The endosomal pathway in Parkinson's disease.
Oxford, United Kingdom. In Mol Cell Neurosci, Mar 2015
In this review, we summarized the evidence that a number of Parkinson's associated genetic mutations or polymorphisms (LRRK2, VPS35, GBA, ATP13A2, ATP6AP2, DNAJC13/RME-8, RAB7L1, GAK) disrupt protein trafficking and degradation via the endosomal pathway and discussed how such defects could arise from or contribute to the accumulation and misfolding of α-synuclein in Lewy bodies.
Multiplying messages LRRK beneath Parkinson disease.
Ann Arbor, United States. In Cell, May 2014
link PD protein leucine-rich repeat kinase 2 (LRRK2) to abnormalities of translational control, a pathogenic mechanism implicated in an increasing number of CNS neurodegenerative diseases, as well as in normal aging.
Progressive degeneration of human neural stem cells caused by pathogenic LRRK2.
Beijing, China. In Nature, 2012
We decided to evaluate nuclear organization in the context of ageing-associated disorders by focusing on a leucine-rich repeat kinase 2 (LRRK2) dominant mutation (G2019S; glycine-to-serine substitution at amino acid 2019), which is associated with familial and sporadic Parkinson's disease as well as impairment of adult neurogenesis in mice.
Pathological roles of α-synuclein in neurological disorders.
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Athens, Greece. In Lancet Neurol, 2011
α-Synuclein also seems to be linked to other genetic forms of Parkinson's disease, such as those linked to mutations in GBA or LRRK2, possibly through common effects on autophagy and lysosomal function.