Items by Bagby, Stefan

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Number of items: 59.

Book Sections

Bagby, S. and Ishima, R., 2017. Forthcoming. Protein dynamics revealed by CPMG dispersion. In: Webb, G., ed. Modern Magnetic Resonance, 2nd edition. 9783319283876: Springer.

Bagby, S., 2013. J coupling. In: Roberts, G. C. K., ed. Encyclopedia of Biophysics. Springer.


Alshammari, A., Posner, M. G., Upadhyay, A., Marken, F., Bagby, S. and Ilie, A., 2016. A Modular Bio-Platform Based on a Versatile Supramolecular Multi-Enzyme Complex Directly Attached to Graphene. ACS Applied Materials and Interfaces, 8 (32), 21077–21088. Item availability may be restricted.

Porazinski, S., Wang, H., Asaoka, Y., Behrndt, M., Miyamoto, T., Morita, H., Hata, S., Sasaki, T., Krens, S. F. G., Osada, Y., Asaka, S., Momoi, A., Linton, S., Miesfeld, J. B., Link, B. A., Senga, T., Castillo-Morales, A., Urrutia, A. O., Shimizu, N., Nagase, H., Matsuura, S., Bagby, S., Kondoh, H., Nishina, H., Heisenberg, C. P. and Furutani-Seiki, M., 2015. YAP is essential for tissue tension to ensure vertebrate 3D body shape. Nature, 521 (7551), pp. 217-221.

Nettleship, J. E., Watson, P. J., Rahman-Huq, N., Fairall, L., Posner, M. G., Upadhyay, A., Reddivari, Y., Chamberlain, J. M. G., Kolstoe, S. E., Bagby, S., Schwabe, J. W. R. and Owens, R. J., 2014. Transient expression in HEK 293 cells:An alternative to E. coli for the production of secreted and intracellular mammalian proteins. Methods in Molecular Biology, 1258, pp. 209-222.

Jones, R. T., Sanchez-Contreras, M., Vlisidou, I., Amos, M. R., Yang, G., Munoz-Berbel, X., Upadhyay, A., Potter, U. J., Joyce, S. A., Ciche, T. A., Jenkins, A. T. A., Bagby, S., ffrench-Constant, R. H. and Waterfield, N. R., 2010. Photorhabdus adhesion modification protein (Pam) binds extracellular polysaccharide and alters bacterial attachment. BMC Microbiology, 10, 141.

Upadhyay, A., Burman, J. D., Clark, E. A., Leung, E., Isenman, D. E., van den Elsen, J. M. H. and Bagby, S., 2008. Structure-function analysis of the C3 binding region of Staphylococcus aureus immune subversion protein Sbi. Journal of Biological Chemistry, 283 (32), pp. 22113-22120.

Burman, J. D., Leung, E., Atkins, K. L., O'Seaghdha, M. N., Lango, L., Bernado, P., Bagby, S., Svergun, D. I., Foster, T. J., Isenman, D. E. and van den Elsen, J. M. H., 2008. Interaction of human complement with Sbi, a staphylococcal immunoglobulin-binding protein: indications of a novel mechanism of complement evasion by Staphylococcus aureus. Journal of Biological Chemistry, 283 (25), pp. 17579-17593.

Atkins, K. L., Burman, J. D., Chamberlain, E. S., Cooper, J. E., Poutrel, B., Bagby, S., Jenkins, T. A., Feil, E. J. and van den Elsen, J. M. H., 2008. S. aureus IgG-binding proteins SpA and Sbi: host specificity and mechanisms of immune complex formation. Molecular Immunology, 45 (6), pp. 1600-1611.

Wright, A. J., Higginbottom, A., Philippe, D., Upadhyay, A., Bagby, S., Read, R. C., Monk, P. N. and Partridge, L. J., 2007. Characterisation of receptor binding by the chemotaxis inhibitory protein of Staphylococcus aureus and the effects of the host immune response. Molecular Immunology, 44 (10), pp. 2507-2517.

Wu, H.-L., Bagby, S. and van den Elsen, J., 2005. Evolution of the genetic triplet code via two types of doublet codons. Journal of Molecular Evolution, 61 (1), pp. 54-64.

Upadhyay, A., Williams, C., Gill, A. C., Philippe, D. L., Davis, K., Taylor, L. A., Stevens, M. P., Galyov, E. E. and Bagby, S., 2004. Biophysical characterization of the catalytic domain of guanine nucleotide exchange factor BopE from Burkholderia pseudomallei. Biochimica Et Biophysica Acta-Proteins and Proteomics, 1698 (1), pp. 111-119.

Wood, M. W., Williams, C., Upadhyay, A., Gill, A. C., Philippe, D. L., Galyov, E. E., van den Elsen, J. M. H. and Bagby, S., 2004. Structural analysis of Salmonella enterica effector protein SopD. Biochimica Et Biophysica Acta-Proteins and Proteomics, 1698 (2), pp. 219-226.

Mal, T. K., Bagby, S. and Ikura, M., 2002. Protein structure calculation from NMR data. Methods in Molecular Biology, 173, pp. 267-283.

Qi, X.-F., Bagby, S., Gombos, Z., Ikura, M. and Chakrabartty, A., 2001. Alternate routes to conformational specificity in a Greek key β barrel protein. European Journal of Biochemistry, 268 (17), pp. 4653-4664.

Bagby, S., Tong, K. I. and Ikura, M., 2001. Optimization of protein solubility and stability for protein nuclear magnetic resonance. Methods in Enzymology, 339B, pp. 20-41.

Bagby, S., Mal, T. K., Liu, D., Raddatz, E., Nakatani, Y. and Ikura, M., 2000. TFIIA–TAF regulatory interplay:NMR evidence for overlapping binding sites on TBP. FEBS Letters, 468 (2-3), pp. 149-154.

Liu, D., Ishima, R., Tong, K. I., Bagby, S., Kokubo, T., Muhandiram, D. R., Kay, L. E., Nakatani, Y. and Ikura, M., 1998. Solution structure of a TBP–TAFII230 complex:protein mimicry of the minor groove surface of the TATA box unwound by TBP. Cell, 94 (5), pp. 573-583.

Hayashi, F., Ishima, R., Liu, D., Tong, K. I., Kim, S., Reinberg, D., Bagby, S. and Ikura, M., 1998. Human general transcription factor TFIIB :conformational variability and interaction with VP16 activation domain. Biochemistry, 37 (22), pp. 7941-7951.

Bagby, S., Arrowsmith, C. H. and Ikura, M., 1998. New perceptions of transcription factor properties from NMR. Biochemistry and Cell Biology - Biochimie Et Biologie Cellulaire, 76 (2-3), pp. 368-378.

Bagby, S., Go, S., Inouye, S., Ikura, M. and Chakrabartty, A., 1998. Equilibrium folding intermediates of a greek key β-barrel protein. Journal of Molecular Biology, 276 (3), pp. 669-681.

Bagby, S., Tong, K. L., Liu, D., Alattia, J.-R. and Ikura, M., 1997. The button test:a small scale method using microdialysis cells for assessing protein solubility at concentrations suitable for NMR. Journal of Biomolecular NMR, 10 (3), pp. 279-282.

Nakatani, Y., Bagby, S. and Ikura, M., 1996. The histone folds in transcription factor TFIID. Journal of Biological Chemistry, 271 (12), pp. 6575-6578.

Bagby, S., Kim, S., Maldonado, E., Tong, K. L., Reinberg, D. and Ikura, M., 1995. Solution structure of the c-terminal core domain of human TFIIB:similarity to cyclin A and interaction with TATA-binding protein. Cell, 82 (5), pp. 857-867.

Overduin, M., Harvey, T. S., Bagby, S., I. Tong, K., Yau, P., Takeichi, M. and Ikura, M., 1995. Solution structure of the epithelial cadherin domain responsible for selective cell adhesion. Science, 267 (5196).

I. Tong, K., Yau, P., Overduin, M., Bagby, S., Porumb, T., Takeichi, M. and Ikura, M., 1994. Purification and spectroscopic characterization of a recombinant amino-terminal polypeptide fragment of mouse epithelial cadherin. FEBS Letters, 352 (3), pp. 318-322.

Bagby, S., Driscoll, P. C., Harvey, T. S. and Hill, H. A. O., 1994. High-resolution solution structure of reduced parsley plastocyanin. Biochemistry, 33 (21), pp. 6611-6622.

Bagby, S., Harvey, T. S., Eagle, S. G., Inouye, S. and Ikura, M., 1994. NMR-derived three-dimensional solution structure of protein S complexed with calcium. Structure, 2 (2), pp. 107-122.

Bagby, S., Harvey, T. S., Eagle, S. G., Inouye, S. and Ikura, M., 1994. Structural similarity of a developmentally regulated bacterial spore coat protein to beta gamma-crystallins of the vertebrate eye lens. Proceedings of the National Academy of Sciences of the United States of America, 91 (10), pp. 4308-4312.

Bagby, S., Barker, P. D., Hill, H. A., Sanghera, G. S., Dunbar, B., Ashby, G. A. and Thorneley, R. N., 1991. Direct electrochemistry of two genetically distinct flavodoxins isolated from Azotobacter chroococcum grown under nitrogen-fixing conditions. Biochemical Journal, 277 (Pt 2), pp. 313-326.

McLendon, G. L., Bagby, S., Charman, J. A., Driscoll, P. C., McIntire, W. S., Mathews, F. S. and Hill, H. A. O., 1991. Subunit interactions change the heme active-site geometry in p-cresol methylhydroxylase. Proceedings of the National Academy of Sciences of the United States of America (PNAS), 88 (21), pp. 9463-9467.

Bagby, S., Barker, P. D., Guo, L. H. and Hill, H. A. O., 1990. Direct electrochemistry of protein-protein complexes involving cytochrome c, cytochrome b5, and plastocyanin. Biochemistry, 29 (13), pp. 3213-3219.

Bagby, S., Driscoll, P. C., Goodall, K. G., Redfield, C. and Hill, H. A. O., 1990. The complex formed between plastocyanin and cytochrome c. Investigation by NMR spectroscopy. European Journal of Biochemistry, 188 (2), pp. 413-420.

Bagby, S., Barker, P. D., Di Gleria, K., Hill, H. A. O. and Lowe, V. J., 1988. The direct electrochemistry of cytochrome b5 at peptide-modified gold electrodes. Biochemical Society Transactions, 16, pp. 958-959.

Conference or Workshop Items

Bagby, S., Jain, M., Olsen, H., Preston, A. and Akeson, M., 2015. Use of MinION data to assemble the 67% GC genome sequence of Bordetella pertussis. In: Genome Science, 2015-09-07 - 2015-09-09, University of Birmingham.

Pula, G., Posner, M., Upadhyay, A. and Bagby, S., 2013. Extracellular fibrinogen-binding protein (Efb) from Staphylococcus aureus inhibits fibrinogen binding, platelet aggregation and whole blood thrombus formation. In: XXIVth Congress of the International Society on Thrombosis and Haemostasis, 2013-06-20 - 2013-06-24, Amsterdam RAI.

This list was generated on Mon Feb 27 13:42:07 2017 GMT.