Research Topics
Genomes and Genes
| R Jeremy NicholsSummaryAffiliation: University of Dundee Country: UK Publications
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Detail Information
Publications
Substrate specificity and inhibitors of LRRK2, a protein kinase mutated in Parkinson's diseaseR Jeremy Nichols
MRC Protein Phosphorylation Unit, College of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, UK
Biochem J 424:47-60. 2009..The findings of the present study will aid with the investigation of LRRK2...
Functional characterization of the vaccinia virus I5 proteinBethany Unger
Department of Microbiology and Molecular Genetics, Medical College of Wisconsin, Milwaukee, WI 53226, USA
Virol J 5:148. 2008..Neither plaque size nor the viral yield produced in BSC40 cells or primary human fibroblasts are affected by the absence of I5 expression...
Inhibition of LRRK2 kinase activity leads to dephosphorylation of Ser(910)/Ser(935), disruption of 14-3-3 binding and altered cytoplasmic localizationNicolas Dzamko
University of Dundee, Scotland, UK
Biochem J 430:405-13. 2010..They will also stimulate further research to understand how phosphorylation of Ser910 and Ser935 is controlled by LRRK2, and establish any relationship to development of Parkinson's disease...
14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localizationR Jeremy Nichols
University of Dundee, Scotland, UK
Biochem J 430:393-404. 2010..These results provide the first evidence suggesting that 14-3-3 regulates LRRK2 and that disruption of the interaction of LRRK2 with 14-3-3 may be linked to Parkinson's disease...
LRRK2 phosphorylates moesin at threonine-558: characterization of how Parkinson's disease mutants affect kinase activityMahaboobi Jaleel
MRC Protein Phosphorylation Unit, MSI WTB complex, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, UK
Biochem J 405:307-17. 2007..The results of the present study suggest that moesin, ezrin and radixin may be LRRK2 substrates, findings that have been exploited to develop the first robust quantitative assay to measure LRRK2 kinase activity...
