Search Results - "FERSHT, A. R"

Structure-function-rescue: the diverse nature of common p53 cancer mutants by Joerger, A C, Fersht, A R

“…The tumor suppressor protein p53 is inactivated by mutation in about half of all human cancers. Most mutations are located in the DNA-binding domain of the…”
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The tumor suppressor p53: from structures to drug discovery by Joerger, Andreas C, Fersht, Alan R

“…Even 30 years after its discovery, the tumor suppressor protein p53 is still somewhat of an enigma. p53's intimate and multifaceted role in the cell cycle is…”
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Regulation by phosphorylation of the relative affinities of the N-terminal transactivation domains of p53 for p300 domains and Mdm2 by Teufel, D P, Bycroft, M, Fersht, A R

“…The transcriptional activity of the tumour suppressor, p53, requires direct binding between its transactivation domain (TAD, 1–57) and the transcriptional…”
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Solution structure of a protein denatured state and folding intermediate by Markson, J. S, Freund, S. M. V, Fersht, A. R, Religa, T. L, Mayor, U

“…The most controversial area in protein folding concerns its earliest stages. Questions such as whether there are genuine folding intermediates, and whether the…”
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Molecular basis of S100 proteins interacting with the p53 homologs p63 and p73 by van Dieck, J, Brandt, T, Teufel, D P, Veprintsev, D B, Joerger, A C, Fersht, A R

“…S100 proteins modulate p53 activity by interacting with its tetramerization (p53TET, residues 325–355) and transactivation (residues 1–57) domains. In this…”
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Time-Resolved Fluorescence Resonance Energy Transfer Study Shows a Compact Denatured State of the B Domain of Protein A by Huang, F, Lerner, E, Sato, S, Amir, D, Haas, E, Fersht, A. R

“…The B domain of protein A (BDPA), a three-helix bundle of 60 residues, folds via a nucleation−condensation mechanism in apparent two-state kinetics. We have…”
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Optimization of Rates of Protein Folding: The Nucleation-Condensation Mechanism and Its Implications by Fersht, Alan R.

“…Small, single-module proteins that fold in a single cooperative step may be paradigms for understanding early events in protein-folding pathways generally…”
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Quantitative analysis of residual folding and DNA binding in mutant p53 core domain : definition of mutant states for rescue in cancer therapy by BULLOCK, A. N, HENCKEL, J, FERSHT, A. R

“…The tumour suppressor p53 is mutated in half of all human cancers, most frequently with missense substitutions in its core domain. We present a new assessment…”
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Importance of Two Buried Salt Bridges in the Stability and Folding Pathway of Barnase by Tissot, A. C, Vuilleumier, S, Fersht, A. R

“…The importance of two buried salt bridges in barnase in the stability of its folded state, the major transition state for unfolding, and a folding intermediate…”
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Single-Molecule characterization of oligomerization kinetics and equilibria of the tumor suppressor p53 by Rajagopalan, Sridharan, Huang, Fang, Fersht, Alan R

“…The state of oligomerization of the tumor suppressor p53 is an important factor in its various biological functions. It has a well-defined tetramerization…”
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Application of Physical Organic Chemistry to Engineered Mutants of Proteins: Hammond Postulate Behavior in the Transition State of Protein Folding by Matouschek, Andreas, Fersht, Alan R.

“…Transition states in protein folding may be analyzed by linear free-energy relationships (LFERs) analogous to the Bronsted equation for changes in reactivity…”
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Quantitative Determination of Helical Propensities from Trifluoroethanol Titration Curves by Jasanoff, Alan, Fersht, Alan R

“…The formation of local secondary structure is an essential step in the folding of a polypeptide from a random coil to a well-defined native conformation…”
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Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation by Clarke, Jane, Fersht, Alan R

“…Disulfide bridges have been introduced into barnase to act as probes of folding. One disulfide (between residues 85 and 102) links two loops known to pack…”
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Interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering by Schreiber, Gideon, Fersht, Alan R

“…Barnase, an extracellular ribonuclease of Bacillus amyloliquefaciens, forms a very tight complex with its intracellular polypeptide inhibitor barstar. At pH 8,…”
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Negative Activation Enthalpies in the Kinetics of Protein Folding by Oliveberg, Mikael, Tan, Yee-Joo, Fersht, Alan R.

“…Although the rates of chemical reactions become faster with increasing temperature, the converse may be observed with protein-folding reactions. The rate…”
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Catalysis of Amide Proton Exchange by the Molecular Chaperones GroEL and SecB by Zahn, Ralph, Perrett, Sarah, Stenberg, Gun, Fersht, Alan R.

“…Hydrogen-deuterium exchange of 39 amide protons of Bacillus amyloliquefaciens ribonuclease (barnase) was analyzed by two-dimensional nuclear magnetic resonance…”
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Sieves in Sequence by Fersht, Alan R.

“…The structure of the isoleucyl-tRNA synthetase, now revealed in molecular detail, provides the resolution to how the isoleucine-selective enzyme excludes…”
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Oxidative refolding chromatography: folding of the scorpion toxin Cn5 by Fersht, Alan R, Altamirano, Myriam M, García, Consuelo, Possani, Lourival D

“…We have made an immobilized and reusable molecular chaperone system for oxidative refolding chromatography. Its three components-GroEL minichaperone (191-345),…”
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PRIMA-1 Reactivates Mutant p53 by Covalent Binding to the Core Domain by 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.

“…Restoration of wild-type p53 expression triggers cell death and eliminates tumors in vivo. The identification of mutant p53-reactivating small molecules such…”
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Capping and α-helix stability by Serrano, Luis, Fersht, Alan R

“…The first and last four residues of alpha-helices differ from the rest by not being able to make the intrehelical hydrogen bonds between the backbone greater…”
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