Alan R. Fersht

发表

Protein engineering: basic research and biotechnology

Alan R. Fersht, 1993 .

Energy transfer and specific fluorescence quenching effects in barnase, studied via multifrequency phase-fluorometry of tryptophan mutants

Alan R. Fersht, Matheus Froeyen, Yves Engelborghs, 1992, Photonics West - Lasers and Applications in Science and Engineering.

Solution structure of p53 core domain: Structural basis for its instability

Alan R. Fersht, Henning Tidow, A. Fersht, 2006, Proceedings of the National Academy of Sciences of the United States of America.

Protein folding from a highly disordered denatured state: The folding pathway of chymotrypsin inhibitor 2 at atomic resolution

Valerie Daggett, Alan R. Fersht, A. Fersht, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Basis of biological specificity

Alan R. Fersht, A. Fersht, 1984 .

Interaction of the p53 DNA-Binding Domain with Its N-Terminal Extension Modulates the Stability of the p53 Tetramer

Alan R. Fersht, Carol V. Robinson, Andreas C. Joerger, 2011, Journal of molecular biology.

Folding and binding: implementing the game plan

Valerie Daggett, Alan R. Fersht, A. Fersht, 2007 .

Core domain interactions in full-length p53 in solution

Antonina Andreeva, Alan R. Fersht, Dmitry B. Veprintsev, 2006, Proceedings of the National Academy of Sciences of the United States of America.

Mechanism of folding and assembly of a small tetrameric protein domain from tumor suppressor p53

Alan R. Fersht, Mauricio G. Mateu, A. Fersht, 1999, Nature Structural Biology.

Stabilization of protein structure by interaction of α-helix dipole with a charged side chain

Alan R. Fersht, A. Fersht, M. Bycroft, 1988, Nature.

Engineering a two-helix bundle protein for folding studies

Alan R. Fersht, Neil Ferguson, A. Fersht, 2010, Protein engineering, design & selection : PEDS.

Directed evolution of new catalytic activity using the α/β-barrel scaffold

Alan R. Fersht, Jonathan M. Blackburn, A. Fersht, 2000, Nature.

Structure and activity of the tyrosy1-tRNA synthetase: the hydrogen bond in catalysis and specificity

Alan R. Fersht, Robin J. Leatherbarrow, Timothy N. C. Wells, 1986, Philosophical Transactions of the Royal Society of London. Series A, Mathematical and Physical Sciences.

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

Markus O. Zimmermann, Frank M. Boeckler, Alan R. Fersht, 2015, ACS chemical biology.

The Crystal Structure of Human CD1b with a Bound Bacterial Glycolipid12

Alan R. Fersht, Dawn Shepherd, Nathan R. Zaccai, 2003, The Journal of Immunology.

Prediction of electrostatic effects of engineering of protein charges

Alan R. Fersht, Alan J. Russell, A. Fersht, 1987, Nature.

Chemical physics of protein folding

Peter G. Wolynes, Alan R. Fersht, William A. Eaton, 1998, Proceedings of the National Academy of Sciences.

Multiple conformations of full-length p53 detected with single-molecule fluorescence resonance energy transfer

Liming Ying, A. J. Bain, Nick Nicolaou, 2009, Proceedings of the National Academy of Sciences.

Oxidative refolding chromatography: folding of the scorpion toxin Cn5

Alan R. Fersht, A. Fersht, L. Possani, 1999, Nature Biotechnology.

Awakening guardian angels: drugging the p53 pathway

Alan R. Fersht, Christopher J. Brown, Sonia Lain, 2009, Nature Reviews Cancer.

Halogen-Enriched Fragment Libraries as Leads for Drug Rescue of Mutant p53

Markus O. Zimmermann, Frank M. Boeckler, Alan R. Fersht, 2012, Journal of the American Chemical Society.

Tailoring the pH dependence of enzyme catalysis using protein engineering

Alan R. Fersht, Alan J. Russell, A. Fersht, 1985, Nature.

Capping and α-helix stability

Alan R. Fersht, Luis Serrano, A. Fersht, 1989, Nature.

Combined Molecular Dynamics and Φ-Value Analysis of Structure−Reactivity Relationships in the Transition State and Unfolding Pathway of Barnase: Structural Basis of Hammond and Anti-Hammond Effects

Valerie Daggett, Alan R. Fersht, A. Fersht, 1998 .

New Look and New Outlook

Alan R. Fersht, Wayne A. Hendrickson, Carl-Ivar Brändén, 2002 .

Binding energy and catalysis: a lesson from protein engineering of the tyrosyl-tRNA synthetase

Alan R. Fersht, Robin J. Leatherbarrow, Timothy N. C. Wells, 1986 .

Redesigning enzyme structure by site-directed mutagenesis: tyrosyl tRNA synthetase and ATP binding

Alan R. Fersht, Anthony J. Wilkinson, Mark Zoller, 1982, Nature.

The complete folding pathway of a protein from nanoseconds to microseconds

Valerie Daggett, Alan R. Fersht, J. Günter Grossmann, 2003, Nature.

Quantitative analysis of structure–activity relationships in engineered proteins by linear free-energy relationships

Alan R. Fersht, Robin J. Leatherbarrow, A. Fersht, 1986, Nature.

Determination of the three-dimensional solution structure of barnase using nuclear magnetic resonance spectroscopy

Alan R. Fersht, Flemming M. Poulsen, A. Fersht, 1991 .

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

Alan R. Fersht, Andreas C. Joerger, A. Fersht, 2011, Journal of the American Chemical Society.

Small molecule induced reactivation of mutant p53 in cancer cells

Alan R. Fersht, Rainer Wilcken, Andreas C. Joerger, 2013, Nucleic acids research.

The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus)

Alan R. Fersht, Anthony J. Wilkinson, A. Fersht, 1984, Cell.

Analysis of Enzyme Structure and Activity by Protein Engineering

Alan R. Fersht, David M. Blow, Anthony J. Wilkinson, 1984 .

From the first protein structures to our current knowledge of protein folding: delights and scepticisms

Alan R. Fersht, A. Fersht, 2008, Nature Reviews Molecular Cell Biology.