R Jeremy Nichols

Summary

Affiliation: University of Dundee
Country: UK

Publications

  1. pmc Substrate specificity and inhibitors of LRRK2, a protein kinase mutated in Parkinson's disease
    R 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
  2. pmc Functional characterization of the vaccinia virus I5 protein
    Bethany Unger
    Department of Microbiology and Molecular Genetics, Medical College of Wisconsin, Milwaukee, WI 53226, USA
    Virol J 5:148. 2008
  3. pmc Inhibition of LRRK2 kinase activity leads to dephosphorylation of Ser(910)/Ser(935), disruption of 14-3-3 binding and altered cytoplasmic localization
    Nicolas Dzamko
    University of Dundee, Scotland, UK
    Biochem J 430:405-13. 2010
  4. pmc 14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization
    R Jeremy Nichols
    University of Dundee, Scotland, UK
    Biochem J 430:393-404. 2010
  5. pmc LRRK2 phosphorylates moesin at threonine-558: characterization of how Parkinson's disease mutants affect kinase activity
    Mahaboobi Jaleel
    MRC Protein Phosphorylation Unit, MSI WTB complex, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, UK
    Biochem J 405:307-17. 2007

Collaborators

Detail Information

Publications5

  1. pmc Substrate specificity and inhibitors of LRRK2, a protein kinase mutated in Parkinson's disease
    R 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...
  2. pmc Functional characterization of the vaccinia virus I5 protein
    Bethany 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...
  3. pmc Inhibition of LRRK2 kinase activity leads to dephosphorylation of Ser(910)/Ser(935), disruption of 14-3-3 binding and altered cytoplasmic localization
    Nicolas 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...
  4. pmc 14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization
    R 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...
  5. pmc LRRK2 phosphorylates moesin at threonine-558: characterization of how Parkinson's disease mutants affect kinase activity
    Mahaboobi 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...