Casein Kinase II-mediated Phosphorylation Regulates α-Synuclein/Synphilin-1 Interaction and Inclusion Body Formation
Authors:
- Mikiei TanakaMTMikiei Tanaka
- Kiho ParkKPKiho Park
- Sang Seop LeeSLSang Seop Lee
- Yong Man KimYKYong Man Kim
- Eunsung JunnEJEunsung Junn
- Sang-Hyeon LeeSLSang-Hyeon Lee
- M. Maral MouradianMMM. Maral Mouradian
Open Access
- 1 February 2004
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 279 (8) , 6834-6839
Abstract
No abstract availableKeywords
This publication has 38 references indexed in Scilit:
- α-Synuclein is phosphorylated in synucleinopathy lesionsNature Cell Biology, 2002
- Recent advances in the genetics and pathogenesis of Parkinson diseaseNeurology, 2002
- Specificity in intracellular protein aggregation and inclusion body formationProceedings of the National Academy of Sciences, 2001
- Parkin ubiquitinates the α-synuclein–interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson diseaseNature Medicine, 2001
- Constitutive Phosphorylation of the Parkinson's Disease Associated α-SynucleinJournal of Biological Chemistry, 2000
- Synphilin-1 associates with α-synuclein and promotes the formation of cytosolic inclusionsNature Genetics, 1999
- Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson diseaseNature Medicine, 1998
- AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's diseaseNature Genetics, 1998
- α-Synuclein in Lewy bodiesNature, 1997
- Mutation in the α-Synuclein Gene Identified in Families with Parkinson's DiseaseScience, 1997