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Journal of Molecular Biology|January 20, 1987
The efficiency of folding of some proteins is increased by controlled rates of translation in vivo. A hypothesisI J Purvis, A J Bettany, T C Santiago, et al.
Biochemical Society Transactions|May 30, 2003
Experiences with the shikimate-pathway enzymes as targets for rational drug designJ R Coggins, C Abell, L B Evans, et al.
The Journal of Biological Chemistry|May 23, 1998
Re-evaluating the role of His-143 in the mechanism of type I dehydroquinase from Escherichia coli using two-dimensional 1H,13C NMRA P Leech, R Boetzel, C McDonald, et al.
International Journal for Parasitology|January 9, 2004
A complete shikimate pathway in Toxoplasma gondii: an ancient eukaryotic innovationS A Campbell, T A Richards, E J Mui, et al.
Nature Structural Biology|June 9, 1999
The two types of 3-dehydroquinase have distinct structures but catalyze the same overall reactionD G Gourley, A K Shrive, I Polikarpov, et al.
The Biochemical Journal|October 1, 1993
Characterization of the type I dehydroquinase from Salmonella typhiJ D Moore, A R Hawkins, I G Charles, et al.
Biochemical Society Transactions|May 30, 2003
Twists and turns: a tale of two shikimate-pathway enzymesK A Brown, E P Carpenter, K A Watson, et al.
The Biochemical Journal|March 15, 1992
A comparison of the enzymological and biophysical properties of two distinct classes of dehydroquinase enzymesC Kleanthous, R Deka, K Davis, et al.
The Biochemical Journal|February 1, 1996
Comparative analysis of the QUTR transcription repressor protein and the three C-terminal domains of the pentafunctional AROM enzymeH K Lamb, J D Moore, J H Lakey, et al.
The Biochemical Journal|February 5, 1999
The folding and assembly of the dodecameric type II dehydroquinasesN C Price, D J Boam, S M Kelly, et al.
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