Publications

Found 10 results
Filters: Author is Walker, Suzanne  [Clear All Filters]
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Schaefer, K., Owens, T. W., Kahne, D., and Walker, S. (2018) Substrate Preferences Establish the Order of Cell Wall Assembly in Staphylococcus aureus. J Am Chem Soc. 140, 2442-2445
Martin, S. E. S., Tan, Z. - W., Itkonen, H. M., Duveau, D. Y., Paulo, J. A., Janetzko, J., Boutz, P. L., Törk, L., Moss, F. A., Thomas, C. J., Gygi, S. P., Lazarus, M. B., and Walker, S. (2018) Structure-Based Evolution of Low Nanomolar O-GlcNAc Transferase Inhibitors. J Am Chem Soc. 10.1021/jacs.8b07328
Lazarus, M. B., Nam, Y., Jiang, J., Sliz, P., and Walker, S. (2011) Structure of human O-GlcNAc transferase and its complex with a peptide substrate. Nature. 469, 564-7
Schaefer, K., Owens, T. W., Page, J. E., Santiago, M., Kahne, D., and Walker, S. (2020) Structure and reconstitution of a hydrolase complex that may release peptidoglycan from the membrane after polymerization. Nat Microbiol. 10.1038/s41564-020-00808-5
Joiner, C. M., Li, H., Jiang, J., and Walker, S. (2019) Structural characterization of the O-GlcNAc cycling enzymes: insights into substrate recognition and catalytic mechanisms. Curr Opin Struct Biol. 56, 97-106
Yuan, Y., Fuse, S., Ostash, B., Sliz, P., Kahne, D., and Walker, S. (2008) Structural analysis of the contacts anchoring moenomycin to peptidoglycan glycosyltransferases and implications for antibiotic design. ACS Chem Biol. 3, 429-36
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Fuse, S., Tsukamoto, H., Yuan, Y., Wang, T. - S. Andrew, Zhang, Y., Bolla, M., Walker, S., Sliz, P., and Kahne, D. (2010) Functional and structural analysis of a key region of the cell wall inhibitor moenomycin. ACS Chem Biol. 5, 701-11
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Sherman, D. J., Lazarus, M. B., Murphy, L., Liu, C., Walker, S., Ruiz, N., and Kahne, D. (2014) Decoupling catalytic activity from biological function of the ATPase that powers lipopolysaccharide transport. Proc Natl Acad Sci U S A. 111, 4982-7
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Yuan, Y., Barrett, D., Zhang, Y., Kahne, D., Sliz, P., and Walker, S. (2007) Crystal structure of a peptidoglycan glycosyltransferase suggests a model for processive glycan chain synthesis. Proc Natl Acad Sci U S A. 104, 5348-53
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Joiner, C. M., Levine, Z. G., Aonbangkhen, C., Woo, C. M., and Walker, S. (2019) Aspartate Residues Far from the Active Site Drive O-GlcNAc Transferase Substrate Selection. J Am Chem Soc. 141, 12974-12978