Alan R Fersht


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Person Info

NAME

Alan R

SURNAME

Fersht

Publications in SciGraph latest 50 shown

  • 2018-08 Correction: Energy-dependent nucleolar localization of p53 in vitro requires two discrete regions within the p53 carboxyl terminus in ONCOGENE
  • 2010-04 Molecular basis of S100 proteins interacting with the p53 homologs p63 and p73 in ONCOGENE
  • 2009-12 Awakening guardian angels: drugging the p53 pathway in NATURE REVIEWS CANCER
  • 2009-05 Regulation by phosphorylation of the relative affinities of the N-terminal transactivation domains of p53 for p300 domains and Mdm2 in ONCOGENE
  • 2008-08 From the first protein structures to our current knowledge of protein folding: delights and scepticisms in NATURE REVIEWS MOLECULAR CELL BIOLOGY
  • 2007-05 Energy-dependent nucleolar localization of p53 in vitro requires two discrete regions within the p53 carboxyl terminus in ONCOGENE
  • 2007-04 Structure–function–rescue: the diverse nature of common p53 cancer mutants in ONCOGENE
  • 2007-02 Structural Biology: Analysis of 'downhill' protein folding in NATURE
  • 2007 Understanding the Effects of Cancer-Associated Mutations in the Tumor Suppressor Protein p53: Structural Consequences of Mutations and Possible Ways of Rescuing Oncogenic Mutants in PROTEIN MISFOLDING, AGGREGATION, AND CONFORMATIONAL DISEASES
  • 2007 Wild Type p53 Conformation, Structural Consequences of p53 Mutations and Mechanisms of Mutant p53 Rescue in 25 YEARS OF P53 RESEARCH
  • 2005-10 Solution structure of a protein denatured state and folding intermediate in NATURE
  • 2005-08 The crystal structure of human CD1d with and without α-galactosylceramide in NATURE IMMUNOLOGY
  • 2003-06 The present view of the mechanism of protein folding in NATURE REVIEWS MOLECULAR CELL BIOLOGY
  • 2003-02 The complete folding pathway of a protein from nanoseconds to microseconds in NATURE
  • 2002-05 retraction: Directed evolution of new catalytic activity using the α/β-barrel scaffold in NATURE
  • 2002-03 Characterization of the p53-rescue drug CP-31398 in vitro and in living cells in ONCOGENE
  • 2002-02-01 Loss of a metal-binding site in gelsolin leads to familial amyloidosis–Finnish type in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 2002 Barnase: Fluorescence Analysis of A Three Tryptophan Protein in TOPICS IN FLUORESCENCE SPECTROSCOPY
  • 2001-10 Rescuing the function of mutant p53 in NATURE REVIEWS CANCER
  • 2000-03 Quantitative analysis of residual folding and DNA binding in mutant p53 core domain: definition of mutant states for rescue in cancer therapy in ONCOGENE
  • 2000-02 Directed evolution of new catalytic activity using the α/β-barrel scaffold in NATURE
  • 1999-02 Oxidative refolding chromatography: folding of the scorpion toxin Cn5 in NATURE BIOTECHNOLOGY
  • 1999-02-01 Mechanism of folding and assembly of a small tetrameric protein domain from tumor suppressor p53 in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 1999-01-01 Upper limit of the time scale for diffusion and chain collapse in chymotrypsin inhibitor 2 in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 1996-05 Rapid, electrostatically assisted association of proteins in NATURE STRUCTURAL & MOLECULAR BIOLOGY
  • 1990-08 Transient folding intermediates characterized by protein engineering in NATURE
  • 1990-08 Detection and characterization of a folding intermediate in barnase by NMR in NATURE
  • 1990-02 Folding pathway enigma in NATURE
  • 1989-11 Capping and α-helix stability in NATURE
  • 1989-07 Mapping the transition state and pathway of protein folding by protein engineering in NATURE
  • 1988-10 Stabilization of protein structure by interaction of α-helix dipole with a charged side chain in NATURE
  • 1988-06 Contribution of hydrophobic interactions to protein stability in NATURE
  • 1988 Altering the Structure of Enzymes by Site-Directed Mutagenesis in REDESIGNING THE MOLECULES OF LIFE
  • 1987 The Role of Separate Domains and of Individual Amino-Acids in Enzyme Catalysis, Studied by Site-Directed Mutagenesis in CRYSTALLOGRAPHY IN MOLECULAR BIOLOGY
  • 1986-07 Quantitative analysis of structure–activity relationships in engineered proteins by linear free-energy relationships in NATURE
  • 1986-06 Commercial samples of subtilisin BPN′ in NATURE
  • 1986 The Study and Redesign of Enzymes by Protein Engineering in ENZYMES AS CATALYSTS IN ORGANIC SYNTHESIS
  • 1986 Protein Engineering in BIOTECHNOLOGY: POTENTIALS AND LIMITATIONS
  • 1985-08 Hydrogen bonding in enzymatic catalysis analysed by protein engineering in NATURE
  • 1985-03 Hydrogen bonding and biological specificity analysed by protein engineering in NATURE
  • 1984 Replication of ΦX174 DNA by Calf Thymus DNA Polymerase-α: Measurement of Error Rates at the Amber-16 Codon in PROTEINS INVOLVED IN DNA REPLICATION
  • 1984 Fidelity of DNA Replication in Vitro in PROTEINS INVOLVED IN DNA REPLICATION
  • 1984 Studying Enzyme-Substrate Interactions by Site-Directed Mutagenesis in SPECIFICITY IN BIOLOGICAL INTERACTIONS
  • 1984-01 A large increase in enzyme–substrate affinity by protein engineering in NATURE
  • 1982-10 Redesigning enzyme structure by site-directed mutagenesis: tyrosyl tRNA synthetase and ATP binding in NATURE
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