Structure of PINK1 and mechanisms of Parkinson's disease-associated mutations.
about
The Anthelmintic Drug Niclosamide and its Analogues Activate the Parkinson's Disease Associated Protein Kinase PINK1.The crystal structure of pseudokinase PEAK1 (Sugen Kinase 269) reveals an unusual catalytic cleft and a novel mode of kinase fold dimerization.Basal Mitophagy Occurs Independently of PINK1 in Mouse Tissues of High Metabolic Demand.PINK1 autophosphorylation is required for ubiquitin recognition.Impact of altered phosphorylation on loss of function of juvenile Parkinsonism-associated genetic variants of the E3 ligase parkin.Cellular and Molecular Basis of Neurodegeneration in Parkinson Disease.Structural insights into ubiquitin phosphorylation by PINK1
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P2860
Structure of PINK1 and mechanisms of Parkinson's disease-associated mutations.
description
2017 nî lūn-bûn
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2017年の論文
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2017年学术文章
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2017年学术文章
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2017年学术文章
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2017年学术文章
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2017年学术文章
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2017年学术文章
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2017年學術文章
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2017年學術文章
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name
Structure of PINK1 and mechanisms of Parkinson's disease-associated mutations.
@en
Structure of PINK1 and mechanisms of Parkinson's disease-associated mutations.
@nl
type
label
Structure of PINK1 and mechanisms of Parkinson's disease-associated mutations.
@en
Structure of PINK1 and mechanisms of Parkinson's disease-associated mutations.
@nl
prefLabel
Structure of PINK1 and mechanisms of Parkinson's disease-associated mutations.
@en
Structure of PINK1 and mechanisms of Parkinson's disease-associated mutations.
@nl
P2093
P2860
P50
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Structure of PINK1 and mechanisms of Parkinson's disease-associated mutations
@en
P2093
Andrew D Waddell
Andrew M Shaw
Helen I Woodroof
Jevgenia Tamjar
Mark Peggie
P2860
P356
10.7554/ELIFE.29985
P407
P577
2017-10-05T00:00:00Z