ArticleThe American journal of pathology2003
Ubiquitination of alpha-synuclein is not required for formation of pathological inclusions in alpha-synucleinopathies.
Article in The American journal of pathology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed.
- Protein modification in neurodegenerative diseases.MedComm · 2024Review
- Single-domain antibody-based protein degrader for synucleinopathies.Molecular neurodegeneration · 2024Article
- Single-Domain Antibody-Based Protein Degrader for Synucleinopathies.bioRxiv : the preprint server for biology · 2024Article
- Review
- Development and validation of an expanded antibody toolset that captures alpha-synuclein pathological diversity in Lewy body diseases.NPJ Parkinson's disease · 2023Article
- Synthesis of ubiquitinated proteins for biochemical and functional analysis.Chemical science · 2023Review
- Neuroprotective Effects of the Neural-Induced Adipose-Derived Stem Cell Secretome against Rotenone-Induced Mitochondrial and Endoplasmic Reticulum Dysfunction.International journal of molecular sciences · 2023Article
- Neuronal activity modulates alpha-synuclein aggregation and spreading in organotypic brain slice cultures and in vivo.Acta neuropathologica · 2020Article
- α-Synuclein filaments from transgenic mouse and human synucleinopathy-containing brains are major seed-competent species.The Journal of biological chemistry · 2020Article
- Targeting α-synuclein for PD Therapeutics: A Pursuit on All Fronts.Biomolecules · 2020Review
- Unique α-synuclein pathology within the amygdala in Lewy body dementia: implications for disease initiation and progression.Acta neuropathologica communications · 2019Article
- The Roles of Post-translational Modifications on α-Synuclein in the Pathogenesis of Parkinson's Diseases.Frontiers in neuroscience · 2019Review
- Skin α-synuclein deposits differ in clinical variants of synucleinopathy: an in vivo study.Scientific reports · 2018Article
- Neurodegeneration and the ordered assembly of α-synuclein.Cell and tissue research · 2018Review
- The Synucleinopathies: Twenty Years On.Journal of Parkinson's disease · 2017Review
- Inhibition of Protein Ubiquitination by Paraquat and 1-Methyl-4-Phenylpyridinium Impairs Ubiquitin-Dependent Protein Degradation Pathways.Molecular neurobiology · 2016Article
- Protein misfolding specifies recruitment to cytoplasmic inclusion bodies.The Journal of cell biology · 2016Article
- Synthesis of a Bis-thio-acetone (BTA) Analogue of the Lysine Isopeptide Bond and its Application to Investigate the Effects of Ubiquitination and SUMOylation on α-Synuclein Aggregation and Toxicity.ACS chemical biology · 2016Article
- Dynamic structural flexibility of α-synuclein.Neurobiology of disease · 2016Review
- Pallidal neuronal apolipoprotein E in pantothenate kinase-associated neurodegeneration recapitulates ischemic injury to the globus pallidus.Molecular genetics and metabolism · 2015Article
4 more citing papers are in PubMed but not listed here.
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5 authors.
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Abstract
alpha-Synucleinopathies, including Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy, are neurodegenerative disorders in which abnormal inclusions containing alpha-synuclein accumulate in selectively vulnerable neurons and glia. In this report, immunohistochemistry demonstrates ubiquitin in subsets of alpha-synuclein inclusions in dementia with Lewy bodies and multiple system atrophy. Biochemistry demonstrates that alpha-synuclein in the sodium dodecyl sulfate-soluble fractions of diseased brains is ubiquitinated, with mono- and di-ubiquitinated species predominating over polyubiquitinated forms. Similar immunohistochemical and biochemical characteristics were observed in an A53T mutant human alpha-synuclein transgenic mouse model of neurodegenerative alpha-synucleinopathies. Furthermore, in vitro ubiquitination of alpha-synuclein fibrils recapitulated the pattern of alpha-synuclein ubiquitination observed in human disease and the A53T alpha-synuclein mouse model. These results suggest that ubiquitination of alpha-synuclein is not required for inclusion formation and follows the fibrillization of alpha-synuclein.
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