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The use of a genetically engineered tryptophan to identify the movement of a domain of B. stearothermophilus lactate dehydrogenase with the process which limits the steady-state turnover of the enzymeAdam Waldman, J. John Holbrook, Dale B. Wigley et al.|Biochemical and Biophysical Research Communications|1988Cited by 66
Changes in the state of subunit association of lactate dehydrogenase from Bacillus stearothermophilusAnthony R. Clarke, J. John Holbrook, Adam Waldman et al.|Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology|1985Cited by 49
The rates of defined changes in protein structure during the catalytic cycle of lactate dehydrogenaseAnthony R. Clarke, J. John Holbrook, Adam Waldman et al.|Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology|1985Cited by 41
The use of site-directed mutagenesis and time-resolved fluorescence spectroscopy to assign the fluorescence contributions of individual tryptophan residues in Bacillus stearothermophilus lactate dehydrogenaseAdam Waldman, J. John Holbrook, Anthony R. Clarke et al.|Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology|1987Cited by 23