Results 21 to 30 of about 14,162 (200)

Inhibition of LRRK2 or Casein Kinase 1 Results in LRRK2 Protein Destabilization [PDF]

Molecular Neurobiology, 2018
Mutations and variations in the leucine-rich repeat kinase 2 (LRRK2) gene are strongly associated with an increased risk to develop Parkinson's disease (PD). Most pathogenic LRRK2 mutations display increased kinase activity, which is believed to underlie LRRK2-mediated toxicity.
De Wit, Tina, Baekelandt, Veerle, Lobbestael, Evy   +2 more
openaire   +3 more sources

ARHGEF7 (Beta-PIX) acts as guanine nucleotide exchange factor for leucine-rich repeat kinase 2. [PDF]

PLoS ONE, 2010
Mutations within the leucine-rich repeat kinase 2 (LRRK2) gene are a common cause of familial and sporadic Parkinson's disease. The multidomain protein LRRK2 exhibits overall low GTPase and kinase activity in vitro.Here, we show that the rho guanine ...
Karina Haebig, Christian Johannes Gloeckner, Marta Garcia Miralles, Frank Gillardon, Claudia Schulte, Olaf Riess, Marius Ueffing, Saskia Biskup, Michael Bonin   +8 more
doaj   +1 more source

LRRK2 Phosphorylation: Behind the Scenes [PDF]

The Neuroscientist, 2018
Mutations in the gene encoding leucine-rich repeat kinase 2 (LRRK2) are known today as the most common genetic cause of Parkinson’s disease (PD). LRRK2 is a large protein that is hypothesized to regulate other proteins as a scaffold in downstream signaling pathways.
De Wit, Tina, Baekelandt, Veerle, Lobbestael, Evy   +2 more
openaire   +2 more sources

GTPase activity plays a key role in the pathobiology of LRRK2. [PDF]

PLoS Genetics, 2010
Mutations in the leucine-rich repeat kinase 2 (LRRK2) gene are associated with late-onset, autosomal-dominant, familial Parkinson's disease (PD) and also contribute to sporadic disease.
Yulan Xiong, Candice E Coombes, Austin Kilaru, Xiaojie Li, Aaron D Gitler, William J Bowers, Valina L Dawson, Ted M Dawson, Darren J Moore   +8 more
doaj   +1 more source

Tissue specific LRRK2 interactomes reveal a distinct striatal functional unit.

PLoS Computational Biology, 2023
Mutations in LRRK2 are the most common genetic cause of Parkinson's disease. Despite substantial research efforts, the physiological and pathological role of this multidomain protein remains poorly defined. In this study, we used a systematic approach to
Yibo Zhao, Nikoleta Vavouraki, Ruth C Lovering, Valentina Escott-Price, Kirsten Harvey, Patrick A Lewis, Claudia Manzoni   +6 more
doaj   +1 more source

Understanding LRRK2 kinase activity in preclinical models and human subjects through quantitative analysis of LRRK2 and pT73 Rab10

Scientific Reports, 2021
Variants in the leucine-rich repeat kinase 2 (LRRK2) gene are associated with increased risk for familial and sporadic Parkinson’s disease (PD). Pathogenic variants in LRRK2, including the common variant G2019S, result in increased LRRK2 kinase activity,
Xiang Wang, Elvira Negrou, Michael T. Maloney, Vitaliy V. Bondar, Shan V. Andrews, Manuel Montalban, Ceyda Llapashtica, Romeo Maciuca, Hoang Nguyen, Hilda Solanoy, Annie Arguello, Laralynne Przybyla, Nathan J. Moerke, Sarah Huntwork-Rodriguez, Anastasia G. Henry   +14 more
doaj   +1 more source

Mechanisms of LRRK2-Mediated Neurodegeneration [PDF]

Current Neurology and Neuroscience Reports, 2012
Mutations in the leucine-rich repeat kinase 2 (LRRK2) gene represent the most common cause of familial Parkinson's disease (PD), whereas common variation at the LRRK2 locus is associated with an increased risk of idiopathic PD. Considerable progress has been made toward understanding the biological functions of LRRK2 and the molecular mechanisms ...
Tsika E, Moore DJ
openaire   +3 more sources

LRRK2 Kinase Activity Is Dependent on LRRK2 GTP Binding Capacity but Independent of LRRK2 GTP Binding

PLoS ONE, 2011
Leucine rich repeat kinase 2 (LRRK2) is a Parkinson's disease (PD) gene that encodes a large multidomain protein including both a GTPase and a kinase domain. GTPases often regulate kinases within signal transduction cascades, where GTPases act as molecular switches cycling between a GTP bound "on" state and a GDP bound "off" state. It has been proposed
Jean-Marc Taymans, Renée Vancraenenbroeck, Petri Ollikainen, Alexandra Beilina, Evy Lobbestael, Marc De Maeyer, Veerle Baekelandt, Mark R Cookson   +7 more
openaire   +4 more sources

LRRK2 Phosphorylation, More Than an Epiphenomenon

Frontiers in Neuroscience, 2020
Mutations in the Leucine Rich Repeat Kinase 2 (LRRK2) gene are linked to autosomal dominant Parkinson's disease (PD), and genetic variations at the LRRK2 locus are associated with an increased risk for sporadic PD.
Antoine Marchand, Antoine Marchand, Matthieu Drouyer, Matthieu Drouyer, Alessia Sarchione, Alessia Sarchione, Marie-Christine Chartier-Harlin, Marie-Christine Chartier-Harlin, Jean-Marc Taymans, Jean-Marc Taymans   +9 more
doaj   +1 more source

In silico, in vitro and cellular analysis with a kinome-wide inhibitor panel correlates cellular LRRK2 dephosphorylation to inhibitor activity on LRRK2

Frontiers in Molecular Neuroscience, 2014
Leucine-rich repeat kinase 2 (LRRK2) is a complex, multidomain protein which is considered a valuable target for potential disease-modifying therapeutic strategies for Parkinson’s disease.
Renee eVancraenenbroeck, Joren eDe Raeymaecker, Evy eLobbestael, Fangye eGao, Marc eDe Maeyer, Arnout eVoet, Veerle eBaekelandt, Jean-Marc eTaymans   +7 more
doaj   +1 more source