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Difference between revisions of "User:Joel Weadge"
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Revision as of 09:06, 19 July 2019
Joel Weadge is an Associate Professor in the Biology Department at Wilfrid Laurier University Dr. Weadge graduated with his B.Sc. from the University of Guelph and then went on to do his Ph.D. in Molecular and Cell Biology at the same institution under Dr. Anthony Clarke while studying peptidoglycan acetylesterases. Dr. Weadge then undertook a research fellowship appointment with Dr. Monica Palcic in the enzymology research group at Carlsberg Laboratory in Copenhagen, Denmark, where he worked on structure-function relationships of glycosyltransferases, including those responsible for blood group determination. He then joined Dr. Lynne Howell’s lab as a postdoctoral fellow at the Hospital for Sick Children in Toronto with CIHR and NSERC fellowships. While at Sick Kids, he continued to work on glycosyltransferases, carbohydrate esterase and acetyltransferases inherent in the alginate biosynthetic complex. Dr. Weadge’s diverse research experiences in the structure-function characterization of glycolic-enzymes and protein export apparati from a variety of carbohydrate systems (peptidoglycan, alginate, blood group antigens) form the basis for his group’s current research interests on cellulose, an exopolysaccharide found in bacterial biofilms.
- Weadge JT, Pfeffer JM, and Clarke AJ. (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. DOI:10.1186/1471-2180-5-49 |
- Weadge JT and Clarke AJ. (2006) Identification and characterization of O-acetylpeptidoglycan esterase: a novel enzyme discovered in Neisseria gonorrhoeae. Biochemistry. 45, 839-51. DOI:10.1021/bi051679s |
- Pfeffer JM, Strating H, Weadge JT, and Clarke AJ. (2006) Peptidoglycan O acetylation and autolysin profile of Enterococcus faecalis in the viable but nonculturable state. J Bacteriol. 188, 902-8. DOI:10.1128/JB.188.3.902-908.2006 |
- Weadge JT and Clarke AJ. (2007) Neisseria gonorrheae O-acetylpeptidoglycan esterase, a serine esterase with a Ser-His-Asp catalytic triad. Biochemistry. 46, 4932-41. DOI:10.1021/bi700254m |
- Li Y, Thapa P, Hawke D, Kondo Y, Furukawa K, Furukawa K, Hsu FF, Adlercreutz D, Weadge J, Palcic MM, Wang PG, Levery SB, and Zhou D. (2009) Immunologic glycosphingolipidomics and NKT cell development in mouse thymus. J Proteome Res. 8, 2740-51. DOI:10.1021/pr801040h |
- Adlercreutz D, Weadge JT, Petersen BO, Duus JØ, Dovichi NJ, and Palcic MM. (2010) Enzymatic synthesis of Gb3 and iGb3 ceramides. Carbohydr Res. 345, 1384-8. DOI:10.1016/j.carres.2010.02.006 |
- Weadge JT, Yip PP, Robinson H, Arnett K, Tipton PA, and Howell PL. (2010) Expression, purification, crystallization and preliminary X-ray analysis of Pseudomonas aeruginosa AlgX. Acta Crystallogr Sect F Struct Biol Cryst Commun. 66, 588-91. DOI:10.1107/S1744309110011851 |
- Schuman B, Persson M, Landry RC, Polakowski R, Weadge JT, Seto NO, Borisova SN, Palcic MM, and Evans SV. (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, 399-411. DOI:10.1016/j.jmb.2010.07.036 |
- Franklin MJ, Nivens DE, Weadge JT, and Howell PL. (2011) Biosynthesis of the Pseudomonas aeruginosa Extracellular Polysaccharides, Alginate, Pel, and Psl. Front Microbiol. 2, 167. DOI:10.3389/fmicb.2011.00167 |
- Pfeffer JM, Weadge JT, and Clarke AJ. (2013) Mechanism of action of Neisseria gonorrhoeae O-acetylpeptidoglycan esterase, an SGNH serine esterase. J Biol Chem. 288, 2605-13. DOI:10.1074/jbc.M112.436352 |
- Riley LM, Weadge JT, Baker P, Robinson H, Codée JD, Tipton PA, Ohman DE, and Howell PL. (2013) Structural and functional characterization of Pseudomonas aeruginosa AlgX: role of AlgX in alginate acetylation. J Biol Chem. 288, 22299-314. DOI:10.1074/jbc.M113.484931 |
- Bay ML, Cuesta-Seijo JA, Weadge JT, Persson M, and Palcic MM. (2014) Flexibility and mutagenic resiliency of glycosyltransferases. Glycoconj J. 31, 469-73. DOI:10.1007/s10719-014-9542-x |