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Wilfrid Laurier University Leaf
November 24, 2014
 
 
Canadian Excellence

Joel Weadge




Contact:

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

 

Publications



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PUBLICATIONS:

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.