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Trends in Biochemical Sciences|October 9, 2001
Immunity proteins: enzyme inhibitors that avoid the active siteC Kleanthous, D WalkerActa Crystallographica. Section D, Biological Crystallography|November 28, 2000
Crystallization of the cytotoxic domain of a ribosome-inactivating colicin in complex with its immunity proteinS Carr, D Walker, R James, et al.Structure (London, England : 1993)|September 15, 2000
Inhibition of a ribosome-inactivating ribonuclease: the crystal structure of the cytotoxic domain of colicin E3 in complex with its immunity proteinS Carr, D Walker, R James, et al.The Journal of Biological Chemistry|July 5, 1990
Reversible alkylation of an active site methionine residue in dehydroquinaseC Kleanthous, J R CogginsThe Biochemical Journal|October 1, 1984
Analysis of the mechanism of chloramphenicol acetyltransferase by steady-state kinetics. Evidence for a ternary-complex mechanismC Kleanthous, W V ShawFolia Microbiologica|December 10, 1999
Translational regulation by modifications of the elongation factor TuB Kraal, C Lippmann, C KleanthousThe Biochemical Journal|October 1, 1996
Conformational changes and the role of metals in the mechanism of type II dehydroquinase from Aspergillus nidulansJ R Bottomley, A R Hawkins, C KleanthousThe Journal of Biological Chemistry|July 5, 1990
Active site labeling of the shikimate pathway enzyme, dehydroquinase. Evidence for a common substrate binding site within dehydroquinase and dehydroquinate synthaseC Kleanthous, D G Campbell, J R CogginsThe Journal of Biological Chemistry|November 5, 1992
Identification of the essential histidine residue at the active site of Escherichia coli dehydroquinaseR K Deka, C Kleanthous, J R CogginsBiochemistry|September 24, 1985
3-(Bromoacetyl)chloramphenicol, an active site directed inhibitor for chloramphenicol acetyltransferaseC Kleanthous, P M Cullis, W V ShawPageof 299