Search Results - "Roberts, G. C. K."

A variety of roles for versatile zinc in metallo-β-lactamases by Karsisiotis, A. I, Damblon, C. F, Roberts, G. C. K

“…Metallo-β-lactamases are important as a major source of resistance of pathogenic bacteria to the widely used β-lactam antibiotics. They show considerable…”
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A Model for Human Cytochrome P450 2D6 Based on Homology Modeling and NMR Studies of Substrate Binding by Modi, S, Paine, M. J, Sutcliffe, M. J, Lian, L.-Y, Primrose, W. U, Wolf, C. R, Roberts, G. C. K

“…The cytochrome P450 responsible for the debrisoquine/sparteine polymorphism (P450 2D6) has been produced in large quantities by expression of a modified cDNA…”
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Insights into drug metabolism by cytochromes P450 from modelling studies of CYP2D6‐drug interactions by Maréchal, J‐D, Kemp, C A, Roberts, G C K, Paine, M J I, Wolf, C R, Sutcliffe, M J

“…The cytochromes P450 (CYPs) comprise a vast superfamily of enzymes found in virtually all life forms. In mammals, xenobiotic metabolizing CYPs provide crucial…”
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Folding and unfolding for binding: large-scale protein dynamics in protein-protein interactions by Roberts, G C K

“…The role of dynamics in the function of proteins, from enzymes to signalling proteins, is widely recognized. In many cases, the dynamic process is a relatively…”
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1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine as a Substrate of Cytochrome P450 2D6:  Allosteric Effects of NADPH−Cytochrome P450 Reductase by Modi, S, Gilham, D. E, Sutcliffe, M. J, Lian, L.-Y, Primrose, W. U, Wolf, C. R, Roberts, G. C. K

“…1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), a neurotoxin that produces Parkinsonism symptoms in man, has been examined as a substrate of recombinant…”
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A novel aldehyde reductase with activity towards a metabolite of aflatoxin B1 is expressed in rat liver during carcinogenesis and following the administration of an anti-oxidant by JUDAH, D. J, HAYES, J. D, YANG, J.-C, LIAN, L.-Y, ROBERTS, G. C. K, FARMER, P. B, LAMB, J. H, NEAL, G. E

“…In contrast with fractions from control animals, an aldehyde reductase, which catalyses the reduction of aflatoxin B1-dihydrodiol, in the dialdehyde form at…”
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Molecular analysis of the regulation of nisin immunity by Dodd, H.M, Horn, N, Chan, W.C, Giffard, C.J, Bycroft, B.W, Roberts, G.C.K, Gasson, M.J

“…The genetic determinants controlling immunity to nisin are coordinately regulated, along with biosynthesis genes, in response to an environmental signal, nisin…”
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Changes in the structure of bovine phospholipase A2 upon micelle binding by Kilby, P M, Primrose, W U, Roberts, G C

“…Phospholipase A2 (PLA2) is a calcium-dependent enzyme which hydrolyses the 2-acyl ester bond of phospholipids. The extracellular PLA2s are activated by as much…”
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A novel post-translational modification of the peptide antibiotic subtilin : isolation and characterization of a natural variant from Bacillus subtilis A.T.C.C. 6633 by CHAN, W. C, BYCROFT, B. W, LEYLAND, M. L, LU-YUN LIAN, ROBERTS, G. C. K

“…A variant of the peptide antibiotic subtilin has been isolated from Bacillus subtilis A.T.C.C. 6633, and its structure has been shown to be [N…”
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The conformation of echinomycin in solution by Cheung, H. T, Feeney, J, Roberts, G. C. K, Williams, D. H, Ughetto, G, Waring, M. J

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A kinetic study of wild-type and mutant dihydrofolate reductases from Lactobacillus casei by Andrews, J, Fierke, C. A, Birdsall, B, Ostler, G, Feeney, J, Roberts, G. C. K, Benkovic, S. J

“…A kinetic scheme is presented for Lactobacillus casei dihydrofolate reductase that predicts steady-state kinetic parameters. This scheme was derived from…”
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Dihydrofolate reductase: multiple conformations and alternative modes of substrate binding by Birdsall, B, Feeney, J, Tendler, S. J. B, Hammond, S. J, Roberts, G. C. K

“…The complex of Lactobacillus casei dihydrofolate reductase with the substrate folate and the coenzyme NADP+ has been shown to exist in solution as a mixture of…”
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Role of the Active-Site Carboxylate in Dihydrofolate Reductase: Kinetic and Spectroscopic Studies of the Aspartate 26 .fwdarw. Asparagine Mutant of the Lactobacillus casei Enzyme by Basran, J, Casarotto, M. G, Barsukov, I. L, Roberts, G. C. K

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Dihydrofolate reductase; sequential resonance assignments using 2D and 3D NMR and secondary structure determination in solution by Carr, M. D, Birdsall, B, Frenkiel, T. A, Bauer, C. J, Jimenez-Barbero, J, Polshakov, V. I, McCormick, J. E, Roberts, G. C. K, Feeney, J

“…Three-dimensional (3D) heteronuclear NMR techniques have been used to make sequential 1H and 15N resonance assignments for most of the residues of…”
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Direct n.m.r. evidence for substrate-induced conformational changes in a β-lactamase by JAMIN, M, DAMBLON, C, BAUDUIN-MISSELYN, A.-M, DURANT, F, ROBERTS, G. C. K, CHARLIER, P, LLABRES, G, FRERE, J.-M

“…Cefoxitin and other beta-lactam antibiotics with a methoxy group on the alpha-face behave as very poor substrates of the Bacillus licheniformis beta-lactamase…”
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Analysis of the binding of 1,3-diacetylchloramphenicol to chloramphenicol acetyltransferase by isotope-edited proton NMR and site-directed mutagenesis by Derrick, J. P, Lian, L. Y, Roberts, G. C. K, Shaw, W. V

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Dynamics of Trimethoprim Bound to Dihydrofolate Reductase by Searle, M. S., Forster, M. J., Birdsall, B., Roberts, G. C. K., Feeney, J., Cheung, H. T. A., Kompis, I., Geddes, A. J.

“…The conformation of a small molecule in its binding site on a protein is a major factor in the specificity of the interaction between them. In this paper, we…”
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Binding of coenzyme analogs to Lactobacillus casei dihydrofolate reductase: binary and ternary complexes by Birdsall, B, Burgen, A. S. V, Roberts, G. C. K

“…The binding, or association, constants of NADP+ NADPH, and a series of structural analogues to dihydrofolate reductase from Lactobacillus casei MTX/R have been…”
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NMR studies of multiple conformations in complexes of Lactobacillus casei dihydrofolate reductase with analogs of pyrimethamine by Birdsall, B, Tendler, S. J. B, Arnold, J. R. P, Feeney, J, Griffin, R. J, Carr, M. D, Thomas, J. A, Roberts, G. C. K, Stevens, M. F. G

“…1H and 19F NMR signals from bound ligands have been assigned in one- and two-dimensional NMR spectra of complexes of Lactobacillus casei dihydrofolate…”
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NMR studies of differences in the conformations and dynamics of ligand complexes formed with mutant dihydrofolate reductases by Birdsall, B, Andrews, J, Ostler, G, Tendler, S. J. B, Feeney, J, Roberts, G. C. K, Davies, R. W, Cheung, H. T. A

“…Two mutants of Lactobacillus casei dihydrofolate reductase, Trp 21---Leu and Asp 26---Glu, have been prepared by using site-directed mutagenesis methods, and…”
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