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MOLECULAR BIOLOGY OF THE CELL (2007)
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Deletion of the ubiquitin ligase CHIP leads to the accumulation, but not the aggregation, of both endogenous phospho- and caspase-3-cleaved tau species
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Diverse effects of pathogenic mutations of parkin that catalyze multiple monoubiquitylation in vitro
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Parkin ubiquitinates and promotes the degradation of RanBP2
JW Um et al.
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In vivo evidence of CHIP up-regulation attenuating tau aggregation
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Familial-associated mutations differentially disrupt the solubility, localization, binding and ubiquitination properties of parkin
SR Sriram et al.
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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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α-Synuclein and Parkin contribute to the assembly of ubiquitin lysine 63-linked multiubiquitin chains
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Parkin mediates nonclassical, proteasomal-independent ubiquitination of synphilin-1: Implications for Lewy body formation
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Association of DJ-1 and parkin mediated by pathogenic DJ-1 mutations and oxidative stress
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CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation
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CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival
H Shimura et al.
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U-box protein carboxyl terminus of Hsc70-interacting protein (CHIP) mediates poly-ubiquitylation preferentially on four-repeat Tau and is involved in neurodegeneration of tauopathy
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CM Pickart et al.
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CHIP promotes proteasomal degradation of familial ALS-linked mutant SOD1 by ubiquitinating Hsp/Hsc70
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JOURNAL OF NEUROCHEMISTRY (2004)
S-nitrosylation of Parkin regulates ubiquitination and compromises Parkin's protective function
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Novel monoclonal antibodies demonstrate biochemical variation of brain parkin with age
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Molecular pathways of neurodegeneration in Parkinson's disease
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The autosomal recessive juvenile Parkinson disease gene product, parkin, interacts with and ubiquitinates synaptotagmin XI
DP Huynh et al.
HUMAN MOLECULAR GENETICS (2003)
SEPT5_v2 is a parkin-binding protein
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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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Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation
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Parkin is a component of an SCF-like ubipuitin ligase complex and protects postmitotic neurons from kainate excitotoxicity
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NEURON (2003)
Staging of brain pathology related to sporadic Parkinson's disease
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NEUROBIOLOGY OF AGING (2003)
Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin-like domain
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NEUROMOLECULAR MEDICINE (2003)
Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome
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JOURNAL OF BIOLOGICAL CHEMISTRY (2002)
Complex relationship between parkin mutations and Parkinson disease
A West et al.
AMERICAN JOURNAL OF MEDICAL GENETICS (2002)
CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity
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The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
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Chaperone suppression of α-synuclein toxicity in a Drosophila model for Parkinson's disease
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JOURNAL OF BIOLOGICAL CHEMISTRY (2001)
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JAMA-JOURNAL OF THE AMERICAN MEDICAL ASSOCIATION (2001)
Parkin ubiquitinates the α-synuclein-interacting protein, synphilin-1:: implications for Lewy-body formation in Parkinson disease
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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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CELL (2001)
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ANNUAL REVIEW OF NEUROSCIENCE (2001)
Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1
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Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity
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JOURNAL OF BIOLOGICAL CHEMISTRY (2000)
Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase
H Shimura et al.
NATURE GENETICS (2000)
Association between early-onset Parkinson's disease and mutations in the parkin gene
CB Lücking et al.
NEW ENGLAND JOURNAL OF MEDICINE (2000)
The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome
J Lüders et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2000)
Recognition of the polyubiquitin proteolytic signal
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