Ontology highlight
ABSTRACT:
SUBMITTER: Kluss JH
PROVIDER: S-EPMC5908918 | biostudies-literature | 2018
REPOSITORIES: biostudies-literature
Kluss Jillian H JH Conti Melissa M MM Kaganovich Alice A Beilina Aleksandra A Melrose Heather L HL Cookson Mark R MR Mamais Adamantios A
NPJ Parkinson's disease 20180419
Parkinson's disease-linked mutations in <i>LRRK2</i> enhance the kinase activity of the protein, therefore targeting LRRK2 kinase activity is a promising therapeutic approach. Phosphorylation at S935 of LRRK2 and of its Rab GTPase substrates have proven very useful biomarkers to monitor its kinase activity. Complementary to these approaches autophosphorylation of LRRK2 can be used as a direct kinase activity readout but to date detection of autophosphorylation at endogenous levels in vivo has be ...[more]