Parkinson's disease-associated mutations in LRRK2 link enhanced GTP-binding and kinase activities to neuronal toxicity.
By A. West, D. Moore, Catherine Y. Choi, Shaida A. Andrabi, X. Li, Dustin A. Dikeman, S. Biskup, Zhenshui Zhang, K. Lim, Valina L. Dawson and 1 more. Human Molecular Genetics, 2007
619 citations recorded by the source corpus.
Subfields: Neurology, Physiology
View Paper: https://www.semanticscholar.org/paper/6b230f30f00d53cee2bdc5e6e327e62da443a2fc
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Citations in the corpus
- Genetic Animal Models of Parkinson’s Disease (2010, neutral): “It has been difficult to build a consensus and unifying theory on how parkin dysfunction leads to neurodegeneration in PD. Numerous putative substrates for parkin have been reported (for review see Dawson and Dawson, 2010; West et al., 2007a).”
- Parkinson Disease Epidemiology, Pathology, Genetics and Pathophysiology (2019, background): “Prior studies suggest that mutations in LRRK2 lead to increased kinase activity(42), and that LRRK2 kinase inhibitors may be protective(43), although the possibility of a role for loss of LRRK2 function has been raised(44).”
- Human Disease Models in Drosophila melanogaster and the Role of the Fly in Therapeutic Drug Discovery (2011, background): “It has been shown that the disease-associated mutations of LRRK2 can increase its kinase activity and thereby its toxicity (Smith et al., 2006; West et al., 2007).”
- Mitochondrial dysfunction in Parkinson's disease: molecular mechanisms and pathophysiological consequences (2012, neutral): “Overexpression of pathogenic LRRK2 mutants in cultured cells, primary neurons or rodents causes cellular toxicity, which is dependent on the kinase activity (Greggio et al , 2006; Smith et al , 2006; West et al , 2007; Ho et al , 2009; Dusonchet et al , 2011).”