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Wilfrid Laurier University Faculty of Science
October 10, 2015
Canadian Excellence

Joel Weadge


email: Joel Weadge
phone: 519-884-0710
ext: 2161





Baker, P., Ricer, T., Moynihan, P.J., Walvoort, M.T., Little, D.J., Whitney, J.C., Dawson, K., Weadge, J.T., Robinson, H., Ohman, D.E., Codée, J.D., Klassen, J.S., Clarke, A.J., and Howell, P.L. (2014) P. aeruginosa SGNH hydrolase-like proteins AlgJ and AlgX have similar topologies but separate and distinct roles in alginate acetylation. PLoS Pathog[Epub ahead of print]. 

Bay, M.L., Cuesta-Seijo, J.A., Weadge, J.T., Persson, M., Palcic, M.M. (2014) Flexibility and mutagenic resiliency of glycosyltransferases. Glycoconj. J. [Epub ahead of print]. 

Riley, L.M., Weadge, J.T., Baker, P., Robinson, H., Codée, J., Tipton, P.A., Ohman, D.E., and Howell, P.L. (2013) Structural and functional characterization of Pseudomonas aeruginosa AlgX: role of AlgX in alginate acetylation. J. Biol. Chem. [Epub ahead of print].

Pfeffer, J.M., Weadge, J.T., and Clarke, A.J. (2013) Mechanism of action of Neisseria gonorrhoea O-acetylpeptidoglycan esterase, an SGNH serine esterase. J. Biol. Chem. 288(4):2605-2613. (doi: 10.1074/jbc.M112.436352)

Franklin, M.J., Nivens, D.E., Weadge, J.T., and Howell, P.L. (2011) Biosynthesis of the Pseudomonas aeruginosa extracellular polysaccharides, Alginate, Pel, and Psl. Front. Microbiol. 2(167):1-16.

Schuman, B., Persson, M., Landry, R.C., Polakowski, R., Weadge, J.T., Seto, N.O.L., Borisova, S.N., Palcic, M.M., and Evans, S.V. (2010) Cysteine to serine mutants dramatically reorder the active site of human ABO(H) blood group B glycosyltransferase without affecting activity: structural insights into cooperative substrate binding. J. Mol. Biol. 402(2):399-411.

Weadge, J.T., Yip, P., Robinson, H., Arnett, K., Tipton, P.A., and Howell, P.L. (2010) Expression, purification, crystallization and preliminary X-ray analysis of Pseudomonas aeruginosa AlgX. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66(5):588-591.

Adlercreutz, D., Weadge, J.T., Peterson, B.O., Duus, J.Ø., Dovichi, N.J. and Palcic, M.M. (2010) Enzymatic synthesis of Gb3 and iGb3 ceramides. Carbohydrate Res. 345(10):1384-1388.

Li, Y., Thapa, P., Hawke, D., Kondo, Y., Furukawa, K., Furukawa, K., Hsu, F., Adlercreutz, D., Weadge, J., Palcic, M.M., Wang, P.G., Levery, S.B., and Zhou, D. (2009) Immunologic glycosphingolipidomics and NKT cell development in mouse thymus. J. Proteome Res. 8(6):2740-2751.

Weadge, J.T., and Palcic, M.M. Glycosyltransferases, Chemistry of, Volume 2, pp 198-210. In Wiley Encyclopedia of Chemical Biology. Ed: Tadhg P. Begley. John Wiley and Sons, Hoboken. 2008.

Weadge, J.T., and Clarke, A.J. (2008) Transacetylations of carbohydrates in organic solvent catalyzed by O-acetylpeptidoglycan esterase from Neisseria gonorrhoeae. Biocatal. Biotransformation. 26(1-2):68-75.

Weadge, J.T., and Clarke, A.J. (2007) Neisseria gonorrhoeae O-acetylpeptidoglycan esterase, a serine esterase with a Ser-His-Asp catalytic triad. Biochemistry. 46(16):4932-4941.

Legaree, B.A., Daniels, K., Weadge, J.T., Cockburn, D., and Clarke, A.J. (2007) Function of penicillin-binding protein 2 in viability and morphology of Pseudomonas aeruginosa. J. Antimicrob. Chemother. 59(3):411-424.

Pfeffer, J.M., Strating, H., Weadge, J.T., and Clarke, A.J. (2006) Peptidoglycan O-acetylation and autolysin profile of Enterococcus faecalis in the viable but non-culturable State. J. Bacteriol. 188(3):902-908.

Weadge, J.T., and Clarke, A.J. (2006) Identification and characterization of an O-acetylpeptidoglycan esterase: a novel enzyme discovered in Neisseria gonorrhoeae. Biochemistry. 45(3):839-851.

Weadge, J.T., and Clarke, A.J. (2005) Identification of a new family of enzymes with potential O-acetylpeptidoglycan esterase activity in both Gram positive and Gram negative bacteria. BMC Microbiol. 5:49.

Payie, K.G., Weadge, J.T., Tanaka, T. and Yada, R.Y. (2000) Purification, N-terminal sequencing and partial characterization of a novel aspartic proteinase from the leaves of Medicago sativa L. (alfalfa). Biotechnol. Lett. 22, 1515-1520.