Found 8 results
Filters: Author is Schormann, Norbert  [Clear All Filters]
Journal Article
Schormann, N., Banerjee, S., Ricciardi, R., and Chattopadhyay, D. (2015) Binding of undamaged double stranded DNA to vaccinia virus uracil-DNA Glycosylase. BMC Struct Biol. 15, 10
Schormann, N., Campos, J., Motamed, R., Hayden, K. L., Gould, J. R., Green, T. J., Senkovich, O., Banerjee, S., Ulett, G. C., and Chattopadhyay, D. (2020) Chlamydia trachomatis Glyceraldehyde 3-phosphate dehydrogenase: Enzyme Kinetics, High Resolution Crystal Structure and Plasminogen Binding. Protein Sci. 10.1002/pro.3975
Schormann, N., Ayres, C. A., Fry, A., Green, T. J., Banerjee, S., Ulett, G. C., and Chattopadhyay, D. (2016) Crystal Structures of Group B Streptococcus Glyceraldehyde-3-Phosphate Dehydrogenase: Apo-Form, Binary and Ternary Complexes. PLoS One. 11, e0165917
Sartmatova, D., Nash, T., Schormann, N., Nuth, M., Ricciardi, R., Banerjee, S., and Chattopadhyay, D. (2013) Crystallization and preliminary X-ray diffraction analysis of three recombinant mutants of Vaccinia virus uracil DNA glycosylase. Acta Crystallogr Sect F Struct Biol Cryst Commun. 69, 295-301
Mieher, J. L., Larson, M. R., Schormann, N., Purushotham, S., Wu, R., Rajashankar, K. R., Wu, H., and Deivanayagam, C. (2018) Glucan Binding Protein C of Mediates both Sucrose-Independent and Sucrose-Dependent Adherence. Infect Immun. 10.1128/IAI.00146-18
Schormann, N., Hayden, K. L., Lee, P., Banerjee, S., and Chattopadhyay, D. (2019) An overview of structure, function, and regulation of pyruvate kinases. Protein Sci. 10.1002/pro.3691
Schormann, N., Zhukovskaya, N., Bedwell, G., Nuth, M., Gillilan, R., Prevelige, P. E., Ricciardi, R. P., Banerjee, S., and Chattopadhyay, D. (2016) Poxvirus uracil-DNA glycosylase-An unusual member of the family I uracil-DNA glycosylases. Protein Sci. 25, 2113-2131
Ayres, C. A., Schormann, N., Senkovich, O., Fry, A., Banerjee, S., Ulett, G. C., and Chattopadhyay, D. (2014) Structure of Streptococcus agalactiae glyceraldehyde-3-phosphate dehydrogenase holoenzyme reveals a novel surface. Acta Crystallogr F Struct Biol Commun. 70, 1333-9