D-Glucosylated derivatives of isofagomine and noeuromycin and their potential as inhibitors of β-glycoside hydrolases. Meloncelli, P. J., Gloster, T. M., Money, V. A., Tarling, C. A., Davies, G. J., Withers, S. G. and Stick, R. V. Aust J Chem, 2007, 60, 549-565.
Characterisation and 3-D structures of two distinct bacterial xyloglucanases from families GH5 and GH12. Gloster, T. M., Ibatullin, F. M., Macauley, K., Eklof, J. M., Roberts, S., Turkenburg, J. P., Bjornvad, M. E., Jorgensen, P. L., Danielsen, S., Johansen, K. S., Borchert, T. V., Wilson, K. S., Brumer, H. and Davies, G. J. J Biol Chem, 2007, 282, 19177-19189.
Molecular basis for trehalase inhibition revealed by the structure of trehalase in complex with potent inhibitors. Gibson, R. P., Gloster, T. M., Roberts, S., Warren, R. A. J., Chiara, J. L. and Davies, G. J. Angew Chem, 2007, 46, 4115-4119.
Glycosidase inhibition: an assessment of the binding of eighteen putative transition-state mimics. Gloster, T. M., Meloncelli, P., Stick, R. V., Zechel, D. L., Vasella, A. and Davies, G. J. J Am Chem Soc, 2007, 129, 2345-2354.
Structural basis for cyclophellitol inhibition of a β-glucosidase. Gloster, T. M., Madsen, R. and Davies, G. J. Org Biomol Chem, 2007, 5, 444-446.
Structure of a carbohydrate esterase from Bacillus anthracis. Oberbarnscheidt, L., Taylor, E. J., Davies, G. J. and Gloster, T. M. Proteins: Struct Funct Bioinf, 2007, 66, 250-252.
Structural, kinetic and thermodynamic analysis of glucoimidazole-derived glycosidase inhibitors. Gloster, T. M., Roberts, S., Perugino, G., Rossi, M., Moracci, M., Panday, N., Terinek, M., Vasella, A. and Davies, G. J. Biochemistry, 2006, 45, 11879-11884.
Dissection of conformationally restricted inhibitors binding to a β-glucosidase. Gloster, T. M., Madsen, R. and Davies, G. J. ChemBiochem, 2006, 7, 738-742.
Structure and activity of two metal ion-dependent acetylxylan esterases involved in plant cell wall degradation reveals a close similarity to peptidoglycan deacetylases. Taylor, E. J., Gloster, T. M., Turkenburg, J. P., Vincent, F., Brzozowski, A. M., Dupont, C., Shareck, F., Centeno, M. S., Prates, J. A., Puchart, V., Ferreira, L. M., Fontes, C. M., Biely, P. and Davies, G. J. J Biol Chem, 2006, 281, 10968-10975.
Recent structural insights into the expanding world of carbohydrate-active enzymes. Davies, G. J., Gloster, T. M. and Henrisatt, B. Curr Op Struct Biol, 2005, 15, 637-645.
Insights into the structural determinants of cohesin-dockerin specificity revealed by the crystal structure of the type II cohesin from Clostridium thermocellum SdbA. Carvalho, A. L., Pires, V. M., Gloster, T. M., Turkenburg, J. P., Prates, J. A., Ferreira, L. M., Romao, M. J., Davies, G. J., Fontes, C. M. and Gilbert, H. J. J Mol Biol, 2005, 349, 909-915.
Common inhibition of both β-glucosidases and β-mannosidases by isofagomine lactam reflects different conformational itineraries for pyranoside hydrolysis. Vincent, F., Gloster, T. M., Macdonald, J., Morland, C., Stick, R. V., Dias, F. M. V., Prates, J. A. M., Fontes, C. M. G. A., Gilbert, H. J. and Davies, G. J. ChemBiochem, 2004, 5, 1596-1599.
Structural, thermodynamic and kinetic analyses of tetrahydrooxazine-derived inhibitors bound to β-glucosidases. Gloster, T. M., Macdonald, J. M., Tarling, C. A., Stick, R. V., Withers, S. G. and Davies, G. J. J Biol Chem, 2004, 279, 49236-49242.
Atomic resolution analyses of the binding of xylobiose-derived deoxynojirimycin and isofagomine to xylanase Xyn10A. Gloster, T. M., Williams, S. J., Roberts, S., Tarling, C. A., Wicki, J., Withers, S. G. and Davies, G. J. Chem Commun, 2004, 1794-1795.
Structural studies of the β-glycosidase from Sulfolobus solfataricus in complex with covalently and noncovalently bound inhibitors. Gloster, T. M., Roberts, S., Ducros, V. M.-A., Perugino, G., Rossi, M., Hoos, R., Moracci, M., Vasella, A. and Davies, G. J. Biochemistry, 2004, 43, 6101-6109.
Structural and biochemical analysis of Cellvibrio japonicus xylanase 10C: how variation in substrate-binding cleft influences the catalytic profile of family GH-10 xylanases. Pell, G., Szabo, L., Charnock, S. J., Xie, H., Gloster, T. M., Davies, G. J. and Gilbert, H. J. J Biol Chem, 2004, 279, 11777-11788.
The mechanisms by which family 10 glycoside hydrolases bind decorated substrates. Pell, G., Taylor, E. J., Gloster, T. M., Turkenburg, J. P., Fontes, C. M. G. A., Ferreira, L. M. A., Nagy, T., Clark, S. J., Davies, G. J. and Gilbert, H. J. J Biol Chem, 2004, 279, 9597-9605.
Iminosugar glycosidase inhibitors: structural and thermodynamic dissection of the binding of isofagomine and 1-deoxynojirimycin to β-glucosidases. Zechel, D. L., Boraston, A. B., Gloster, T., Boraston, C. M., Macdonald, J. M., Tilbrook, D. M. G., Stick, R. V. and Davies, G. J. J Am Chem Soc, 2003, 125, 14313-14323.
A xylobiose-derived isofagomine lactam glycosidase inhibitor binds as its amide tautomer. Gloster, T., Williams, S. J., Tarling, C. A., Roberts, S., Dupont, C., Jodoin, P., Shareck, F., Withers, S. G. and Davies, G. J. Chem Commun, 2003, 944-945.
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