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Trends in Pharmacological Sciences|July 1, 1990
Protein engineering and the study of structure--function relationships in receptorsW H Ward, D Timms, A R FershtBiochemistry|July 26, 1988
Tyrosyl-tRNA synthetase acts as an asymmetric dimer in charging tRNA. A rationale for half-of-the-sites activityW H Ward, A R FershtThe Journal of Biological Chemistry|July 25, 1986
Protein engineering of homodimeric tyrosyl-tRNA synthetase to produce active heterodimersW H Ward, D H Jones, A R FershtBiochemistry|June 30, 1987
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 subunitsW H Ward, D H Jones, A R FershtBiochemistry|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 FershtPageof 36