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Search results 1 to 13 out of 13 for Lrrk2

Category restricted to InteractionExperiment (x)

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Category: InteractionExperiment
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Type Details Score
Interaction Experiment
Shin N (2008)
Description: LRRK2 regulates synaptic vesicle endocytosis.
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Interaction Experiment
Moehle MS (2015)
Description: The G2019S LRRK2 mutation increases myeloid cell chemotactic responses and enhances LRRK2 binding to actin-regulatory proteins.
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Interaction Experiment
Stafa K (2012)
Description: GTPase activity and neuronal toxicity of Parkinsons disease-associated LRRK2 is regulated by ArfGAP1.
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Interaction Experiment
Li X (2011)
Description: Phosphorylation-dependent 14-3-3 binding to LRRK2 is impaired by common mutations of familial Parkinsons disease.
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Interaction Experiment
Berwick DC (2012)
Description: LRRK2 functions as a Wnt signaling scaffold, bridging cytosolic proteins and membrane-localized LRP6.
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Interaction Experiment
Jaleel M (2007)
Description: LRRK2 phosphorylates moesin at threonine-558: characterization of how Parkinsons disease mutants affect kinase activity.
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Interaction Experiment
Nichols RJ (2010)
Description: 14-3-3 binding to LRRK2 is disrupted by multiple Parkinsons disease-associated mutations and regulates cytoplasmic localization.
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Interaction Experiment
Imai Y (2015)
Description: The Parkinsons Disease-Associated Protein Kinase LRRK2 Modulates Notch Signaling through the Endosomal Pathway.
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Interaction Experiment
Nucifora FC (2016)
Description: Ubiqutination via K27 and K29 chains signals aggregation and neuronal protection of LRRK2 by WSB1.
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Interaction Experiment
Shanley MR (2015)
Description: LRRK2 Facilitates tau Phosphorylation through Strong Interaction with tau and cdk5.
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Interaction Experiment
Stafa K (2014)
Description: Functional interaction of Parkinsons disease-associated LRRK2 with members of the dynamin GTPase superfamily.
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Interaction Experiment
Zach S (2010)
Description: Signal transduction protein array analysis links LRRK2 to Ste20 kinases and PKC zeta that modulate neuronal plasticity.
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Interaction Experiment
Dzamko N (2010)
Description: Inhibition of LRRK2 kinase activity leads to dephosphorylation of Ser(910)/Ser(935), disruption of 14-3-3 binding and altered cytoplasmic localization.
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