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Nature|August 6, 1987
Rational modification of enzyme catalysis by engineering surface chargeA J Russell, A R FershtJournal of Molecular Biology|February 20, 1987
Electrostatic effects on modification of charged groups in the active site cleft of subtilisin by protein engineeringA J Russell, P G Thomas, A R FershtNature|November 5, 1987
Prediction of electrostatic effects of engineering of protein chargesM J Sternberg, F R Hayes, A J Russell, et al.Biochemistry|March 8, 1988
Relationships between apparent binding energies measured in site-directed mutagenesis experiments and energetics of binding and catalysisA R FershtProceedings of the National Academy of Sciences of the United States of America|March 4, 2000
Transition-state structure as a unifying basis in protein-folding mechanisms: contact order, chain topology, stability, and the extended nucleus mechanismA R FershtProceedings of the National Academy of Sciences of the United States of America|November 21, 1995
Optimization of rates of protein folding: the nucleation-condensation mechanism and its implicationsA R FershtCurrent Opinion in Structural Biology|February 1, 1995
Characterizing transition states in protein folding: an essential step in the puzzleA R FershtBiochemistry|December 15, 1987
Dissection of the structure and activity of the tyrosyl-tRNA synthetase by site-directed mutagenesisA R FershtFEBS Letters|June 28, 1993
The sixth Datta Lecture. Protein folding and stability: the pathway of folding of barnaseA R FershtPhilosophical Transactions of the Royal Society of London. Series B, Biological Sciences|April 29, 1995
Mapping the structures of transition states and intermediates in folding: delineation of pathways at high resolutionA R FershtPageof 40