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Parkin mediates neuroprotection through activation of IκB kinase/nuclear factor-κB signaling
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Parkin is an E3 ubiquitin-ligase for normal and mutant ataxin-2 and prevents ataxin-2-induced cell death
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Parkin protects against neurotoxicity in the 6-hydroxydopamine rat model for Parkinson's disease
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Parkinsonism genes: culprits and clues
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A regulated interaction with the UIM protein Eps15 implicates parkin in EGF receptor trafficking and PI(3) K-Akt signalling
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Cellular parkin mutants are soluble under non-stress conditions
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Diagnosis and treatment of Parkinson disease: molecules to medicine
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Biochemical analysis of Parkinson's disease-causing variants of Parkin, an E3 ubiquitin-protein ligase with monoubiquitylation capacity
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Parkin protects against mitochondrial toxins and β-amyloid accumulation in skeletal muscle cells
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Mutant α-synuclein-induced degeneration is reduced by parkin in a fly model of Parkinson's disease
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GENOME (2006)
α-Synuclein facilitates the toxicity of oxidized catechol metabolites:: Implications for selective neurodegeneration in Parkinson's disease
T Hasegawa et al.
FEBS LETTERS (2006)
Parkin-mediated lysine 63-linked polyubiquitination: A link to protein inclusions formation in Parkinson's and other conformational diseases?
KL Lim et al.
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Stress-induced alterations in parkin solubility promote parkin aggregation and compromise parkin's protective function
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Dopamine covalently modifies and functionally inactivates parkin
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Effect of overexpression of wild-type or mutant parkin on the cellular response induced by toxic insults
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L-DOPA treatment from the viewpoint of neuroprotection - Possible mechanism of specific and progressive dopaminergic neuronal death in Parkinson's disease
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Familial-associated mutations differentially disrupt the solubility, localization, binding and ubiquitination properties of parkin
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Accumulation of the authentic parkin substrate aminoacyl-tRNA synthetase cofactor, p38/JTV-1, leads to catecholaminergic cell death
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Neurotoxicity and behavioral deficits associated with Septin 5 accumulation in dopaminergic neurons
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Parkin negatively regulates JNK pathway in the dopaminergic neurons of Drosophila
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Mixed lineage kinase-c-jun N-terminal kinase signaling pathway: A new therapeutic target in Parkinson's disease
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Alterations in the solubility and intracellular localization of parkin by several familial Parkinson's disease-linked point mutations
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Tyrosinase exacerbates dopamine toxicity but is not genetically associated with Parkinson's disease
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Parkin phosphorylation and modulation of its E3 ubiquitin ligase activity
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Parkin gene therapy for α-synucleinopathy:: A rat model of Parkinson's disease
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Pathogenic mutations inactivate parkin by distinct mechanisms
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Parkin genetics: one model for Parkinson's disease
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Parkin protects human dopaminergic neuroblastoma cells against dopamine-induced apoptosis
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Lentiviral vector delivery of parkin prevents dopaminergic degeneration in an α-synuclein rat model of Parkinson's disease
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Nitrosative stress linked to sporadic Parkinson's disease:: S-nitrosylation of parkin regulates its E3 ubiquitin ligase activity
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PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2004)
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Parkin is recruited into aggresomes in a stress-specific manner: over-expression of parkin reduces aggresome formation but can be dissociated from parkin's effect on neuronal survival
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Parkin attenuates manganese-induced dopaminergic cell death
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S-nitrosylation of Parkin regulates ubiquitination and compromises Parkin's protective function
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SCIENCE (2004)
The C289G and C418R missense mutations cause rapid sequestration of human Parkin into insoluble aggregates
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Novel monoclonal antibodies demonstrate biochemical variation of brain parkin with age
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Inactivation of parkin by oxidative stress and C-terminal truncations - A protective role of molecular chaperones
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RING finger 1 mutations in Parkin produce altered localization of the protein
MR Cookson et al.
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Inhibition of proteasomal activity causes inclusion formation in neuronal and non-neuronal cells overexpressing Parkin
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Increased dopamine and its metabolites in SH-SY5Y neuroblastoma cells that express tyrosinase
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Dopamine induces autophagic cell death and α-synuclein increase in human neuroblastoma SH-SY5Y cells
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The p38 subunit of the aminoacyl-tRNA synthetase complex is a Parkin substrate: linking protein biosynthesis and neurodegeneration
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Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function
YC Tsai et al.
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Parkin suppresses dopaminergic neuron-selective neurotoxicity induced by Pael-R in Drosophila
YF Yang et al.
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Parkin is a component of an SCF-like ubipuitin ligase complex and protects postmitotic neurons from kainate excitotoxicity
JF Staropoli et al.
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Parkin prevents mitochondrial swelling and cytochrome c release in mitochondria-dependent cell death
F Darios et al.
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Parkin protects against the toxicity associated with mutant α-synuclein:: Proteasome dysfunction selectively affects catecholaminergic neurons
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Apoptotic signaling in dopamine-induced cell death:: the role of oxidative stress, p38 mitogen-activated protein kinase, cytochrome c and caspases
E Junn et al.
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An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of parkin
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Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1
Y Zhang et al.
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Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity
Y Imai et al.
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Assembly, target-signaling and intracellular transport of tyrosinase gene family proteins in the initial stage of melanosome biogenesis
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Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase
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