Matthew S. Kimber, Ph.D.

Affiliations: 
2001 University of Toronto, Toronto, ON, Canada 
Area:
Genetics
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"Matthew Kimber"
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Emil F. Pai grad student 2001 University of Guelph (Canada)
 (Structural studies of the chloroplastic beta-carbonic anhydrase from the common garden pea Pisum sativum.)
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Publications

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Abraham N, Schroeter KL, Zhu Y, et al. (2022) Structure-function characterization of an aldo-keto reductase involved in detoxification of the mycotoxin, deoxynivalenol. Scientific Reports. 12: 14737
Kelly SD, Williams DM, Nothof JT, et al. (2022) The biosynthetic origin of ribofuranose in bacterial polysaccharides. Nature Chemical Biology. 18: 530-537
Boddington K, Soubeyrand E, Van Gelder K, et al. (2021) Bibenzyl synthesis in Cannabis sativa L. The Plant Journal : For Cell and Molecular Biology
Wang W, Zhu Y, Abraham N, et al. (2021) The Ribosome-Binding Mode of Trichothecene Mycotoxins Rationalizes Their Structure-Activity Relationships. International Journal of Molecular Sciences. 22
Stirling AJ, Gilbert SE, Conner M, et al. (2020) A Key Glycine in Bacterial Steroid-Degrading Acyl-CoA Dehydrogenases Allows Flavin-Ring Repositioning and Modulates Substrate Side Chain Specificity. Biochemistry. 59: 4081-4092
Clarke BR, Ovchinnikova OG, Sweeney RP, et al. (2020) A bifunctional O-antigen polymerase structure reveals a new glycosyltransferase family. Nature Chemical Biology
Kimber MS, Forrester TJ, Mallette E, et al. (2020) The Structurally Unusual Retaining β‐Kdo Glycosyltransferase WbbB Uses a Double‐Displacement Mechanism with an Intermediate Adduct Rearrangement Step The Faseb Journal. 34: 1-1
Wang W, Archbold T, Lam JS, et al. (2019) A processive endoglucanase with multi-substrate specificity is characterized from porcine gut microbiota. Scientific Reports. 9: 13630
Mann E, Kimber MS, Whitfield C. (2019) Bioinformatics analysis of diversity in bacterial glycan chain-termination chemistry and organization of carbohydrate binding modules linked to ABC transporters. Glycobiology
Aggett R, Mallette E, Gilbert SE, et al. (2019) The steroid side chain-cleaving aldolase Ltp2-ChsH2 is a thiolase superfamily member with a radically repurposed active site. The Journal of Biological Chemistry
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