Dept of Biological Sciences | Our staff | Emeritus staff | Professor Christine Slingsby
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Professor Christine Slingsby

Emeritus Professor of Structural Biology

Contact details

email: c.slingsby@mail.cryst.bbk.ac.uk
office: room G54, extension building, Malet Street, London WC1E 7HX

About Professor Christine Slingsby

Research interests

    • The origin of the vertebrate eye lens
    • Interactions of crystallins, refractive index and transparency
    • The structure of alpha-crystallin and related small heat shock proteins
    • Changes to eye lens crystallins in cataract
    • The role of small heat shock proteins in neuromuscular systems
    • Small heat shock proteins in aging and disease

Selected recent publications

  • Papers

    Crystal structure of R120G disease mutant of human alphaB-crystallin domain dimer shows closure of a groove. Clark, A.R., Naylor, C.E., Bagnéris, C., Keep, N.H. and Slingsby, C. (2011) J. Mol. Biol. 408:118-134.

    Explosive expansion of gamma-crystallin genes in the ancestral vertebrate. Kappe, G., Purkiss, A.G., van Genesen, S.T., Slingsby, C. and Lubsen, N.H. (2010) J. Mol. Evol. 71:219-230.

    Crystal structures of alpha-crystallin domain dimers of alphaB-crystallin and Hsp20. Bagneris, C., Bateman, O.A., Naylor, C.E., Cronin, N., Boelens, W.C., Keep, N.H. and Slingsby, C. (2009) J. Mol. Biol. 392:1242-1252.

    Urochordate bg-crystallin and the evolutionary origin of the vertebrate eye lens. Shimeld, S.M., Purkiss, A.G., Dirks, R.P.H., Bateman, O.A., Slingsby, C. & Lubsen, N.H. (2005) Curr. Biol. 15:1684-1689.

    Wrapping the a-crystallin domain fold in a chaperone assembly. Stamler, R., Kappé, G., Boelens, W. & Slingsby, C. (2005) J. Mol. Biol. 353: 68-79.

    The P23T cataract mutation causes loss of solubility of folded gD-crystallin. Evans, P., Wyatt, K., Wistow, G.J., Bateman, O. A., Wallace, B.A. and Slingsby, C. (2004) J. Mol. Biol. 343:435-444.

    Characterisation of the G91del CRYBA1/3-crystallin protein: a cause of human inherited cataract. Reddy, M.A., Bateman, O.A., Chakarova, C., Ferris, J., Berry, V., Lomas, E., Sarra, R., Smith, M.A., Moore, A.T., Bhattacharya, S.S. and Slingsby, C. (2004) Hum. Mol. Genetics, 13:945-953.

     

    Reviews

    Functions of crystallins in and out of the lens: Roles in elongated and post-mitotic cells. Slingsby, C & Wistow GJ. (2014) Progress in Biophys & Mol Biol. In press

    Flexible Nanoassembly for Sequestering Non-Native Proteins. Slingsby, C. & Clark, AR. (2013) Structure 21: 193-194.

    Evolution of crystallins for a role in the vertebrate eye lens. Slingsby, C., Wistow, GJ, Clark AR. (2013) Protein Science 22: 367-380.

    sHSP in the eye lens: Crystallin mutations, cataract and proteostasis. Clark AR, Lubsen, NH. & Slingsby, C. (2012) Int J Biochem Cell Biol 44: 1687-1697.

    Breaking down order to keep cells tidy. Slingsby, C. & Clark, AR. (2012) Chemistry & Biology 19: 547-548.

    Structure and Evolution of Crystallins. Wistow, G. and Slingsby, C. (2010). In “The Encyclopedia of the Eye” (Ed. D.A. Dartt, J.C. Besharse, R. Dana Vol 2, 229-238. Elsevier.

    Ageing and vision: structure, stability and function of lens crystallins. Bloemendal, H., de Jong, W., Jaenicke, R., Lubsen, N.H., Slingsby, C. and Tardieu, A. (2004) Progress Biophys & Mol. Biol. 86, 407-485.