Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity.

Proceedings of the National Academy of Sciences of the United States of America, 2005

1,228 citations recorded by the source corpus.

Subfields: Neurology, Physiology

View Paper: https://www.semanticscholar.org/paper/7502af449a9fc5d3f492a55a05b15fa6f9675f8d

Citations in the corpus

• LRRK2 Mutant iPSC-Derived DA Neurons Demonstrate Increased Susceptibility to Oxidative Stress (2011, neutral): “West and colleagues have shown that the G2019S mutation increases LRRK2 kinase activity and that expression of a LRRK2 G2019S transgene increases susceptibility to peroxide-induced cell death (Cookson, 2009; West et al., 2005).”
• Expanding insights of mitochondrial dysfunction in Parkinson's disease (2006, neutral): “It might be associated with the outer mitochondrial membrane (OMM”
• Human Disease Models in Drosophila melanogaster and the Role of the Fly in Therapeutic Drug Discovery (2011, neutral): “LRRK2 is composed of multiple domains, including a GTPase domain and a kinase domain capable of exhibiting GTP-dependent phosphorylation activity (West et al., 2005).”
• Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates a subset of Rab GTPases (2016, neutral): “The most common PD-associated LRRK2 mutation is the G2019S amino acid substitution, which activates the kinase two- to threefold (West et al., 2005; Khan, 2005; Jaleel et al., 2007).”
• Parkinson's disease: genetics and pathogenesis. (2011, neutral): “Importantly, the most common and best-studied variant, G2019S, increased kinase activity in a number of assays (83), consistent with a toxic, gain-of-function mechanism for LRRK2-associated PD for this allele.”
• Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases (2006, neutral): “Recently, West and colleagues showed that LRRK2 is a kinase, that two disease-associated mutations, including the most common G2019S mutation, augment the kinase activity, and that ∼10p of LRRK2 is associated with mitochondri”
• Pathological roles of MAPK signaling pathways in human diseases. (2010, neutral): “several mutations in the Ras-related GTPase and MAP3K domains of LRRK2 have been associated with familial or sporadic PD [95–97], the”
• The Role of Oxidative Stress in Parkinson’s Disease (2013, neutral): “LRRK2 is predominantly a cytoplasmic protein, although it can also be associated with the outer mitochondrial membrane, raising the possibility that the increased kinase activity of mutant LRRK2 might directly affect mitochondrial function [153] [393].”
• Parkinson's disease-associated mutations in LRRK2 link enhanced GTP-binding and kinase activities to neuronal toxicity. (2007, neutral): “The LRRK2 open-reading frame fused to an myc-his c-terminal tag has been described previously (14).”
• Mitochondrial dysfunction in Parkinson's disease: molecular mechanisms and pathophysiological consequences (2012, neutral): “…kinase families, 4E-BP, the eukaryotic translation initiation factor 4E-binding protein, or the forkhead box transcription factor FoxO1 (West et al , 2005; Gloeckner et al , 2006, 2009; Jaleel et al , 2007; Imai et al , 2008; Parisiadou et al , 2009; Kanao et al , 2010; Zach et al ,…”