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Difference between revisions of "User:Tom Wennekes"
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| − | + | Tom Wennekes is currently a postdoctoral fellow in [http://www.chem.ubc.ca/personnel/faculty/withers/group/ the group] of [[User:Steve_Withers| Prof. Steve Withers]] at the University of British Columbia in Canada. Here, with support from a dutch NWO Rubicon fellowship, he is involved in the development of mechanism-based inhibitors and probes for the neuraminidase of the influenza A virus ([[GH34]]). He received his Ph.D. from Leiden University in 2008 under the supervision of [http://biosyn.lic.leidenuniv.nl/ Prof. Hermen Overkleeft] and [http://www.amc.nl/index.cfm?sid=1266&contentitemid=118&itemid=99 Prof. Hans Aerts] for his research on inhibitors of the glycosphingolipid metabolism-involved glucocerebrosidase ([[GH30]]), β-glucosidase-2 ([[GH116]]) and glycosylceramide synthase (GT21). As of November 2010 he will join [http://www.orc.wur.nl/UK/ the Laboratory of Organic Chemistry] at Wageningen University in the Netherlands as an assistant professor in Synthetic Bio-organic Chemistry and Chemical Biology. | |
| + | |||
| + | |||
| + | ---- | ||
| + | <biblio> | ||
| + | #Wennekes2010 pmid=20000679 | ||
| + | #Wennekes2009 pmid=19862781 | ||
| + | #Bussink2007 pmid=17392268 | ||
| + | #Aerts2007 pmid=17287460 | ||
| + | #Wennekes2007 pmid=17243712 | ||
| + | #Boot2007 pmid=17105727 | ||
| + | </biblio> | ||
| + | |||
| + | |||
| + | [[Category:Contributors|Wennekes,Tom]] | ||
Latest revision as of 04:01, 27 May 2011
Tom Wennekes is currently a postdoctoral fellow in the group of Prof. Steve Withers at the University of British Columbia in Canada. Here, with support from a dutch NWO Rubicon fellowship, he is involved in the development of mechanism-based inhibitors and probes for the neuraminidase of the influenza A virus (GH34). He received his Ph.D. from Leiden University in 2008 under the supervision of Prof. Hermen Overkleeft and Prof. Hans Aerts for his research on inhibitors of the glycosphingolipid metabolism-involved glucocerebrosidase (GH30), β-glucosidase-2 (GH116) and glycosylceramide synthase (GT21). As of November 2010 he will join the Laboratory of Organic Chemistry at Wageningen University in the Netherlands as an assistant professor in Synthetic Bio-organic Chemistry and Chemical Biology.
- Wennekes T, Meijer AJ, Groen AK, Boot RG, Groener JE, van Eijk M, Ottenhoff R, Bijl N, Ghauharali K, Song H, O'Shea TJ, Liu H, Yew N, Copeland D, van den Berg RJ, van der Marel GA, Overkleeft HS, and Aerts JM. (2010). Dual-action lipophilic iminosugar improves glycemic control in obese rodents by reduction of visceral glycosphingolipids and buffering of carbohydrate assimilation. J Med Chem. 2010;53(2):689-98. DOI:10.1021/jm901281m |
- Wennekes T, van den Berg RJ, Boot RG, van der Marel GA, Overkleeft HS, and Aerts JM. (2009). Glycosphingolipids--nature, function, and pharmacological modulation. Angew Chem Int Ed Engl. 2009;48(47):8848-69. DOI:10.1002/anie.200902620 |
- Bussink AP, van Swieten PF, Ghauharali K, Scheij S, van Eijk M, Wennekes T, van der Marel GA, Boot RG, Aerts JM, and Overkleeft HS. (2007). N-azidoacetylmannosamine-mediated chemical tagging of gangliosides. J Lipid Res. 2007;48(6):1417-21. DOI:10.1194/jlr.C700006-JLR200 |
- Aerts JM, Ottenhoff R, Powlson AS, Grefhorst A, van Eijk M, Dubbelhuis PF, Aten J, Kuipers F, Serlie MJ, Wennekes T, Sethi JK, O'Rahilly S, and Overkleeft HS. (2007). Pharmacological inhibition of glucosylceramide synthase enhances insulin sensitivity. Diabetes. 2007;56(5):1341-9. DOI:10.2337/db06-1619 |
- Wennekes T, van den Berg RJ, Donker W, van der Marel GA, Strijland A, Aerts JM, and Overkleeft HS. (2007). Development of adamantan-1-yl-methoxy-functionalized 1-deoxynojirimycin derivatives as selective inhibitors of glucosylceramide metabolism in man. J Org Chem. 2007;72(4):1088-97. DOI:10.1021/jo061280p |
- Boot RG, Verhoek M, Donker-Koopman W, Strijland A, van Marle J, Overkleeft HS, Wennekes T, and Aerts JM. (2007). Identification of the non-lysosomal glucosylceramidase as beta-glucosidase 2. J Biol Chem. 2007;282(2):1305-12. DOI:10.1074/jbc.M610544200 |