, highly electrostatic binding site in p53.
The Journal of biological chemistry 2005;280(9):8051-9.
2005: Garcia Pascal; Bruix Marta; Rico Manuel; Ciofi-Baffoni Simone; Banci Lucia; Ramachandra Shastry M C; Roder Heinrich; de Lumley Woodyear Thierry; Johnson Christopher M; Fersht Alan R; Barker Paul D
Effects of heme on the structure of the denatured state and folding kinetics of cytochrome b562.
Journal of molecular biology 2005;346(1):331-44.
2005: Sánchez-Puig Nuria; Veprintsev Dmitry B; Fersht Alan R
Binding of natively unfolded HIF-1alpha ODD domain to p53.
Molecular cell 2005;17(1):11-21.
2005: Fulton Kate F; Devlin Glyn L; Jodun Rachel A; Silvestri Linda; Bottomley Stephen P; Fersht Alan R; Buckle Ashley M
PFD: a database for the investigation of protein folding kinetics and stability.
Nucleic acids research 2005;33(Database issue):D279-83.
2004: Fersht Alan R
Phi value versus psi analysis.
Proceedings of the National Academy of Sciences of the United States of America 2004;101(50):17327-8.
2004: Ferguson Neil; Schartau Pamela J; Sharpe Timothy D; Sato Satoshi; Fersht Alan R
One-state downhill versus conventional protein folding.
Journal of molecular biology 2004;344(2):295-301.
2004: Fersht Alan R
Relationship of Leffler (Bronsted) alpha values and protein folding Phi values to position of transition-state structures on reaction coordinates.
Proceedings of the National Academy of Sciences of the United States of America 2004;101(40):14338-42.
2004: Weinberg Richard L; Freund Stefan M V; Veprintsev Dmitry B; Bycroft Mark; Fersht Alan R
Regulation of DNA binding of p53 by its C-terminal domain.
Journal of molecular biology 2004;342(3):801-11.
2004: Weinberg Richard L; Veprintsev Dmitry B; Fersht Alan R
Cooperative binding of tetrameric p53 to DNA.
Journal of molecular biology 2004;341(5):1145-59.
2004: Fersht Alan R; Sato Satoshi
Phi-value analysis and the nature of protein-folding transition states.
Proceedings of the National Academy of Sciences of the United States of America 2004;101(21):7976-81.
2004: Sato Satoshi; Religa Tomasz L; Daggett Valerie; Fersht Alan R
Testing protein-folding simulations by experiment: B domain of protein A.
Proceedings of the National Academy of Sciences of the United States of America 2004;101(18):6952-6.
2004: Oliynyk Z; Briseño-Roa L; Janowitz T; Sondergeld P; Fersht A R
Designing a metal-binding site in the scaffold of Escherichia coli KDO8PS.
Protein engineering, design & selection : PEDS 2004;17(4):383-90.
2004: Jemth Per; Gianni Stefano; Day Ryan; Li Bin; Johnson Christopher M; Daggett Valerie; Fersht Alan R
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 2004;101(17):6450-5.
2004: Batuwangala Thil; Shepherd Dawn; Gadola Stephan D; Gibson Kevin J C; Zaccai Nathan R; Fersht Alan R; Besra Gurdyal S; Cerundolo Vincenzo; Jones E Yvonne
The crystal structure of human CD1b with a bound bacterial glycolipid.
Journal of immunology (Baltimore, Md. : 1950) 2004;172(4):2382-8.
2004: Schon Oliver; Friedler Assaf; Freund Stefan; Fersht Alan R
Binding of p53-derived ligands to MDM2 induces a variety of long range conformational changes.
Journal of molecular biology 2004;336(1):197-202.
2004: Friedler Assaf; DeDecker Brian S; Freund Stefan M V; Blair Caroline; Rüdiger Stefan; Fersht Alan R
Structural distortion of p53 by the mutation R249S and its rescue by a designed peptide: implications for "mutant conformation".
Journal of molecular biology 2004;336(1):187-96.
2004: Joerger Andreas C; Allen Mark D; Fersht Alan R
Crystal structure of a superstable mutant of human p53 core domain. Insights into the mechanism of rescuing oncogenic mutations.
The Journal of biological chemistry 2004;279(2):1291-6.
2003: Gianni Stefano; Mayor Ugo; Fersht Alan R
Structural insights in the folding of small single-domain proteins.
The Italian journal of biochemistry 2003;52(4):154-61.
2003: Issaeva Natalia; Friedler Assaf; Bozko Przemyslaw; Wiman Klas G; Fersht Alan R; Selivanova Galina
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 2003;100(23):13303-7.
2003: Gianni Stefano; Guydosh Nicholas R; Khan Faaizah; Caldas Teresa D; Mayor Ugo; White George W N; DeMarco Mari L; Daggett Valerie; Fersht Alan R
Unifying features in protein-folding mechanisms.
Proceedings of the National Academy of Sciences of the United States of America 2003;100(23):13286-91.
2003: Mayor Ugo; Grossmann J Günter; Foster Nicholas W; Freund Stefan M V; Fersht Alan R
The denatured state of Engrailed Homeodomain under denaturing and native conditions.
Journal of molecular biology 2003;333(5):977-91.
2003: Khan Faaizah; Chuang Jessica I; Gianni Stefano; Fersht Alan R
The kinetic pathway of folding of barnase.
Journal of molecular biology 2003;333(1):169-86.
2003: Stollar Elliott J; Mayor Ugo; Lovell Simon C; Federici Luca; Freund Stefan M V; Fersht Alan R; Luisi Ben F
Crystal structures of engrailed homeodomain mutants: implications for stability and dynamics.
The Journal of biological chemistry 2003;278(44):43699-708.
2003: Ferguson Neil; Berriman John; Petrovich Miriana; Sharpe Timothy D; Finch John T; Fersht Alan R
Rapid amyloid fiber formation from the fast-folding WW domain FBP28.
Proceedings of the National Academy of Sciences of the United States of America 2003;100(17):9814-9.
2003: Friedler Assaf; Veprintsev Dmitry B; Hansson Lars O; Fersht Alan R
Kinetic instability of p53 core domain mutants: implications for rescue by small molecules.
The Journal of biological chemistry 2003;278(26):24108-12.
2003: Joerger Andreas C; Mayer Sebastian; Fersht Alan R
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 2003;100(10):5694-9.
2003: Mayor Ugo; Guydosh Nicholas R; Johnson Christopher M; Grossmann J Günter; Sato Satoshi; Jas Gouri S; Freund Stefan M V; Alonso Darwin O V; Daggett Valerie; Fersht Alan R
The complete folding pathway of a protein from nanoseconds to microseconds.
Nature 2003;421(6925):863-7.
2003: Ferguson Neil; Fersht Alan R
Early events in protein folding.
Current opinion in structural biology 2003;13(1):75-81.
2003: Daggett Valerie; Fersht Alan R
Is there a unifying mechanism for protein folding?
Trends in biochemical sciences 2003;28(1):18-25.
2003: Tang Kit S; Fersht Alan R; Itzhaki Laura S
Sequential unfolding of ankyrin repeats in tumor suppressor p16.
Structure (London, England : 1993) 2003;11(1):67-73.
2002: Fersht Alan R
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 2002;99(22):14122-5.
2002: Schon Oliver; Friedler Assaf; Bycroft Mark; Freund Stefan M V; Fersht Alan R
Molecular mechanism of the interaction between MDM2 and p53.
Journal of molecular biology 2002;323(3):491-501.
2002: Rudiger Stefan; Freund Stefan M V; Veprintsev Dmitry B; Fersht Alan R
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 2002;99(17):11085-90.
2002: Hansson Lars O; Friedler Assaf; Freund Stefan; Rudiger Stefan; Fersht Alan R
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 2002;99(16):10305-9.
2002: Rippin Thomas M; Freund Stefan M V; Veprintsev Dmitry B; Fersht Alan R
Recognition of DNA by p53 core domain and location of intermolecular contacts of cooperative binding.
Journal of molecular biology 2002;319(2):351-8.
2002: Altamirano M M; Blackburn J M; Aguayo C; Fersht A R
Retraction. Directed evolution of new catalytic activity using the alpha/beta-barrel scaffold.
Nature 2002;417(6887):468.
2002: Fersht Alan R
Max Ferdinand Perutz OM FRS.
Nature structural biology 2002;9(4):245-6.
2002: Vaughan Cara K; Harryson Pia; Buckle Ashley M; Fersht Alan R
A structural double-mutant cycle: estimating the strength of a buried salt bridge in barnase.
Acta crystallographica. Section D, Biological crystallography 2002;58(Pt 4):591-600.
2002: Rippin Thomas M; Bykov Vladimir J N; Freund Stefan M V; Selivanova Galina; Wiman Klas G; Fersht Alan R
Characterization of the p53-rescue drug CP-31398 in vitro and in living cells.
Oncogene 2002;21(14):2119-29.
2002: Fersht Alan R; Daggett Valerie
Protein folding and unfolding at atomic resolution.
Cell 2002;108(4):573-82.
2002: Kazmirski Steven L; Isaacson Rivka L; An Chahm; Buckle Ashley; Johnson Christopher M; Daggett Valerie; Fersht Alan R
Loss of a metal-binding site in gelsolin leads to familial amyloidosis-Finnish type.
Nature structural biology 2002;9(2):112-6.
2002: Friedler Assaf; Hansson Lars O; Veprintsev Dmitry B; Freund Stefan M V; Rippin Thomas M; Nikolova Penka V; Proctor Mark R; Rüdiger Stefan; Fersht Alan R
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 2002;99(2):937-42.
2002: Galani Despina; Fersht Alan R; Perrett Sarah
Folding of the yeast prion protein Ure2: kinetic evidence for folding and unfolding intermediates.
Journal of molecular biology 2002;315(2):213-27.
2001: Ferguson N; Pires J R; Toepert F; Johnson C M; Pan Y P; 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 2001;98(23):13008-13.
2001: Ferguson N; Johnson C M; 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 2001;98(23):13002-7.
2001: Bullock A N; Fersht A R
Rescuing the function of mutant p53.
Nature reviews. Cancer 2001;1(1):68-76.
2001: Ikura T; Fersht A R
[Folding mechanism and folding rate]
Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme 2001;46(11 Suppl):1553-9.
2001: Frisch C; Fersht A R; Schreiber G
Experimental assignment of the structure of the transition state for the association of barnase and barstar.
Journal of molecular biology 2001;308(1):69-77.
2001: Smoot A L; Panda M; Brazil B T; Buckle A M; Fersht A R; Horowitz P M
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 2001;40(14):4484-92.
2001: Kazmirski S L; Wong K B; Freund S M; Tan Y J; Fersht A R; 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 2001;98(8):4349-54.
2001: Wang W K; Bycroft M; Foster N W; Buckle A M; Fersht A R; Chen Y W
Structure of the C-terminal sterile alpha-motif (SAM) domain of human p73 alpha.
Acta crystallographica. Section D, Biological crystallography 2001;57(Pt 4):545-51.
2001: Karadimitris A; Gadola S; Altamirano M; Brown D; Woolfson A; Klenerman P; Chen J L; Koezuka Y; Roberts I A; Price D A; 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 2001;98(6):3294-8.
2001: Altamirano M M; Woolfson A; Donda A; Shamshiev A; Briseño-Roa L; Foster N W; Veprintsev D B; De Libero G; Fersht A R; 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 2001;98(6):3288-93.
2000: Clarke J; Hounslow A M; Bond C J; Fersht A R; Daggett V
The effects of disulfide bonds on the denatured state of barnase.
Protein science : a publication of the Protein Society 2000;9(12):2394-404.
2000: Chatellier J; Hill F; Foster N W; Goloubinoff P; Fersht A R
From minichaperone to GroEL 3: properties of an active single-ring mutant of GroEL.
Journal of molecular biology 2000;304(5):897-910.
2000: Chatellier J; Hill F; Fersht A R
From minichaperone to GroEL 2: importance of avidity of the multisite ring structure.
Journal of molecular biology 2000;304(5):883-96.
2000: Wang Q; Buckle A M; Fersht A R
From minichaperone to GroEL 1: information on GroEL-polypeptide interactions from crystal packing of minichaperones.
Journal of molecular biology 2000;304(5):873-81.
2000: Fersht A R
A kinetically significant intermediate in the folding of barnase.
Proceedings of the National Academy of Sciences of the United States of America 2000;97(26):14121-6.
2000: Mayor U; Johnson C M; Daggett V; Fersht A R
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 2000;97(25):13518-22.
2000: Buchberger A; Howard M J; Freund S M; Proctor M; Butler P J; Fersht A R; Bycroft M
Biophysical characterization of elongin C from Saccharomyces cerevisiae.
Biochemistry 2000;39(36):11137-46.
2000: Kazmirski S L; Howard M J; Isaacson R L; Fersht A R
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 2000;97(20):10706-11.
2000: Inaba K; Kobayashi N; Fersht A R
Conversion of two-state to multi-state folding kinetics on fusion of two protein foldons.
Journal of molecular biology 2000;302(1):219-33.
2000: Carmichael J; Chatellier J; Woolfson A; Milstein C; Fersht A R; Rubinsztein D C
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 2000;97(17):9701-5.
2000: Yiu C P; Mateu M G; Fersht A R
Protein folding transition states: elicitation of Hammond effects by 2,2,2-trifluoroethanol.
Chembiochem : a European journal of chemical biology 2000;1(1):49-55.
2000: Neira J L; Vázquez E; Fersht A R
Stability and folding of the protein complexes of barnase.
European journal of biochemistry / FEBS 2000;267(10):2859-70.
2000: Wang Q; Buckle A M; Fersht A R
Stabilization of GroEL minichaperones by core and surface mutations.
Journal of molecular biology 2000;298(5):917-26.
2000: Bullock A N; Henckel J; Fersht A R
Quantitative analysis of residual folding and DNA binding in mutant p53 core domain: definition of mutant states for rescue in cancer therapy.
Oncogene 2000;19(10):1245-56.
2000: Wong K B; Clarke J; Bond C J; Neira J L; Freund S M; Fersht A R; 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 2000;296(5):1257-82.
2000: Altamirano M M; Blackburn J M; Aguayo C; Fersht A R
Directed evolution of new catalytic activity using the alpha/beta-barrel scaffold.
Nature 2000;403(6770):617-22.
2000: Fersht A R
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 2000;97(4):1525-9.
2000: Nikolova P V; Wong K B; DeDecker B; Henckel J; Fersht A R
Mechanism of rescue of common p53 cancer mutations by second-site suppressor mutations.
The EMBO journal 2000;19(3):370-8.
1999: Chatellier J; Hartley O; Griffiths A D; Fersht A R; Winter G; Riechmann L
Interdomain interactions within the gene 3 protein of filamentous phage.
FEBS letters 1999;463(3):371-4.
1999: Wang Q; Buckle A M; Foster N W; Johnson C M; Fersht A R
Design of highly stable functional GroEL minichaperones.
Protein science : a publication of the Protein Society 1999;8(10):2186-93.
1999: Durocher D; Henckel J; Fersht A R; Jackson S P
The FHA domain is a modular phosphopeptide recognition motif.
Molecular cell 1999;4(3):387-94.
1999: Isaacson R L; Weeds A G; Fersht A R
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 1999;96(20):11247-52.
1999: Kobayashi N; Freund S M; Chatellier J; Zahn R; Fersht A R
NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution.
Journal of molecular biology 1999;292(1):181-90.
1999: Tanaka N; Fersht A R
Identification of substrate binding site of GroEL minichaperone in solution.
Journal of molecular biology 1999;292(1):173-80.
1999: Chatellier J; Buckle A M; Fersht A R
GroEL recognises sequential and non-sequential linear structural motifs compatible with extended beta-strands and alpha-helices.
Journal of molecular biology 1999;292(1):163-72.
1999: Golbik R; Fischer G; Fersht A R
Folding of barstar C40A/C82A/P27A and catalysis of the peptidyl-prolyl cis/trans isomerization by human cytosolic cyclophilin (Cyp18).
Protein science : a publication of the Protein Society 1999;8(7):1505-14.
1999: Wong K B; DeDecker B S; Freund S M; Proctor M R; Bycroft M; Fersht A R
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 1999;96(15):8438-42.
1999: Arnesano F; Banci L; Bertini I; Faraone-Mennella J; Rosato A; Barker P D; Fersht A R
The solution structure of oxidized Escherichia coli cytochrome b562.
Biochemistry 1999;38(27):8657-70.
1999: Perrett S; Freeman S J; Butler P J; Fersht A R
Equilibrium folding properties of the yeast prion protein determinant Ure2.
Journal of molecular biology 1999;290(1):331-45.
1999: Killick T R; Freund S M; Fersht A R
Real-time NMR studies on a transient folding intermediate of barstar.
Protein science : a publication of the Protein Society 1999;8(6):1286-91.
1999: Mateu M G; Fersht A R
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 1999;96(7):3595-9.
1999: Neira J L; Fersht A R
Acquisition of native-like interactions in C-terminal fragments of barnase.
Journal of molecular biology 1999;287(2):421-32.
1999: Vaughan C K; Buckle A M; Fersht A R
Structural response to mutation at a protein-protein interface.
Journal of molecular biology 1999;286(5):1487-506.
1999: Axe D D; Foster N W; Fersht A R
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 1999;286(5):1471-85.
1999: Altamirano M M; García C; Possani L D; Fersht A R
Oxidative refolding chromatography: folding of the scorpion toxin Cn5.
Nature biotechnology 1999;17(2):187-91.
1999: Mateu M G; Sánchez Del Pino M M; Fersht A R
Mechanism of folding and assembly of a small tetrameric protein domain from tumor suppressor p53.
Nature structural biology 1999;6(2):191-8.
1999: Otzen D E; Fersht A R
Analysis of protein-protein interactions by mutagenesis: direct versus indirect effects.
Protein engineering 1999;12(1):41-5.
1999: Tang K S; Guralnick B J; Wang W K; Fersht A R; Itzhaki L S
Stability and folding of the tumour suppressor protein p16.
Journal of molecular biology 1999;285(4):1869-86.
1999: Neira J L; Fersht A R
Exploring the folding funnel of a polypeptide chain by biophysical studies on protein fragments.
Journal of molecular biology 1999;285(3):1309-33.
1999: Ladurner A G; Fersht A R
Upper limit of the time scale for diffusion and chain collapse in chymotrypsin inhibitor 2.
Nature structural biology 1999;6(1):28-31.
1998: Ben-Zvi A P; Chatellier J; Fersht A R; Goloubinoff P
Minimal and optimal mechanisms for GroE-mediated protein folding.
Proceedings of the National Academy of Sciences of the United States of America 1998;95(26):15275-80.
1998: Nikolova P V; Henckel J; Lane D P; Fersht A R
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 1998;95(25):14675-80.
1998: Chatellier J; Hill F; Lund P A; Fersht A R
In vivo activities of GroEL minichaperones.
Proceedings of the National Academy of Sciences of the United States of America 1998;95(17):9861-6.
1998: Ladurner A G; Itzhaki L S; Daggett V; Fersht A R
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 1998;95(15):8473-8.
1998: Fersht A R; Shakhnovich E I
Protein folding: think globally, (inter)act locally.
Current biology : CB 1998;8(14):R478-9.
1998: Otzen D E; Fersht A R
Folding of circular and permuted chymotrypsin inhibitor 2: retention of the folding nucleus.
Biochemistry 1998;37(22):8139-46.
1998: Vijayakumar M; Wong K Y; Schreiber G; Fersht A R; Szabo A; Zhou H X
Electrostatic enhancement of diffusion-controlled protein-protein association: comparison of theory and experiment on barnase and barstar.
Journal of molecular biology 1998;278(5):1015-24.
1998: Axe D D; Foster N W; Fersht A R
A search for single substitutions that eliminate enzymatic function in a bacterial ribonuclease.
Biochemistry 1998;37(20):7157-66.
1998: Mateu M G; Fersht A R
Nine hydrophobic side chains are key determinants of the thermodynamic stability and oligomerization status of tumour suppressor p53 tetramerization domain.
The EMBO journal 1998;17(10):2748-58.
1998: Fersht A R
Sieves in sequence.
Science (New York, N.Y.) 1998;280(5363):541.
1998: Golbik R; Zahn R; Harding S E; Fersht A R
Thermodynamic stability and folding of GroEL minichaperones.
Journal of molecular biology 1998;276(2):505-15.
1998: Killick T R; Freund S M; Fersht A R
Real-time NMR studies on folding of mutants of barnase and chymotrypsin inhibitor 2.
FEBS letters 1998;423(1):110-2.
1997: Bullock A N; Henckel J; DeDecker B S; Johnson C M; Nikolova P V; Proctor M R; Lane D P; Fersht A R
Thermodynamic stability of wild-type and mutant p53 core domain.
Proceedings of the National Academy of Sciences of the United States of America 1997;94(26):14338-42.
1997: Bond C J; Wong K B; Clarke J; Fersht A R; 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 1997;94(25):13409-13.
1997: Stenberg G; Fersht A R
Folding of barnase in the presence of the molecular chaperone SecB.
Journal of molecular biology 1997;274(2):268-75.
1997: Soler-González A S; Fersht A R
Helix stability in barstar peptides.
European journal of biochemistry / FEBS 1997;249(3):724-32.
1997: Ladurner A G; Fersht A R
Glutamine, alanine or glycine repeats inserted into the loop of a protein have minimal effects on stability and folding rates.
Journal of molecular biology 1997;273(1):330-7.
1997: Ladurner A G; Itzhaki L S; de Prat Gay G; Fersht A R
Complementation of peptide fragments of the single domain protein chymotrypsin inhibitor 2.
Journal of molecular biology 1997;273(1):317-29.
1997: Clarke J; Itzhaki L S; Fersht A R
Hydrogen exchange at equilibrium: a short cut for analysing protein-folding pathways?
Trends in biochemical sciences 1997;22(8):284-7.
1997: Nölting B; Golbik R; Soler-González A S; Fersht A R
Circular dichroism of denatured barstar suggests residual structure,.
Biochemistry 1997;36(32):9899-905.
1997: Schreiber G; Frisch C; Fersht A R
The role of Glu73 of barnase in catalysis and the binding of barstar.
Journal of molecular biology 1997;270(1):111-22.
1997: Neira J L; Itzhaki L S; Otzen D E; Davis B; Fersht A R
Hydrogen exchange in chymotrypsin inhibitor 2 probed by mutagenesis.
Journal of molecular biology 1997;270(1):99-110.
1997: Itzhaki L S; Neira J L; Fersht A R
Hydrogen exchange in chymotrypsin inhibitor 2 probed by denaturants and temperature.
Journal of molecular biology 1997;270(1):89-98.
1997: Perrett S; Zahn R; Stenberg G; Fersht A R
Importance of electrostatic interactions in the rapid binding of polypeptides to GroEL.
Journal of molecular biology 1997;269(5):892-901.
1997: Wong K B; Fersht A R; Freund S M
NMR 15N relaxation and structural studies reveal slow conformational exchange in barstar C40/82A.
Journal of molecular biology 1997;268(2):494-511.
1997: Sánchez del Pino M M; Fersht A R
Nonsequential unfolding of the alpha/beta barrel protein indole-3-glycerol-phosphate synthase.
Biochemistry 1997;36(18):5560-5.
1997: Neira J L; Itzhaki L S; Ladurner A G; Davis B; de Prat Gay G; Fersht A R
Following co-operative formation of secondary and tertiary structure in a single protein module.
Journal of molecular biology 1997;268(1):185-97.
1997: Gopalan V; Golbik R; Schreiber G; Fersht A R; 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 1997;267(4):765-9.
1997: Frisch C; Schreiber G; Johnson C M; Fersht A R
Thermodynamics of the interaction of barnase and barstar: changes in free energy versus changes in enthalpy on mutation.
Journal of molecular biology 1997;267(3):696-706.
1997: Altamirano M M; Golbik R; Zahn R; Buckle A M; Fersht A R
Refolding chromatography with immobilized mini-chaperones.
Proceedings of the National Academy of Sciences of the United States of America 1997;94(8):3576-8.
1997: Buckle A M; Zahn R; Fersht A R
A structural model for GroEL-polypeptide recognition.
Proceedings of the National Academy of Sciences of the United States of America 1997;94(8):3571-5.
1997: Chène P; Day A G; Fersht A R
Role of isoleucine-164 at the active site of rubisco from Rhodospirillum rubrum.
Biochemical and biophysical research communications 1997;232(2):482-6.
1997: Fersht A R
Nucleation mechanisms in protein folding.
Current opinion in structural biology 1997;7(1):3-9.
1997: Nölting B; Golbik R; Neira J L; Soler-Gonzalez A S; Schreiber G; Fersht A R
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 1997;94(3):826-30.
1997: Ladurner A G; Itzhaki L S; Fersht A R
Strain in the folding nucleus of chymotrypsin inhibitor 2.
Folding & design 1997;2(6):363-8.
1996: Zahn R; Buckle A M; Perrett S; Johnson C M; Corrales F J; Golbik R; Fersht A R
Chaperone activity and structure of monomeric polypeptide binding domains of GroEL.
Proceedings of the National Academy of Sciences of the United States of America 1996;93(26):15024-9.
1996: Freund S M; Wong K B; Fersht A R
Initiation sites of protein folding by NMR analysis.
Proceedings of the National Academy of Sciences of the United States of America 1996;93(20):10600-3.
1996: Zahn R; Perrett S; Fersht A R
Conformational states bound by the molecular chaperones GroEL and secB: a hidden unfolding (annealing) activity.
Journal of molecular biology 1996;261(1):43-61.
1996: Wong K B; Freund S M; Fersht A R
Cold denaturation of barstar: 1H, 15N and 13C NMR assignment and characterisation of residual structure.
Journal of molecular biology 1996;259(4):805-18.
1996: Axe D D; Foster N W; Fersht A R
Active barnase variants with completely random hydrophobic cores.
Proceedings of the National Academy of Sciences of the United States of America 1996;93(11):5590-4.
1996: Schreiber G; Fersht A R
Rapid, electrostatically assisted association of proteins.
Nature structural biology 1996;3(5):427-31.
1996: Corrales F J; Fersht A R
Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage.
Proceedings of the National Academy of Sciences of the United States of America 1996;93(9):4509-12.
1996: Buckle A M; Cramer P; Fersht A R
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 1996;35(14):4298-305.
1996: Daggett V; Li A; Itzhaki L S; Otzen D E; Fersht A R
Structure of the transition state for folding of a protein derived from experiment and simulation.
Journal of molecular biology 1996;257(2):430-40.
1996: Oliveberg M; Fersht A R
Thermodynamics of transient conformations in the folding pathway of barnase: reorganization of the folding intermediate at low pH.
Biochemistry 1996;35(8):2738-49.
1996: Oliveberg M; Fersht A R
Formation of electrostatic interactions on the protein-folding pathway.
Biochemistry 1996;35(8):2726-37.
1996: Zahn R; Perrett S; Stenberg G; Fersht A R
Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB.
Science (New York, N.Y.) 1996;271(5249):642-5.
1996: Corrales F J; Fersht A R
Kinetic significance of GroEL14.(GroES7)2 complexes in molecular chaperone activity.
Folding & design 1996;1(4):265-73.
1996: Clarke J; Fersht A R
An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway.
Folding & design 1996;1(4):243-54.
1996: Neira J L; Fersht A R
An NMR study on the beta-hairpin region of barnase.
Folding & design 1996;1(3):231-41.
1996: Neira J L; Davis B; Ladurner A G; Buckle A M; Gay G de P; Fersht A R
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 1996;1(3):189-208.
1995: de Prat Gay G; Ruiz-Sanz J; Neira J L; Corrales F J; Otzen D E; Ladurner A G; Fersht A R
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 1995;254(5):968-79.
1995: Itzhaki L S; Otzen D E; Fersht A R
Nature and consequences of GroEL-protein interactions.
Biochemistry 1995;34(44):14581-7.
1995: Arcus V L; Vuilleumier S; Freund S M; Bycroft M; Fersht A R
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 1995;254(2):305-21.
1995: Itzhaki L S; Neira J L; Ruiz-Sanz J; de Prat Gay G; Fersht A R
Search for nucleation sites in smaller fragments of chymotrypsin inhibitor 2.
Journal of molecular biology 1995;254(2):289-304.
1995: Itzhaki L S; Otzen D E; Fersht A R
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 1995;254(2):260-88.
1995: Fersht A R
Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications.
Proceedings of the National Academy of Sciences of the United States of America 1995;92(24):10869-73.
1995: Nölting B; Golbik R; Fersht A R
Submillisecond events in protein folding.
Proceedings of the National Academy of Sciences of the United States of America 1995;92(23):10668-72.
1995: Matouschek A; Otzen D E; Itzhaki L S; Jackson S E; Fersht A R
Movement of the position of the transition state in protein folding.
Biochemistry 1995;34(41):13656-62.
1995: Otzen D E; Rheinnecker M; Fersht A R
Structural factors contributing to the hydrophobic effect: the partly exposed hydrophobic minicore in chymotrypsin inhibitor 2.
Biochemistry 1995;34(40):13051-8.
1995: Clarke J; Hounslow A M; Fersht A R
Disulfide mutants of barnase. II: Changes in structure and local stability identified by hydrogen exchange.
Journal of molecular biology 1995;253(3):505-13.
1995: Clarke J; Henrick K; Fersht A R
Disulfide mutants of barnase. I: Changes in stability and structure assessed by biophysical methods and X-ray crystallography.
Journal of molecular biology 1995;253(3):493-504.
1995: Frisch C; Schreiber G; Fersht A R
Characterization of in vitro oxidized barstar.
FEBS letters 1995;370(3):273-7.
1995: Perrett S; Clarke J; Hounslow A M; Fersht A R
Relationship between equilibrium amide proton exchange behavior and the folding pathway of barnase.
Biochemistry 1995;34(29):9288-98.
1995: Corrales F J; Fersht A R
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 1995;92(12):5326-30.
1995: Matthews J M; Fersht A R
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 1995;34(20):6805-14.
1995: Otzen D E; Fersht A R
Side-chain determinants of beta-sheet stability.
Biochemistry 1995;34(17):5718-24.
1995: Eder J; Fersht A R
Pro-sequence-assisted protein folding.
Molecular microbiology 1995;16(4):609-14.
1995: Fersht A R
Mapping the structures of transition states and intermediates in folding: delineation of pathways at high resolution.
Philosophical transactions of the Royal Society of London. Series B, Biological sciences 1995;348(1323):11-5.
1995: Schreiber G; Fersht A R
Energetics of protein-protein interactions: analysis of the barnase-barstar interface by single mutations and double mutant cycles.
Journal of molecular biology 1995;248(2):478-86.
1995: De Prat Gay G; Ruiz-Sanz J; Neira J L; Itzhaki L S; Fersht A R
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 1995;92(9):3683-6.
1995: Martínez J C; Filimonov V V; Mateo P L; Schreiber G; Fersht A R
A calorimetric study of the thermal stability of barstar and its interaction with barnase.
Biochemistry 1995;34(15):5224-33.
1995: First E A; Fersht A R
Analysis of the role of the KMSKS loop in the catalytic mechanism of the tyrosyl-tRNA synthetase using multimutant cycles.
Biochemistry 1995;34(15):5030-43.
1995: Chen Y W; Fersht A R; Henrick K
Crystallographic analysis of Phe-->Leu substitution in the hydrophobic core of barnase.
Acta crystallographica. Section D, Biological crystallography 1995;51(Pt 2):220-31.
1995: Shaw G L; Davis B; Keeler J; Fersht A R
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 1995;34(7):2225-33.
1995: Ruiz-Sanz J; de Prat Gay G; Otzen D E; Fersht A R
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 1995;34(5):1695-701.
1995: Fersht A R
Characterizing transition states in protein folding: an essential step in the puzzle.
Current opinion in structural biology 1995;5(1):79-84.
1995: Ibba M; Johnson C M; Hennecke H; Fersht A R
Increased rates of tRNA charging through modification of the enzyme-aminoacyl-adenylate complex of phenylalanyl-tRNA synthetase.
FEBS letters 1995;358(3):293-6.
1995: Kippen A D; Fersht A R
Analysis of the mechanism of assembly of cleaved barnase from two peptide fragments and its relevance to the folding pathway of uncleaved barnase.
Biochemistry 1995;34(4):1464-8.
1994: de Prat Gay G; Ruiz-Sanz J; Davis B; Fersht A R
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 1994;91(23):10943-6.
1994: Jackson S E; Fersht A R
Contribution of residues in the reactive site loop of chymotrypsin inhibitor 2 to protein stability and activity.
Biochemistry 1994;33(46):13880-7.
1994: Fersht A R; Itzhaki L S; elMasry N F; Matthews J M; Otzen D E
Single versus parallel pathways of protein folding and fractional formation of structure in the transition state.
Proceedings of the National Academy of Sciences of the United States of America 1994;91(22):10426-9.
1994: Otzen D E; Itzhaki L S; elMasry N F; Jackson S E; Fersht A R
Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding.
Proceedings of the National Academy of Sciences of the United States of America 1994;91(22):10422-5.
1994: Schreiber G; Buckle A M; Fersht A R
Stability and function: two constraints in the evolution of barstar and other proteins.
Structure (London, England : 1993) 1994;2(10):945-51.
1994: Arcus V L; Vuilleumier S; Freund S M; Bycroft M; Fersht A R
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 1994;91(20):9412-6.
1994: Matouschek A; Matthews J M; Johnson C M; Fersht A R
Extrapolation to water of kinetic and equilibrium data for the unfolding of barnase in urea solutions.
Protein engineering 1994;7(9):1089-95.
1994: Sanz J M; Johnson C M; Fersht A R
The A-state of barnase.
Biochemistry 1994;33(37):11189-99.
1994: Kippen A D; Arcus V L; Fersht A R
Structural studies on peptides corresponding to mutants of the major alpha-helix of barnase.
Biochemistry 1994;33(33):10013-21.
1994: Buckle A M; Schreiber G; Fersht A R
Protein-protein recognition: crystal structural analysis of a barnase-barstar complex at 2.0-A resolution.
Biochemistry 1994;33(30):8878-89.
1994: Lubienski M J; Bycroft M; Freund S M; Fersht A R
Three-dimensional solution structure and 13C assignments of barstar using nuclear magnetic resonance spectroscopy.
Biochemistry 1994;33(30):8866-77.
1994: Chen Y W; Fersht A R
Stability and solvation of Thr/Ser to Ala and Gly mutations at the N-cap of alpha-helices.
FEBS letters 1994;347(2-3):304-9.
1994: de Prat Gay G; Ruiz-Sanz J; Fersht A R
Generation of a family of protein fragments for structure-folding studies. 2. Kinetics of association of the two chymotrypsin inhibitor-2 fragments.
Biochemistry 1994;33(25):7964-70.
1994: de Prat Gay G; Fersht A R
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 1994;33(25):7957-63.
1994: elMasry N F; Fersht A R
Mutational analysis of the N-capping box of the alpha-helix of chymotrypsin inhibitor 2.
Protein engineering 1994;7(6):777-82.
1994: Jasanoff A; Davis B; Fersht A R
Detection of an intermediate in the folding of the (beta alpha)8-barrel N-(5'-phosphoribosyl)anthranilate isomerase from Escherichia coli.
Biochemistry 1994;33(20):6350-5.
1994: Sanz J M; Fersht A R
Measurement of barnase refolding rate constants under denaturing conditions.
FEBS letters 1994;344(2-3):216-20.
1994: Fersht A R
Jubilee Lecture. Pathway and stability of protein folding.
Biochemical Society transactions 1994;22(2):267-73.
1994: Martínez J C; el Harrous M; Filimonov V V; Mateo P L; Fersht A R
A calorimetric study of the thermal stability of barnase and its interaction with 3'GMP.
Biochemistry 1994;33(13):3919-26.
1994: Kippen A D; Sancho J; Fersht A R
Folding of barnase in parts.
Biochemistry 1994;33(12):3778-86.
1994: Jasanoff A; Fersht A R
Quantitative determination of helical propensities from trifluoroethanol titration curves.
Biochemistry 1994;33(8):2129-35.
1994: Buckle A M; Fersht A R
Subsite binding in an RNase: structure of a barnase-tetranucleotide complex at 1.76-A resolution.
Biochemistry 1994;33(7):1644-53.
1994: Rheinnecker M; Eder J; Pandey P S; Fersht A R
Variants of subtilisin BPN' with altered specificity profiles.
Biochemistry 1994;33(1):221-5.
1994: Harpaz Y; Elmasry N; Fersht A R; 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 1994;91(1):311-5.
1994: de Prat Gay G; Johnson C M; Fersht A R
Contribution of a proline residue and a salt bridge to the stability of a type I reverse turn in chymotrypsin inhibitor-2.
Protein engineering 1994;7(1):103-8.
1993: Jackson S E; Fersht A R
Contribution of long-range electrostatic interactions to the stabilization of the catalytic transition state of the serine protease subtilisin BPN'.
Biochemistry 1993;32(50):13909-16.
1993: Chen Y W; Fersht A R; Henrick K
Contribution of buried hydrogen bonds to protein stability. The crystal structures of two barnase mutants.
Journal of molecular biology 1993;234(4):1158-70.
1993: Eder J; Rheinnecker M; Fersht A R
Hydrolysis of small peptide substrates parallels binding of chymotrypsin inhibitor 2 for mutants of subtilisin BPN'.
FEBS letters 1993;335(3):349-52.
1993: First E A; Fersht A R
Mutational and kinetic analysis of a mobile loop in tyrosyl-tRNA synthetase.
Biochemistry 1993;32(49):13658-63.
1993: First E A; Fersht A R
Mutation of lysine 233 to alanine introduces positive cooperativity into tyrosyl-tRNA synthetase.
Biochemistry 1993;32(49):13651-7.
1993: First E A; Fersht A R
Involvement of threonine 234 in catalysis of tyrosyl adenylate formation by tyrosyl-tRNA synthetase.
Biochemistry 1993;32(49):13644-50.
1993: Sanz J M; Fersht A R
Rationally designing the accumulation of a folding intermediate of barnase by protein engineering.
Biochemistry 1993;32(49):13584-92.
1993: Buckle A M; Henrick K; Fersht A R
Crystal structural analysis of mutations in the hydrophobic cores of barnase.
Journal of molecular biology 1993;234(3):847-60.
1993: Clarke J; Hounslow A M; Bycroft M; Fersht A R
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 1993;90(21):9837-41.
1993: Gray T E; Eder J; Bycroft M; Day A G; Fersht A R
Refolding of barnase mutants and pro-barnase in the presence and absence of GroEL.
The EMBO journal 1993;12(11):4145-50.
1993: Lubienski M J; Bycroft M; Jones D N; Fersht A R
Assignment of the backbone 1H and 15N NMR resonances and secondary structure characterization of barstar.
FEBS letters 1993;332(1-2):81-7.
1993: Jackson S E; elMasry N; Fersht A R
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 1993;32(42):11270-8.
1993: Jackson S E; Moracci M; elMasry N; Johnson C M; Fersht A R
Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2.
Biochemistry 1993;32(42):11259-69.
1993: Schreiber G; Fersht A R
The refolding of cis- and trans-peptidylprolyl isomers of barstar.
Biochemistry 1993;32(41):11195-203.
1993: Meiering E M; Bycroft M; Lubienski M J; Fersht A R
Structure and dynamics of barnase complexed with 3'-GMP studied by NMR spectroscopy.
Biochemistry 1993;32(41):10975-87.
1993: Jones D N; Bycroft M; Lubienski M J; Fersht A R
Identification of the barstar binding site of barnase by NMR spectroscopy and hydrogen-deuterium exchange.
FEBS letters 1993;331(1-2):165-72.
1993: Serrano L; Day A G; Fersht A R
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 1993;233(2):305-12.
1993: Eder J; Rheinnecker M; Fersht A R
Folding of subtilisin BPN': role of the pro-sequence.
Journal of molecular biology 1993;233(2):293-304.
1993: Matouschek A; Fersht A R
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 1993;90(16):7814-8.
1993: Gray T E; Fersht A R
Refolding of barnase in the presence of GroE.
Journal of molecular biology 1993;232(4):1197-207.
1993: Loewenthal R; Sancho J; Reinikainen T; Fersht A R
Long-range surface charge-charge interactions in proteins. Comparison of experimental results with calculations from a theoretical method.
Journal of molecular biology 1993;232(2):574-83.
1993: Fersht A R
The sixth Datta Lecture. Protein folding and stability: the pathway of folding of barnase.
FEBS letters 1993;325(1-2):5-16.
1993: Avis J M; Fersht A R
Use of binding energy in catalysis: optimization of rate in a multistep reaction.
Biochemistry 1993;32(20):5321-6.
1993: Avis J M; Day A G; Garcia G A; Fersht A R
Reaction of modified and unmodified tRNA(Tyr) substrates with tyrosyl-tRNA synthetase (Bacillus stearothermophilus).
Biochemistry 1993;32(20):5312-20.
1993: Schreiber G; Fersht A R
Interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering.
Biochemistry 1993;32(19):5145-50.
1993: Clarke J; Fersht A R
Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation.
Biochemistry 1993;32(16):4322-9.
1993: Day A G; Chène P; Fersht A R
Role of phenylalanine-327 in the closure of loop 6 of ribulosebisphosphate carboxylase/oxygenase from Rhodospirillum rubrum.
Biochemistry 1993;32(8):1940-4.
1993: de Prat Gay G; Duckworth H W; Fersht A R
Modification of the amino acid specificity of tyrosyl-tRNA synthetase by protein engineering.
FEBS letters 1993;318(2):167-71.
1993: Rheinnecker M; Baker G; Eder J; Fersht A R
Engineering a novel specificity in subtilisin BPN'.
Biochemistry 1993;32(5):1199-203.
1993: Eder J; Rheinnecker M; Fersht A R
Folding of subtilisin BPN': characterization of a folding intermediate.
Biochemistry 1993;32(1):18-26.
1992: Horovitz A; Matthews J M; Fersht A R
Alpha-helix stability in proteins. II. Factors that influence stability at an internal position.
Journal of molecular biology 1992;227(2):560-8.
1992: Serrano L; Sancho J; Hirshberg M; Fersht A R
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 1992;227(2):544-59.
1992: Day A G; Parsonage D; Ebel S; Brown T; Fersht A R
Barnase has subsites that give rise to large rate enhancements.
Biochemistry 1992;31(28):6390-5.
1992: Chène P; Day A G; Fersht A R
Mutation of asparagine 111 of rubisco from Rhodospirillum rubrum alters the carboxylase/oxygenase specificity.
Journal of molecular biology 1992;225(3):891-6.
1992: Meiering E M; Serrano L; Fersht A R
Effect of active site residues in barnase on activity and stability.
Journal of molecular biology 1992;225(3):585-9.
1992: Serrano L; Matouschek A; Fersht A R
The folding of an enzyme. VI. The folding pathway of barnase: comparison with theoretical models.
Journal of molecular biology 1992;224(3):847-59.
1992: Matouschek A; Serrano L; Meiering E M; Bycroft M; Fersht A R
The folding of an enzyme. V. H/2H exchange-nuclear magnetic resonance studies on the folding pathway of barnase: complementarity to and agreement with protein engineering studies.
Journal of molecular biology 1992;224(3):837-45.
1992: Matouschek A; Serrano L; Fersht A R
The folding of an enzyme. IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedure.
Journal of molecular biology 1992;224(3):819-35.
1992: Serrano L; Matouschek A; Fersht A R
The folding of an enzyme. III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedure.
Journal of molecular biology 1992;224(3):805-18.
1992: Serrano L; Kellis J T; Cann P; Matouschek A; Fersht A R
The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability.
Journal of molecular biology 1992;224(3):783-804.
1992: Fersht A R; Matouschek A; Serrano L
The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding.
Journal of molecular biology 1992;224(3):771-82.
1992: Loewenthal R; Sancho J; Fersht A R
Histidine-aromatic interactions in barnase. Elevation of histidine pKa and contribution to protein stability.
Journal of molecular biology 1992;224(3):759-70.
1992: Sancho J; Neira J L; Fersht A R
An N-terminal fragment of barnase has residual helical structure similar to that in a refolding intermediate.
Journal of molecular biology 1992;224(3):749-58.
1992: Sancho J; Fersht A R
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 1992;224(3):741-7.
1992: Horovitz A; Fersht A R
Co-operative interactions during protein folding.
Journal of molecular biology 1992;224(3):733-40.
1992: Serrano L; Neira J L; Sancho J; Fersht A R
Effect of alanine versus glycine in alpha-helices on protein stability.
Nature 1992;356(6368):453-5.
1992: Sancho J; Serrano L; Fersht A R
Histidine residues at the N- and C-termini of alpha-helices: perturbed pKas and protein stability.
Biochemistry 1992;31(8):2253-8.
1992: Fersht A R; Matouschek A; Sancho J; Serrano L; Vuilleumier S
Pathway of protein folding.
Faraday discussions 1992;(93):183-93.
1991: Meiering E M; Bycroft M; Fersht A R
Characterization of phosphate binding in the active site of barnase by site-directed mutagenesis and NMR.
Biochemistry 1991;30(47):11348-56.
1991: Gray T E; Fersht A R
Cooperativity in ATP hydrolysis by GroEL is increased by GroES.
FEBS letters 1991;292(1-2):254-8.
1991: Jackson S E; Fersht A R
Folding of chymotrypsin inhibitor 2. 2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding.
Biochemistry 1991;30(43):10436-43.
1991: Jackson S E; Fersht A R
Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition.
Biochemistry 1991;30(43):10428-35.
1991: Sancho J; Meiering E M; Fersht A R
Mapping transition states of protein unfolding by protein engineering of ligand-binding sites.
Journal of molecular biology 1991;221(3):1007-14.
1991: Bycroft M; Ludvigsen S; Fersht A R; Poulsen F M
Determination of the three-dimensional solution structure of barnase using nuclear magnetic resonance spectroscopy.
Biochemistry 1991;30(35):8697-701.
1991: Sali D; Bycroft M; Fersht A R
Surface electrostatic interactions contribute little of stability of barnase.
Journal of molecular biology 1991;220(3):779-88.
1991: Loewenthal R; Sancho J; Fersht A R
Fluorescence spectrum of barnase: contributions of three tryptophan residues and a histidine-related pH dependence.
Biochemistry 1991;30(27):6775-9.
1991: Fothergill M D; Fersht A R
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 1991;30(21):5157-64.
1991: Horovitz A; Serrano L; Fersht A R
COSMIC analysis of the major alpha-helix of barnase during folding.
Journal of molecular biology 1991;219(1):5-9.
1991: Fersht A R; Bycroft M; Horovitz A; Kellis J T; Matouschek A; Serrano L
Pathway and stability of protein folding.
Philosophical transactions of the Royal Society of London. Series B, Biological sciences 1991;332(1263):171-6.
1991: Wells T N; Knill-Jones J W; Gray T E; Fersht A R
Kinetic and thermodynamic properties of wild-type and engineered mutants of tyrosyl-tRNA synthetase analyzed by pyrophosphate-exchange kinetics.
Biochemistry 1991;30(21):5151-6.
1991: Serrano L; Bycroft M; Fersht A R
Aromatic-aromatic interactions and protein stability. Investigation by double-mutant cycles.
Journal of molecular biology 1991;218(2):465-75.
1991: Fersht A R; Wells T N
Linear free energy relationships in enzyme binding interactions studied by protein engineering.
Protein engineering 1991;4(3):229-31.
1991: Matouschek A; Fersht A R
Protein engineering in analysis of protein folding pathways and stability.
Methods in enzymology 1991;202():82-112.
1990: Horovitz A; Serrano L; Avron B; Bycroft M; Fersht A R
Strength and co-operativity of contributions of surface salt bridges to protein stability.
Journal of molecular biology 1990;216(4):1031-44.
1990: Serrano L; Horovitz A; Avron B; Bycroft M; Fersht A R
Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double-mutant cycles.
Biochemistry 1990;29(40):9343-52.
1990: Horovitz A; Fersht A R
Strategy for analysing the co-operativity of intramolecular interactions in peptides and proteins.
Journal of molecular biology 1990;214(3):613-7.
1990: Bycroft M; Matouschek A; Kellis J T; Serrano L; Fersht A R
Detection and characterization of a folding intermediate in barnase by NMR.
Nature 1990;346(6283):488-90.
1990: Matouschek A; Kellis J T; Serrano L; Bycroft M; Fersht A R
Transient folding intermediates characterized by protein engineering.
Nature 1990;346(6283):440-5.
1990: Bycroft M; Sheppard R N; Lau F T; Fersht A R
Sequential assignment of the 1H nuclear magnetic resonance spectrum of barnase.
Biochemistry 1990;29(32):7425-32.
1990: Longstaff C; Campbell A F; Fersht A R
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 1990;29(31):7339-47.
1990: Ward W H; Timms D; Fersht A R
Protein engineering and the study of structure--function relationships in receptors.
Trends in pharmacological sciences 1990;11(7):280-4.
1990: Garcia G A; Leatherbarrow R J; Eckstein F; Fersht A R
Metal ion dependence of phosphorothioate ATP analogues in the Bacillus stearothermophilus tyrosyl-tRNA synthetase reaction.
Biochemistry 1990;29(6):1643-8.
1989: Serrano L; Fersht A R
Capping and alpha-helix stability.
Nature 1989;342(6247):296-9.
1989: Wells T N; Fersht A R
Protection of an unstable reaction intermediate examined with linear free energy relationships in tyrosyl-tRNA synthetase.
Biochemistry 1989;28(23):9201-9.
1989: Lau F T; Fersht A R
Dissection of the effector-binding site and complementation studies of Escherichia coli phosphofructokinase using site-directed mutagenesis.
Biochemistry 1989;28(17):6841-7.
1989: Matouschek A; Kellis J T; Serrano L; Fersht A R
Mapping the transition state and pathway of protein folding by protein engineering.
Nature 1989;340(6229):122-6.
1989: Kellis J T; Nyberg K; Fersht A R
Energetics of complementary side-chain packing in a protein hydrophobic core.
Biochemistry 1989;28(11):4914-22.
1989: Mossakowska D E; Nyberg K; Fersht A R
Kinetic characterization of the recombinant ribonuclease from Bacillus amyloliquefaciens (barnase) and investigation of key residues in catalysis by site-directed mutagenesis.
Biochemistry 1989;28(9):3843-50.
1989: Fersht A R; Sternberg M J
Can a simple function for the dielectric response model electrostatic effects in globular proteins?
Protein engineering 1989;2(7):527-30.
1988: Sali D; Bycroft M; Fersht A R
Stabilization of protein structure by interaction of alpha-helix dipole with a charged side chain.
Nature 1988;335(6192):740-3.
1988: Bycroft M; Fersht A R
Assignment of histidine resonances in the 1H NMR (500 MHz) spectrum of subtilisin BPN' using site-directed mutagenesis.
Biochemistry 1988;27(19):7390-4.
1988: Ward W H; Fersht A R
Tyrosyl-tRNA synthetase acts as an asymmetric dimer in charging tRNA. A rationale for half-of-the-sites activity.
Biochemistry 1988;27(15):5525-30.
1988: Kellis J T; Nyberg K; Sali D; Fersht A R
Contribution of hydrophobic interactions to protein stability.
Nature 1988;333(6175):784-6.
1988: Fersht A R
Relationships between apparent binding energies measured in site-directed mutagenesis experiments and energetics of binding and catalysis.
Biochemistry 1988;27(5):1577-80.
1988: Fersht A R; Knill-Jones J W; Bedouelle H; Winter G
Reconstruction by site-directed mutagenesis of the transition state for the activation of tyrosine by the tyrosyl-tRNA synthetase: a mobile loop envelopes the transition state in an induced-fit mechanism.
Biochemistry 1988;27(5):1581-7.
1988: Ward W H; Fersht A R
Asymmetry of tyrosyl-tRNA synthetase in solution.
Biochemistry 1988;27(3):1041-9.
1987: Fersht A R
Linear free energy relationships are valid!
Protein engineering 1987;1(6):442-5.
1987: Fersht A R
Dissection of the structure and activity of the tyrosyl-tRNA synthetase by site-directed mutagenesis.
Biochemistry 1987;26(25):8031-7.
1987: Leatherbarrow R J; Fersht A R
Investigation of transition-state stabilization by residues histidine-45 and threonine-40 in the tyrosyl-tRNA synthetase.
Biochemistry 1987;26(26):8524-8.
1987: Borgford T J; Gray T E; Brand N J; Fersht A R
Site-directed mutagenesis reveals transition-state stabilization as a general catalytic mechanism for aminoacyl-tRNA synthetases.
Biochemistry 1987;26(23):7246-50.
1987: Sternberg M J; Hayes F R; Russell A J; Thomas P G; Fersht A R
Prediction of electrostatic effects of engineering of protein charges.
Nature 1987;330(6143):86-8.
1987: Lowe D M; Winter G; Fersht A R
Structure-activity relationships in engineered proteins: characterization of disruptive deletions in the alpha-ammonium group binding site of tyrosyl-tRNA synthetase.
Biochemistry 1987;26(19):6038-43.
1987: Fersht A R; Leatherbarrow R J; Wells T N
Structure-activity relationships in engineered proteins: analysis of use of binding energy by linear free energy relationships.
Biochemistry 1987;26(19):6030-8.
1987: Russell A J; Fersht A R
Rational modification of enzyme catalysis by engineering surface charge.
Nature 1987;328(6130):496-500.
1987: Lau F T; Fersht A R; Hellinga H W; Evans P R
Site-directed mutagenesis in the effector site of Escherichia coli phosphofructokinase.
Biochemistry 1987;26(13):4143-8.
1987: Ward W H; Jones D H; Fersht A R
Effects of engineering complementary charged residues into the hydrophobic subunit interface of tyrosyl-tRNA synthetase. Appendix: Kinetic analysis of dimeric enzymes that reversibly dissociate into inactive subunits.
Biochemistry 1987;26(13):4131-8.
1987: Borgford T J; Brand N J; Gray T E; Fersht A R
The valyl-tRNA synthetase from Bacillus stearothermophilus has considerable sequence homology with the isoleucyl-tRNA synthetase from Escherichia coli.
Biochemistry 1987;26(9):2480-6.
1987: Lau F T; Fersht A R
Conversion of allosteric inhibition to activation in phosphofructokinase by protein engineering.
Nature 1987;326(6115):811-2.
1987: Russell A J; Thomas P G; Fersht A R
Electrostatic effects on modification of charged groups in the active site cleft of subtilisin by protein engineering.
Journal of molecular biology 1987;193(4):803-13.
1986: Jones M D; Brand N J; Fersht A R
Single-stranded M13 DNA: use as a cloning vector.
Nucleic acids research 1986;14(24):10116.
1986: Wells T N; Ho C K; Fersht A R
Free energy of hydrolysis of tyrosyl adenylate and its binding to wild-type and engineered mutant tyrosyl-tRNA synthetases.
Biochemistry 1986;25(21):6603-8.
1986: Leatherbarrow R J; Fersht A R
Protein engineering.
Protein engineering 1986;1(1):7-16.
1986: Ward W H; Jones D H; Fersht A R
Protein engineering of homodimeric tyrosyl-tRNA synthetase to produce active heterodimers.
The Journal of biological chemistry 1986;261(21):9576-8.
1986: Ho C K; Fersht A R
Internal thermodynamics of position 51 mutants and natural variants of tyrosyl-tRNA synthetase.
Biochemistry 1986;25(8):1891-7.
1986: Wells T N; Fersht A R
Use of binding energy in catalysis analyzed by mutagenesis of the tyrosyl-tRNA synthetase.
Biochemistry 1986;25(8):1881-6.
1986: Jones M D; Lowe D M; Borgford T; Fersht A R
Natural variation of tyrosyl-tRNA synthetase and comparison with engineered mutants.
Biochemistry 1986;25(8):1887-91.
1986: Brand N J; Fersht A R
Molecular cloning of the gene encoding the valyl-tRNA synthetase from Bacillus stearothermophilus.
Gene 1986;44(1):139-42.
1985: Leatherbarrow R J; Fersht A R; 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 1985;82(23):7840-4.
1985: Jones D H; McMillan A J; Fersht A R; Winter G
Reversible dissociation of dimeric tyrosyl-tRNA synthetase by mutagenesis at the subunit interface.
Biochemistry 1985;24(21):5852-7.
1985: Fersht A R; Wilkinson A J; Carter P; Winter G
Fine structure-activity analysis of mutations at position 51 of tyrosyl-tRNA synthetase.
Biochemistry 1985;24(21):5858-61.
1985: Lowe D M; Fersht A R; Wilkinson A J; Carter P; Winter G
Probing histidine-substrate interactions in tyrosyl-tRNA synthetase using asparagine and glutamine replacements.
Biochemistry 1985;24(19):5106-9.
1985: Bedouelle H; Carter P; Waye M M; Winter G; Lowe D M; Wilkinson A J; Fersht A R
Engineering of tyrosyl tRNA synthetase.
Biochimie 1985;67(7-8):737-43.
1985: Fersht A R; Shi J P; Knill-Jones J; Lowe D M; Wilkinson A J; Blow D M; Brick P; Carter P; Waye M M; Winter G
Hydrogen bonding and biological specificity analysed by protein engineering.
Nature 1985;314(6008):235-8.
1985: Fersht A R; Winter G P
Redesigning enzymes by site-directed mutagenesis.
Ciba Foundation symposium 1985;111():204-18.
1984: Carter P J; Winter G; Wilkinson A J; Fersht A R
The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus).
Cell 1984;38(3):835-40.
1984: Shi J P; Fersht A R
Fidelity of DNA replication under conditions used for oligodeoxynucleotide-directed mutagenesis.
Journal of molecular biology 1984;177(2):269-78.
1984: Winter G; Carter P; Waye M M; Blow D M; Wilkinson A J; Shi J P; Fersht A R
Genetic dissection of tyrosyl-tRNA synthetase.
Biochemical Society transactions 1984;12(2):224-5.
1984: Wilkinson A J; Fersht A R; Blow D M; Carter P; Winter G
A large increase in enzyme-substrate affinity by protein engineering.
Nature 1984;307(5947):187-8.
1984: Grosse F; Krauss G; Knill-Jones J W; Fersht A R
Replication of phi X174 DNA by calf thymus DNA polymerase-alpha: measurement of error rates at the amber-16 codon.
Advances in experimental medicine and biology 1984;179():535-40.
1984: Fersht A R
Fidelity of DNA replication in vitro.
Advances in experimental medicine and biology 1984;179():525-33.
1983: Cotterill S M; Fersht A R
Direct observation of complexes of ssb and recA proteins with a fluorescent single-stranded deoxyribonucleic acid derivative.
Biochemistry 1983;22(25):5878-81.
1983: Wilkinson A J; Fersht A R; Blow D M; Winter G
Site-directed mutagenesis as a probe of enzyme structure and catalysis: tyrosyl-tRNA synthetase cysteine-35 to glycine-35 mutation.
Biochemistry 1983;22(15):3581-6.
1983: Silver M S; Fersht A R
Investigation of binding between recA protein and single-stranded polynucleotides with the aid of a fluorescent deoxyribonucleic acid derivative.
Biochemistry 1983;22(12):2860-6.
1983: Fersht A R; Shi J P; Tsui W C
Kinetics of base misinsertion by DNA polymerase I of Escherichia coli.
Journal of molecular biology 1983;165(4):655-67.
1983: Fersht A R; Knill-Jones J W
Contribution of 3' leads to 5' exonuclease activity of DNA polymerase III holoenzyme from Escherichia coli to specificity.
Journal of molecular biology 1983;165(4):669-82.
1983: Fersht A R; Knill-Jones J W
Fidelity of replication of bacteriophage phi X174 DNA in vitro and in vivo.
Journal of molecular biology 1983;165(4):633-54.
1983: Grosse F; Krauss G; Knill-Jones J W; Fersht A R
Accuracy of DNA polymerase-alpha in copying natural DNA.
The EMBO journal 1983;2(9):1515-9.
1983: Waye M M; Winter G; Wilkinson A J; Fersht A R
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 1983;2(10):1827-9.
1982: Silver M S; Fersht A R
Direct observation of complexes formed between recA protein and a fluorescent single-stranded deoxyribonucleic acid derivative.
Biochemistry 1982;21(24):6066-72.
1982: Winter G; Fersht A R; Wilkinson A J; Zoller M; Smith M
Redesigning enzyme structure by site-directed mutagenesis: tyrosyl tRNA synthetase and ATP binding.
Nature 1982;299(5885):756-8.
1982: Cotterill S M; Satterthwait A C; Fersht A R
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 1982;21(18):4332-7.
1982: Fersht A R; Knill-Jones J W; Tsui W C
Kinetic basis of spontaneous mutation. Misinsertion frequencies, proofreading specificities and cost of proofreading by DNA polymerases of Escherichia coli.
Journal of molecular biology 1982;156(1):37-51.
1981: Tsui W C; Fersht A R
Probing the principles of amino acid selection using the alanyl-tRNA synthetase from Escherichia coli.
Nucleic acids research 1981;9(18):4627-37.
1981: Fersht A R
Enzymic editing mechanisms and the genetic code.
Proceedings of the Royal Society of London. Series B, Containing papers of a Biological character. Royal Society (Great Britain) 1981;212(1189):351-79.
1981: Jakubowski H; Fersht A R
Alternative pathways for editing non-cognate amino acids by aminoacyl-tRNA synthetases.
Nucleic acids research 1981;9(13):3105-17.
1981: Fersht A R; Knill-Jones J W
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 1981;78(7):4251-5.
1980: Fersht A R; Shindler J S; Tsui W C
Probing the limits of protein-amino acid side chain recognition with the aminoacyl-tRNA synthetases. Discrimination against phenylalanine by tyrosyl-tRNA synthetases.
Biochemistry 1980;19(24):5520-4.

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