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Human Molecular Genetics|October 22, 2005
Induction of inclusion formation and disruption of lamin A/C structure by premutation CGG-repeat RNA in human cultured neural cellsDolores Garcia Arocena, Christine K Iwahashi, Nelly Won, et al.Nature Communications|August 5, 2025
14-3-3 binding maintains the Parkinson's associated kinase LRRK2 in an inactive stateJuliana A Martinez Fiesco, Alexandra Beilina, Astrid Alvarez de la Cruz, et al.Biorxiv : the Preprint Server for Biology|November 28, 2024
14-3-3 binding maintains the Parkinson's associated kinase LRRK2 in an inactive stateJuliana A Martinez Fiesco, Ning Li, Astrid Alvarez de la Cruz, et al.The Journal of Cell Biology|September 24, 2025
JIP4 and RILPL1 utilize opposing motor force to dynamically regulate lysosomal tubulationLuis Bonet-Ponce, Tsion Tegicho, Nuria Fernandez-Martinez, et al.Nature Communications|December 16, 2014
Phosphorylation of LRRK2 by casein kinase 1α regulates trans-Golgi clustering via differential interaction with ARHGEF7Ruth Chia, Sara Haddock, Alexandra Beilina, et al.Journal of Neurochemistry|March 31, 2007
Mutations in LRRK2/dardarin associated with Parkinson disease are more toxic than equivalent mutations in the homologous kinase LRRK1Elisa Greggio, Patrick A Lewis, Marcel P van der Brug, et al.Neurobiology of Disease|May 21, 2020
Sequential screening nominates the Parkinson's disease associated kinase LRRK2 as a regulator of Clathrin-mediated endocytosisGeorge R Heaton, Natalie Landeck, Adamantios Mamais, et al.Human Molecular Genetics|October 14, 2010
DJ-1 acts in parallel to the PINK1/parkin pathway to control mitochondrial function and autophagyKelly Jean Thomas, Melissa K McCoy, Jeff Blackinton, et al.Biochemical and Biophysical Research Communications|September 8, 2009
The Parkinson's disease kinase LRRK2 autophosphorylates its GTPase domain at multiple sitesElisa Greggio, Jean-Marc Taymans, Eugene Yuejun Zhen, et al.The Journal of Biological Chemistry|April 10, 2008
The Parkinson disease-associated leucine-rich repeat kinase 2 (LRRK2) is a dimer that undergoes intramolecular autophosphorylationElisa Greggio, Ibardo Zambrano, Alice Kaganovich, et al.Pageof 6