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Kei Okatsu et al.
JOURNAL OF CELL BIOLOGY (2015)
The Roles of PINK1, Parkin, and Mitochondrial Fidelity in Parkinson's Disease
Alicia M. Pickrell et al.
NEURON (2015)
Defining roles of PARKIN and ubiquitin phosphorylation by PINK1 in mitochondrial quality control using a ubiquitin replacement strategy
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Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis
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PINK1 and Parkin - mitochondrial interplay between phosphorylation and ubiquitylation in Parkinson's disease
Agne Kazlauskaite et al.
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Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65
Agne Kazlauskaite et al.
BIOCHEMICAL JOURNAL (2014)
PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity
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Quantitative Proteomics Reveal a Feedforward Mechanism for Mitochondrial PARKIN Translocation and Ubiquitin Chain Synthesis
Alban Ordureau et al.
MOLECULAR CELL (2014)
Phosphorylation by PINK1 Releases the UBL Domain and Initializes the Conformational Opening of the E3 Ubiquitin Ligase Parkin
Thomas R. Caulfield et al.
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Phosphorylation of Mitochondrial Polyubiquitin by PINK1 Promotes Parkin Mitochondrial Tethering
Kahori Shiba-Fukushima et al.
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Parkin mitochondrial translocation is achieved through a novel catalytic activity coupled mechanism
Xinde Zheng et al.
CELL RESEARCH (2013)
Mitochondrial quality control turns out to be the principal suspect in parkin and PINK1-related autosomal recessive Parkinson's disease
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TRIAD1 and HHARI bind to and are activated by distinct neddylated Cullin-RING ligase complexes
Ian R. Kelsall et al.
EMBO JOURNAL (2013)
Structure of the human Parkin ligase domain in an autoinhibited state
Tobias Wauer et al.
EMBO JOURNAL (2013)
Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization
Shireen A. Sarraf et al.
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Structure of Parkin Reveals Mechanisms for Ubiquitin Ligase Activation
Jean-Francois Trempe et al.
SCIENCE (2013)
Structure of HHARI, a RING-IBR-RING Ubiquitin Ligase: Autoinhibition of an Ariadne-Family E3 and Insights into Ligation Mechanism
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Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases
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BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer
Hao Dou et al.
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PINK1-mediated phosphorylation of the Parkin ubiquitin-like domain primes mitochondrial translocation of Parkin and regulates mitophagy
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PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65
Chandana Kondapalli et al.
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Features and development of Coot
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ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY (2010)
Somatic mutations of the Parkinson's disease-associated gene PARK2 in glioblastoma and other human malignancies
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Evidence for Bidentate Substrate Binding as the Basis for the K48 Linkage Specificity of Otubain 1
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JOURNAL OF MOLECULAR BIOLOGY (2009)
Genotypic and Phenotypic Characteristics of Dutch Patients with Early Onset Parkinson's Disease
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MOVEMENT DISORDERS (2009)
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JOURNAL OF APPLIED CRYSTALLOGRAPHY (2007)
Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin-like domain
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EMBO REPORTS (2003)
Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme
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