Structure of PINK1 and mechanisms of Parkinson's disease-associated mutations
Published 2017 View Full Article
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Title
Structure of PINK1 and mechanisms of Parkinson's disease-associated mutations
Authors
Keywords
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Journal
eLife
Volume 6, Issue -, Pages -
Publisher
eLife Sciences Organisation, Ltd.
Online
2017-10-05
DOI
10.7554/elife.29985
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Related references
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- Sequence Determinants of a Specific Inactive Protein Kinase Conformation
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- PINK1 rendered temperature sensitive by disease-associated and engineered mutations
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- A Dimeric PINK1-containing Complex on Depolarized Mitochondria Stimulates Parkin Recruitment
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- Parkin-catalyzed Ubiquitin-Ester Transfer Is Triggered by PINK1-dependent Phosphorylation
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- PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria
- (2012) Kei Okatsu et al. Nature Communications
- PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65
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