Structural and mechanistic studies of Escherichia coli nitroreductase with the antibiotic nitrofurazone. Reversed binding orientations in different redox states of the enzyme von Race, Paul R, Lovering, Andrew L, Green, Richard M, Ossor, Abdelmijd, White, Scott A, Searle, Peter F, Wrighton, Christopher J, Hyde, Eva I

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NITROREDUCTASE: A PRODRUG-ACTIVATING ENZYME FOR CANCER GENE THERAPY von Searle, Peter F, Chen, Ming-Jen, Hu, Longqin, Race, Paul R, Lovering, Andrew L, Grove, Jane I, Guise, Chris, Jaberipour, Mansooreh, James, Nicholas D, Mautner, Vivien, Young, Lawrence S, Kerr, David J, Mountain, Andrew, White, Scott A, Hyde, Eva I

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Generation of Escherichia coli nitroreductase mutants conferring improved cell sensitization to the prodrug CB1954 von GROVE, Jane I, LOVERING, Andrew L, GUISE, Christopher, RACE, Paul R, WRIGHTON, Christopher J, WHITE, Scott A, HYDE, Eva I, SEARLE, Peter F

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Nitroaryl Phosphoramides as Novel Prodrugs for E. coli Nitroreductase Activation in Enzyme Prodrug Therapy von Hu, Longqin, Yu, Chengzhi, Jiang, Yongying, Han, Jiye, Li, Zhuorong, Browne, Patrick, Race, Paul R, Knox, Richard J, Searle, Peter F, Hyde, Eva I

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A simple mechanism for co-dependence on two activators at an Escherichia coli promoter von Wade, Joseph T., Belyaeva, Tamara A., Hyde, Eva I., Busby, Stephen J.W.

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Transcription activation at the Escherichia coli melAB promoter: interactions of MelR with its DNA target site and with domain 4 of the RNA polymerase σ subunit von Grainger, David C., Webster, Christine L., Belyaeva, Tamara A., Hyde, Eva I., Busby, Stephen J. W.

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Transcription activation at the Escherichia coli melAB promoter: interactions of MelR with the C‐terminal domain of the RNA polymerase α subunit von Grainger, David C., Belyaeva, Tamara A., Lee, David J., Hyde, Eva I., Busby, Stephen J. W.

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Binding of the Escherichia coli MelR protein to the melAB promoter: orientation of MelR subunits and investigation of MelR–DNA contacts von Grainger, David C., Belyaeva, Tamara A., Lee, David J., Hyde, Eva I., Busby, Stephen J. W.

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Trp Repressor−Operator Binding: NMR and Electrophoretic Mobility Shift Studies of the Effect of DNA Sequence and Corepressor Binding on Two Trp Repressor−Operator Complexes von Jaseja, Mahesh, Jeeves, Mark, Hyde, Eva I

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Secondary structure and DNA binding by the C‐terminal domain of the transcriptional activator NifA from Klebsiella pneumoniae von Ray, Pampa, Smith, K. John, Parslow, Rosemary A., Dixon, Ray, Hyde, Eva I.

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Transcription activation at the Escherichia coli melAB promoter: the role of MelR and the cyclic AMP receptor protein von Belyaeva, Tamara A., Wade, Joseph T., Webster, Christine L., Howard, Victoria J., Thomas, Mark S., Hyde, Eva I., Busby, Stephen J. W.

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Repression of the Escherichia coli melR promoter by MelR: evidence that efficient repression requires the formation of a repression loop von Wade, Joseph T., Belyaeva, Tamara A., Hyde, Eva I., Busby, Stephen J. W.

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DNA binding and DNA bending by the MelR transcription activator protein from Escherichia coli von Bourgerie, Sylvain J., Michán, Carmen M., Busby, Stephen J.W., Hyde, Eva I., Thomas, Mark S.

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The Escherichia coli MelR transcription activator: production of a stable fragment containing the DNA-binding domain von Michán, C M, Busby, S J, Hyde, E I

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Secondary structure of the C-terminal DNA-binding domain of the transcriptional activator NifA from Klebsiella pneumoniae: spectroscopic analyses von Missaillidis, S, Jaseja, M, Ray, P, Chittock, R, Wharton, C W, Drake, A F, Buck, M, Hyde, E I

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Flexibility of KorA, a plasmid-encoded, global transcription regulator, in the presence and the absence of its operator von Rajasekar, KV, Lovering, AL, Dancea, F, Scott, DJ, Harris, SA, Bingle, LEH, Roessle, M, Thomas, CM, Hyde, EI, White, SA

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Studies of the Escherichia coli Trp repressor binding to its five operators and to variant operator sequences von Jeeves, Mark, Evans, Paul D., Parslow, Rosemary A., Jaseja, Mahesh, Hyde, Eva I.

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Interactions of Bacillus subtilis RNA polymerase with subunits determining the specificity of initiation. Sigma and delta peptides can bind simultaneously to core von Hyde, E I, Hilton, M D, Whiteley, H R

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Proton nuclear magnetic resonance saturation transfer studies of coenzyme binding to Lactobacillus casei dihydrofolate reductase von Hyde, E. I, Birdsall, B, Roberts, G. C. K, Feeney, J, Burgen, A. S. V

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NMR studies of the activation of the Escherichia coli trp repressor von HYDE, Eva I., RAMESH, Vasudevan, FREDERICK, Ronnie, ROBERTS, Gordon C. K.

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