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The Biochemical Journal|January 1, 1992
Mechanistic and active-site studies on D(--)-mandelate dehydrogenase from Rhodotorula graminisD P Baker, C Kleanthous, J N Keen, et al.
The Journal of Biological Chemistry|June 15, 1991
Stabilization of the shikimate pathway enzyme dehydroquinase by covalently bound ligandC Kleanthous, M Reilly, A Cooper, et al.
Biochemistry|February 21, 1998
Specificity in protein-protein recognition: conserved Im9 residues are the major determinants of stability in the colicin E9 DNase-Im9 complexR Wallis, K Y Leung, M J Osborne, et al.
Biochemistry|August 26, 1998
Dual recognition and the role of specificity-determining residues in colicin E9 DNase-immunity protein interactionsW Li, S J Hamill, A M Hemmings, et al.
Molecular Microbiology|November 9, 2000
A 76-residue polypeptide of colicin E9 confers receptor specificity and inhibits the growth of vitamin B12-dependent Escherichia coli 113/3 cellsC N Penfold, C Garinot-Schneider, A M Hemmings, et al.
Protein Science : a Publication of the Protein Society|October 25, 2000
NMR investigation of the interaction of the inhibitor protein Im9 with its partner DNaseR Boetzel, M Czisch, R Kaptein, et al.
Journal of Inorganic Biochemistry|June 1, 2000
NMR studies of metal ion binding to the Zn-finger-like HNH motif of colicin E9J P Hannan, S B Whittaker, A M Hemmings, et al.
The Biochemical Journal|June 26, 1998
A structural comparison of the colicin immunity proteins Im7 and Im9 gives new insights into the molecular determinants of immunity-protein specificityC A Dennis, H Videler, R A Pauptit, et al.
Biochemistry|October 18, 1994
Sequential assignments and identification of secondary structure elements of the colicin E9 immunity protein in solution by homonuclear and heteronuclear NMRM J Osborne, L Y Lian, R Wallis, et al.
Biochemistry|October 24, 1995
Protein-protein interactions in colicin E9 DNase-immunity protein complexes. 2. Cognate and noncognate interactions that span the millimolar to femtomolar affinity rangeR Wallis, K Y Leung, A J Pommer, et al.
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