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Professor CHARLES LAUGHTON's Outputs (3)

In vitro antitumor mechanism of (E)-N-(2-methoxy-5-(((2,4,6-trimethoxystyryl)sulfonyl)methyl)pyridin-3-yl)methanesulfonamide (2014)
Journal Article
Lu, T., Laughton, C., Wang, S., & Bradshaw, T. (2015). In vitro antitumor mechanism of (E)-N-(2-methoxy-5-(((2,4,6-trimethoxystyryl)sulfonyl)methyl)pyridin-3-yl)methanesulfonamide. Molecular Pharmacology, 87(1), 18-30. https://doi.org/10.1124/mol.114.093245

ON01910.Na [sodium (E)-2-(2-methoxy-5-((2,4,6-trimethoxystyrylsulfonyl)methyl)phenylamino)acetate; Rigosertib, Estybon], a styryl benzylsulfone, is a phase III stage anticancer agent. This non-ATP competitive kinase inhibitor has multitargeted activi... Read More about In vitro antitumor mechanism of (E)-N-(2-methoxy-5-(((2,4,6-trimethoxystyryl)sulfonyl)methyl)pyridin-3-yl)methanesulfonamide.

Investigation of the flexibility of protein kinases implicated in the pathology of Alzheimer's Disease (2014)
Journal Article
Laughton, C., Mazanetz, M., & Fischer, P. (2014). Investigation of the flexibility of protein kinases implicated in the pathology of Alzheimer's Disease. Molecules, 19(7), 9134-9159. https://doi.org/10.3390/molecules19079134

The pathological characteristics of Alzheimer’s Disease (AD) have been linked to the activity of three particular kinases—Glycogen Synthase Kinase 3β (GSK3β), Cyclin-Dependent Kinase 5 (CDK5) and Extracellular-signal Regulated Kinase 2 (ERK2). As a c... Read More about Investigation of the flexibility of protein kinases implicated in the pathology of Alzheimer's Disease.

Investigating the binding preferences of small molecule inhibitors of human protein arginine methyltransferase 1 using molecular modelling (2014)
Journal Article
Hong, W., Laughton, C. A., Li, J., Yap, L. F., Paterson, I. C., & Wang, H. (2014). Investigating the binding preferences of small molecule inhibitors of human protein arginine methyltransferase 1 using molecular modelling. Journal of Molecular Graphics and Modelling, 51, 193-202. https://doi.org/10.1016/j.jmgm.2014.05.010

Protein arginine methyltransferases (PRMTs) catalyse the methylation of arginine residues of target proteins. PRMTs utilise S-adenosyl methionine (SAM) as the methyl group donor, leading to S-adenosyl homocysteine (SAH) and monomethylarginine (mMA).... Read More about Investigating the binding preferences of small molecule inhibitors of human protein arginine methyltransferase 1 using molecular modelling.