BRAMHAM, Janice - University of Edinburgh - School of Biological Sciences

个人简介

1993 PhD, St Andrews University 1992-94 CRC Postdoctoral Research Assistant, Dept. of Biochemistry, University of Dundee 1994 NIH Postdoctoral Research Assistant, Dept. of Chemistry and Biochemistry, University of San Diego 1994-97 CRC Postdoctoral Research Assistant, Dept. of Biochemistry, University of Dundee 1997-2000 BBSRC Postdoctoral Research Fellow, Institute of Cell and Molecular Biology, University of Edinburgh 2000-02 Wellcome Trust Postdoctoral Research Fellow, Dept. of Biochemistry, University of Leicester 2002-04 MRC Postdoctoral Research Fellow, Department of Chemistry, University of Edinburgh 2004-08 Lecturer, Department of Biological Sciences, University of Edinburgh 2008-2014 Manager of Biophysical Characterisation Facility, CTCB, University of Edinburgh 2014-current Lecturer and Programme Director for MSc Biochemistry, University of Edinburgh

研究领域

I am interested in the three-dimensional structures, intrinsic dynamics and interactions of biological macromolecules with the ultimate aim of understanding their structure-function relationships. Current work is focused upon multi-domain, disulphide-bonded, glycoslyated proteins, many of which act as membrane receptors, including: proteins of the human complement system, which plays an essential role in our immune response to infection; proteins involved in bone metabolism, in order to understand the molecular basis of bone diseases; yolk proteins of insect pests, in order to find potential targets for crop management in developing countries

近期论文

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The mitosis and neurodevelopment proteins NDE1 and NDEL1 form dimers, tetramers and polymers with a folded-back structure in solution.Soares, D. C., Bradshaw, N. J., Zou, J., Kennaway, C. K., Hamilton, R. S., Chen, Z. A., Wear, M. A., Blackburn, E. A., Bramham, J., Boettcher, B., Millar, J. K., Barlow, P. N., Walkinshaw, M. D., Rappsilber, J. & Porteous, D. J. (2012) J. Biol. Chem. 287, 32381-32393. A novel p53 phosphorylation site within the MDM2 ubiquitination sSignal: II. A model in which phosphorylation at Ser269 induces a mutant conformation to p53.Fraser, J. A., Madhumalar, A., Blackburn, E., Bramham, J., Walkinshaw, M. D., Verma, C. & Hupp, T. R. (2010) J. Biol. Chem. 285, 37773-37786. Actinidine and glucose from the defensive secretion of the stick insect Megacrania nigrosulfurea.Prescott, T., Bramham, J., Zompro, O. & Maciver, S. K. (2009) Biochem. Syst. & Ecol. 37, 759-760. Solution structure of factor I-like modules from complement C7 reveals a pair of follistatin domains in compact pseudosymmetric arrangementPhelan, M. M., Thai, C-T., Soares, D. C., Ogata, R. T., Barlow, P. N. & Bramham, J. (2009) J. Biol. Chem. 284, 19637-19649. A function for the RING finger domain in the allosteric control of MDM2 conformation and activity.Wawrzynow, B., Pettersson, S., Zylicz, A., Bramham, J., Worrall, E., Hupp, T. R. & Ball, K. L. (2009) J. Biol. Chem. 284, 11517-11530. ZZ domain of dystrophin and utrophin: topology and mapping of a beta-dystroglycan interaction siteHnia, K., Zouiten, D., Cantel, S., Chazalette, D., Hugon, G., Fehrentz, J-A., Masmoudi, A., Diment, A., Bramham, J., Mornet, D. & Winder, S. J. (2007) Biochem. J. 401, 667-77. Structural diversity in p160/CREB-binding protein coactivator complexes.Waters, L., Yue, B., Veverka, V., Renshaw, P., Bramham, J., Matsuda, S., Frenkiel, T., Kelly, G., Muskett, F., Carr, M. & Heery, D. M. (2006) J. Biol. Chem. 281, 14787-95. Functional insights from the structure of the multifunctional C345C domain of C5 of complement.Bramham, J., Thai, C-T., Soares, D. C., Uhrín, D., Ogata, R. T. & Barlow, P. ( 2005) J. Biol. Chem. 280, 10636-10645. Solution structure of the calponin CH domain and fitting to the 3D-helical reconstruction of F-actin : calponin.Bramham, J., Hodgkinson, J. L., Smith, B. O., Uhrin, D., Barlow, P. N. & Winder, S. J. (2002) Structure. 10,249-258. Lithium in BiologyBramham, J. (1999). in 'Perspectives in Bioinorganic Chemistry', Hay, R.W., ed., J.A.I. Press Inc. 1-61.