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Items by Bagby, Stefan

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Number of items: 45.

Book Sections

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

Articles

Posner, M. G., Upadhyay, A., Crennell, S., Watson, A. J. A., Dorus, S., Danson, M. J. and Bagby, S., 2013. Post-translational modification in the archaea: structural characterization of multi-enzyme complex lipoylation. Biochemical Journal, 449 (2), pp. 415-425.

Cherrett, C., Furutani-Seiki, M. and Bagby, S., 2012. The Hippo pathwaya : Key interaction and catalytic domains in organ growth control, stem cell self-renewal and tissue regeneration. Essays in Biochemistry, 53 (1), pp. 111-127.

Webb, C., Upadhyay, A., Giuntini, F., Eggleston, I., Furutani-Seiki, M., Ishima, R. and Bagby, S., 2011. Structural features and ligand binding properties of tandem WW domains from YAP and TAZ, nuclear effectors of the Hippo pathway. Biochemistry, 50 (16), pp. 3300-3309.

Clark, E. A., Crennell, S., Upadhyay, A., Zozulya, A. V., Mackay, J. D., Svergun, D. I., Bagby, S. and van den Elsen, J. M. H., 2011. A structural basis for Staphylococcal complement subversion : X-ray structure of the complement-binding domain of Staphylococcus aureus protein Sbi in complex with ligand C3d. Molecular Immunology, 48 (4), pp. 452-462.

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.

Isenman, D. E., Leung, E., Mackay, J. D., Bagby, S. and van den Elsen, J. M. H., 2010. Mutational analyses reveal that the staphylococcal immune evasion molecule Sbi and complement receptor 2 (CR2) share overlapping contact residues on C3d: implications for the controversy regarding the CR2/C3d cocrystal structure. The Journal of Immunology, 184 (4), pp. 1946-1955.

Posner, M. G., Upadhyay, A., Bagby, S., Hough, D. W. and Danson, M. J., 2009. A unique lipoylation system in the Archaea: lipoylation in Thermoplasma acidophilum requires two proteins. FEBS Journal, 276 (15), pp. 4012-4022.

Clark, E., Upadhyay, A., Bagby, S. and van den Elsen, J., 2009. IsaB, a new immunoglobulin-binding protein from Staphylococcus aureus. Molecular Immunology, 46 (14), pp. 2834-2835.

Isenman, D. E., Leung, E., Mackay, J. D., Bagby, S. and van den Elsen, J. M. H., 2008. Mutational analyses reveal that the staphylococcal immune evasion molecule Sbi and complement eeceptor 2 (CR2) share overlapping contact residues on C3d: Implications for the controversy regarding the CR2/C3d cocrystal structure. Molecular Immunology, 45 (16), pp. 4095-4096.

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.

Upadhyay, A., Wu, H.-L., Williams, C., Field, T., Galyov, E. E., van den Elsen, J. M. H. and Bagby, S., 2008. The guanine-nucleotide-exchange factor BopE from Burkholderia pseudomallei adopts a compact version of the Salmonella SopE/SopE2 fold and undergoes a closed-to-open conformational change upon interaction with Cdc42. Biochemical Journal, 411 (3), pp. 485-493.

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.

van den Elsen, J., Upadhyay, A., Burman, J., Leung, E., Clark, E., Isenman, D. and Bagby, S., 2008. Structure–function analysis of the novel Staphylococcus aureus immune subversion protein Sbi. Molecular Immunology, 45 (16), p. 4119.

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.

Wu, H.-L., Williams, C., Upadhyay, A., Galyov, E. E. and Bagby, S., 2004. Assignment of the 1H, 13C and 15N resonances of the catalytic domain of guanine nucleotide exchange factor BopE from Burkholderia pseudomallei. Journal of Biomolecular NMR, 29 (2), pp. 215-216.

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.

Williams, C., Galyov, E. E. and Bagby, S., 2004. Solution structure, backbone dynamics, and interaction with Cdc42 of Salmonella guanine nucleotide exchange factor SopE2. Biochemistry, 43 (38), pp. 11998-12008.

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.

Williams, C., Galyov, E. E. and Bagby, S., 2003. Assignment of the 1H, 13C and 15N resonances of the catalytic domain of guanine nucleotide exchange factor SopE2 from Salmonella dublin. Journal of Biomolecular NMR, 26 (4), pp. 379-380.

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., Kay, L. E., Eagle, S. G., Inouye, S. and Ikura, M., 1994. Unusual helix-containing greek keys in development-specific Ca2+-binding protein S. 1H, 15N, and 13C assignments and secondary structure determined with the use of multidimensional double and triple resonance heteronuclear NMR spectroscopy. Biochemistry, 33 (9), pp. 2409-2421.

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

Alshammari, A., Posner, M., Jones, G., Upadhyay, A., Bagby, S., Ilie, A. and Estrela, P., 2011. Graphene-based amperometric and field-effect biosensing with supramolecular protein complexes. In: Electrochem 2011, 2011-09-05 - 2011-09-06, Bath.

This list was generated on Mon Sep 22 21:20:31 2014 IST.