Revisiting the Roco G protein cycle.
In Biochem J, 15 Nov 2014
UNLABELLED: Mutations in leucine-rich-repeat kinase 2 (LRRK2) are the most frequent cause of late-onset Parkinson's disease (PD).
Injury-induced immune responses in Hydra.
Genève, Switzerland. In Semin Immunol, Aug 2014
These regulations point to an enhanced cytoprotection via ROS signaling (Nrf, C/EBP, p62/SQSMT1-l2), TNFR and TLR signaling (TNFR16-like, TRAF2l, TRAF5l, jun, fos-related, SIK2, ATF1/CREB, LRRC28, LRRC40, LRRK2), proteasomal activity (p62/SQSMT1-l1, Ced6/Gulf, NEDD8-conjugating enzyme Ubc12), stress proteins (CRYAB1, CRYAB2, HSP16.2,
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.
Interaction of LRRK2 with kinase and GTPase signaling cascades.
Boston, United States. In Front Mol Neurosci, Dec 2013
LRRK2 is a protein that interacts with a plethora of signaling molecules, but the complexity of LRRK2 function presents a challenge for understanding the role of LRRK2 in the pathophysiology of Parkinson's disease (PD).
Genetics and genomics of Parkinson's disease.
Vancouver, Canada. In Genome Med, Dec 2013
Recent discoveries in sporadic, Mendelian and more complex forms of parkinsonism provide novel insight into disease etiology; 28 genes, including those encoding alpha-synuclein (SNCA), leucine-rich repeat kinase 2 (LRRK2) and microtubule-associated protein tau (MAPT), have been linked and/or associated with PD.
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.
More papers using
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.