- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Bibliographic citation
-
A Ubl/ubiquitin switch in the activation of Parkin ; volume:34 ; number:20 ; year:2015 ; pages:2492-2505 ; extent:14
The EMBO journal / European Molecular Biology Organization ; 34, Heft 20 (2015), 2492-2505 (gesamt 14)
- Creator
-
Sauvé, Véronique
Lilov, Asparouh
Seirafi, Marjan
Vranas, Marta
Rasool, Shafqat
Kozlov, Guennadi
Sprules, Tara
Wang, Jimin
Trempe, Jean‐François
Gehring, Kalle
- DOI
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10.15252/embj.201592237
- URN
-
urn:nbn:de:101:1-2022112405533928597520
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:32 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Sauvé, Véronique
- Lilov, Asparouh
- Seirafi, Marjan
- Vranas, Marta
- Rasool, Shafqat
- Kozlov, Guennadi
- Sprules, Tara
- Wang, Jimin
- Trempe, Jean‐François
- Gehring, Kalle
Other Objects (12)
Parkin is an E3 ligase for the ubiquitin-like modifier FAT10, which inhibits Parkin activation and mitophagy
Binding to serine 65‐phosphorylated ubiquitin primes Parkin for optimal PINK 1‐dependent phosphorylation and activation
A conformational switch regulates the ubiquitin ligase HUWE1
Activation of parkin by a molecular glue
Interleukin-1β drives NEDD8 nuclear-to-cytoplasmic translocation, fostering parkin activation via NEDD8 binding to the P-ubiquitin activating site
Mechanistic insights into the function and dysfunction of Parkin, an E3 ubiquitin ligase associated with Parkinson's disease
Mechanistic insights into the function and dysfunction of Parkin, an E3 ubiquitin ligase associated with Parkinson's disease
Disruption of the autoinhibited state primes the E3 ligase parkin for activation and catalysis
Parkin, J. H.
Dr. Parkin's Opinion.
Expressionsstudien zu Parkin
The ubiquitin-like modifier FAT10 interferes with SUMO activation
Parkin is an E3 ligase for the ubiquitin-like modifier FAT10, which inhibits Parkin activation and mitophagy
Binding to serine 65‐phosphorylated ubiquitin primes Parkin for optimal PINK 1‐dependent phosphorylation and activation
A conformational switch regulates the ubiquitin ligase HUWE1
Activation of parkin by a molecular glue
Interleukin-1β drives NEDD8 nuclear-to-cytoplasmic translocation, fostering parkin activation via NEDD8 binding to the P-ubiquitin activating site
Mechanistic insights into the function and dysfunction of Parkin, an E3 ubiquitin ligase associated with Parkinson's disease
Mechanistic insights into the function and dysfunction of Parkin, an E3 ubiquitin ligase associated with Parkinson's disease
Disruption of the autoinhibited state primes the E3 ligase parkin for activation and catalysis
Parkin, J. H.
Dr. Parkin's Opinion.
Expressionsstudien zu Parkin
The ubiquitin-like modifier FAT10 interferes with SUMO activation
Parkin is an E3 ligase for the ubiquitin-like modifier FAT10, which inhibits Parkin activation and mitophagy
Binding to serine 65‐phosphorylated ubiquitin primes Parkin for optimal PINK 1‐dependent phosphorylation and activation
A conformational switch regulates the ubiquitin ligase HUWE1
Activation of parkin by a molecular glue
Interleukin-1β drives NEDD8 nuclear-to-cytoplasmic translocation, fostering parkin activation via NEDD8 binding to the P-ubiquitin activating site
Mechanistic insights into the function and dysfunction of Parkin, an E3 ubiquitin ligase associated with Parkinson's disease
Mechanistic insights into the function and dysfunction of Parkin, an E3 ubiquitin ligase associated with Parkinson's disease
Disruption of the autoinhibited state primes the E3 ligase parkin for activation and catalysis
Parkin, J. H.
Dr. Parkin's Opinion.
Expressionsstudien zu Parkin