Hyde, Eva - University of Birmingham

个人简介

After her PhD in NMR studies of coenzyme binding to the enzyme dihydrofolate reductase, in NIMR, London, Eva Hyde spent seven months at the University of Cambridge and then went to the University of Washington for five years. She studied tRNA structure using NMR spectroscopy, for two years, and was in the Dept. of Microbiology studying transcription by B.subtilis RNA Polymerase for three years. She returned to England in 1986, obtaining an MRC project grant for NMR studies on the structure of Trp repressor, at the University of Leicester. In 1989 she obtained a Welcome Trust Senior fellowship and shortly thereafter became a lecturer at the University of Birmingham. Here she continued her research on the structures and interactions of DNA-binding proteins, including Trp repressor, MelR, NifA and KorA. She also determined the structures of two snake toxins with similar function but very different 3D structure, by NMR spectroscopy. She is currently studying the kinetics and specificity of nitroreductase, an enzyme with potential for cancer gene therapy, and also the structure and interactions of the DNA-partitioning protein, KorB.

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Rajasekar, K.V.; Tul Muntaha, S.; Tame, J.R.H.; Kommareddy, S.: Morris, G.; Wharton, C.W.; Thomas, C.M.; White, S.A.; Hyde, E.I. and Scott D.J. (2010). Order and disorder in the domain organisation of the plasmid partition protein KorB. J. Biol. Chem. 285 (20) 15440-15449. Jaberipour M., Guise, C.P., Grove, J.I., Knox, R.J., Hu, L., Hyde, E.I. and Searle, P.F. (2010) Testing double mutants of the enzyme nitroreductase for enhanced cell sensitization to prodrugs: effects of combining beneficial single mutations. Biochem. Pharmacol. 79 (2) 102-111. Jarrom, D., Jaberipour M., Guise, C.P., Daff, S., White, S.A., Searle, P.F., and Hyde, E.I. (2009) Steady-state and stopped-flow kinetic studies of three E. coli NfsB mutants with enhanced activity for the prodrug CB1954. Biochemistry 48, (32) 7665-7672. Vass, S.O., Jarrom, D., Wilson, W.R., Hyde E.I., and Searle, P.F. (2009) E. coli NfsA; an alternative nitroreductase for prodrug activation gene therapy in conjunction with CB1954. Br. J. Cancer 100, 1903-1911. Bingle, L.E.H., Rajasekar, K.V., tul Muntaha, S., Nadella, V., Hyde, E.I., and Thomas, C.M. (2008) A single aromatic residue in transcriptional repressor protein KorA is critical for cooperativity with its coregulator KorB. Mol. Micro 70 (6) 1502-1514. Smith, K.J., Baillie, G.S., HydeE.I., Li Xiang, Li, Houslay, T.M., McCahill, A., Dunlop, A.J.; Bolger, G.B., Klussmann, E., Adams, D.R., and Houslay, M.D. (2007) Functional and structural characterisation of a cAMP-specific phosphodiesterase-4D5 (PDE4D5) N-terminal region peptide that disrupts PDE4D5 interaction with the signalling scaffold proteins, b-arrestin and RACK1. Cellular Signalling, 19, 2612-2624. Race, P.R., Lovering, A.L., White, S.A, Grove, J.I., Searle, P.F., Wrighton, C.J., and Hyde, E.I. (2007) Kinetic and structural characterization of Escherichia coli Nitroreductase mutants showing improved efficacy for the prodrug substrate CB1954. J. Mol. Biol., 368, 481-492 Guise, C.P., Grove, J.I., Mountain, A., Hyde, E.I. and Searle, P.F. (2007) Direct positive selection for improved nitroreductase variants. Gene Therapy, 14 , 690-698. Rajasekar, K. V., Bingle, L.E.H., Thomas, C.M. and Hyde, E.I. (2006) Letter to the Editor: 1H, 13C and 15N assignments of the KorA global transcriptional repressor protein from the low copy number IncP-1 plasmid, RK2. J. Biomol. NMR 36, 71