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Professor David Moss

Emeritus Professor of Biomolecular Structure

Contact details

tel: 020 7631 6802
email: d.moss@cryst.bbk.ac.uk

About Professor David Moss

Research highlights

Professor David Moss and Professor Barnes gave a talk at Science Week 2014: Crystallography: past, present and future [view video (72 mins) on our Science Youtube channel]

Research interests

Recent publications

  • Yelland, T.S. and Naylor, Claire E. and Bagoban, T. and Savva, Christos G. and Moss, David S. and McClane, B.A. and Blasig, I.E. and Popoff, M. and Basak, Ajit K. (2014) Structure of a C. perfringens Enterotoxin mutant in complex with a Modified Claudin-2 Extracellular Loop 2.  Journal of Molecular Biology 426 (18), pp. 3134-3147. ISSN 0022-2836.

    Pentiah, Kevin and Lees, William D. and Moss, David S. and Shepherd, Adrian J. (2014) N-linked glycans on influenza A H3N2 hemagglutinin constrain binding of host antibodies, but shielding is limited. Glycobiology, ISSN 0959-6658. (In Press)

    Bokori-Brown, M. and Hall, C.A. and Vance, C. and Fernandes da Costa, S.P. and Savva, Christos G. and Naylor, Claire E. and Cole, Ambrose R. and Basak, Ajit K. and Moss, David S. and Titball, R.W. (2014) Clostridium perfringens epsilon toxin mutant Y30A-Y196A as a recombinant vaccine candidate against enterotoxemia. Vaccine 32 (23), pp. 2682-2687. ISSN 0264-410X.

    da Costa, S. and Savva, Christos G. and Bokori-Brown, M. and Naylor, Claire E. and Moss, David S. and Basak, Ajit K. and Titball, R. (2014) Identification of a key residue for Oligomerisation and pore-formation of Clostridium perfringens NetB. Toxins 6 (3), pp. 1049-1061. ISSN 2072-6651.

    Lees, William D. and Moss, David S. and Shepherd, Adrian J. (2014) Evolution in the influenza A H3 stalk - a challenge for broad-spectrum vaccines? Journal of General Virology 95 (2), pp. 317-324. ISSN 0022-1317. .

    Bokori-Brown, M. and Kokkinidou, M.C. and Savva, Christos G. and Fernandes da Costa, S.P. and Naylor, Claire E. and Cole, Ambrose R. and Moss, David S. and Basak, Ajit K. and Titball, R.W. (2013) Clostridium perfringensepsilon toxin H149A mutant as a platform for receptor binding studies. Protein Science 22 (5), pp. 650-659. ISSN 0961-8368.

    Ashford, Paul and Moss, David S. and Alex, A. and Yeap, S.K. and Povia, Alice and Nobeli, Irilenia and Williams, Mark A. (2012) Visualization of variable binding pockets on protein surfaces by probabilistic analysis of related structure sets. BMC Bioinformatics 13 , p. 39. ISSN 1471-2105.

    Briggs, David C. and Naylor, Claire E. and Smedley, J.G. and Lukoyanova, Natalya and Robertson, S. and Moss, David S. and McClane, B.A. and Basak, Ajit K. (2011) Structure of the food-poisoning Clostridium perfringens enterotoxin reveals similarity to the aerolysin-like pore-forming toxins. Journal of Molecular Biology 413 (1), pp. 138-149. ISSN 0022-2836.

    Lees, William D. and Moss, David S. and Shepherd, Adrian J. (2011) Analysis of antigenically important residues in human influenza A virus in terms of B-cell epitopes. Journal of Virology 85 (17), pp. 8548-8555. ISSN 0022-538X. Item not available from this repository.

    Halling-Brown, Mark D. and Pappalardo, F. and Rapin, N. and Zhang, P. and Alemani, D. and Emerson, A. and Castiglione, F. and Duroux, P. and Pennisi, M. and Miotto, O. and Churchill, D. and Rossi, E. and Moss, David S. and Sansom, Clare E. and Bernaschi, M. and Lefranc, M.P. and Brunak, S. and Lund, O. and Motta, S. and Lollini, P.L. and Murgo, A. and Palladini, A. and Basford, K.E. and Brusic, V. and Shepherd, Adrian J. (2010) ImmunoGrid: towards agent-based simulations of the human immune system at a natural scale. Philosophical Transactions of the Royal Society A 368 (1920), pp. 1799-1815. ISSN 0080-4614.

The Prize is perhaps the most prestigious available in the field of crystallography, given to Sir Tom Blundell in recognition of his worldwide leadership in crystallographic innovation.

Student and postdoctoral delegates are challenged to consider scientific research in the broader context of industry and society.