Dyrk1A phosphorylates parkin at Ser-131 and negatively regulates its ubiquitin E3 ligase activity
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Title
Dyrk1A phosphorylates parkin at Ser-131 and negatively regulates its ubiquitin E3 ligase activity
Authors
Keywords
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Journal
JOURNAL OF NEUROCHEMISTRY
Volume 134, Issue 4, Pages 756-768
Publisher
Wiley
Online
2015-05-12
DOI
10.1111/jnc.13164
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Note: Only part of the references are listed.- New Perspectives of Dyrk1A Role in Neurogenesis and Neuropathologic Features of Down Syndrome
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- Structure of Parkin Reveals Mechanisms for Ubiquitin Ligase Activation
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- Dyrk1A-mediated phosphorylation of Presenilin 1: a functional link between Down syndrome and Alzheimer’s disease
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- Parkin Directly Modulates 26S Proteasome Activity
- (2010) J. W. Um et al. JOURNAL OF NEUROSCIENCE
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- (2010) H. S. Ko et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Development of a novel selective inhibitor of the Down syndrome-related kinase Dyrk1A
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- Identification of a Novel Zn2+-binding Domain in the Autosomal Recessive Juvenile Parkinson-related E3 Ligase Parkin
- (2009) Ventzislava A. Hristova et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- The role of overexpressed DYRK1A protein in the early onset of neurofibrillary degeneration in Down syndrome
- (2008) Jerzy Wegiel et al. ACTA NEUROPATHOLOGICA
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- (2008) Yongsung Kim et al. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
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