Related references
Note: Only part of the references are listed.Parkin mitochondrial translocation is achieved through a novel catalytic activity coupled mechanism
Xinde Zheng et al.
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PHYSIOLOGICAL REVIEWS (2011)
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JOURNAL OF CELL BIOLOGY (2010)
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JOURNAL OF CELL BIOLOGY (2010)
PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy
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Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress
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EMBO JOURNAL (2006)
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HUMAN MOLECULAR GENETICS (2006)
Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin
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NATURE (2006)
Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin
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NATURE (2006)
Phosphate-binding tag, a new tool to visualize phosphorylated proteins
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Diverse effects of pathogenic mutations of parkin that catalyze multiple monoubiquitylation in vitro
N Matsuda et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2006)
Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability
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PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2005)
Parkin phosphorylation and modulation of its E3 ubiquitin ligase activity
A Yamamoto et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2005)
PINK1 mutations are associated with sporadic early-onset parkinsonism
EM Valente et al.
ANNALS OF NEUROLOGY (2004)
Specific and covalent targeting of conjugating and deconjugating enzymes of ubiquitin-like proteins
J Hemelaar et al.
MOLECULAR AND CELLULAR BIOLOGY (2004)
Hereditary early-onset Parkinson's disease caused by mutations in PINK1
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SCIENCE (2004)
Novel monoclonal antibodies demonstrate biochemical variation of brain parkin with age
AC Pawlyk et al.
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Alterations in the common fragile site gene Parkin in ovarian and other cancers
SR Denison et al.
ONCOGENE (2003)
Retrovirus-mediated gene transfer and expression cloning: Powerful tools in functional genornics
T Kitamura et al.
EXPERIMENTAL HEMATOLOGY (2003)
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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Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase
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