A novel mouse model for investigating α-synuclein aggregates in oligodendrocytes: implications for the glial cytoplasmic inclusions in multiple system atrophy
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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1 Online-Ressource.
- Language
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Englisch
- Bibliographic citation
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A novel mouse model for investigating α-synuclein aggregates in oligodendrocytes: implications for the glial cytoplasmic inclusions in multiple system atrophy ; volume:17 ; number:1 ; day:24 ; month:5 ; year:2024 ; pages:1-13 ; date:12.2024
Molecular brain ; 17, Heft 1 (24.5.2024), 1-13, 12.2024
- Creator
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Ishimoto, Tomoyuki
Oono, Miki
Kaji, Seiji
Ayaki, Takashi
Nishida, Katsuya
Funakawa, Itaru
Maki, Takakuni
Matsuzawa, Shu-ichi
Takahashi, Ryosuke
Yamakado, Hodaka
- Contributor
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SpringerLink (Online service)
- DOI
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10.1186/s13041-024-01104-7
- URN
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urn:nbn:de:101:1-2408051123260.905125197741
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 10:44 AM CEST
Data provider
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Associated
- Ishimoto, Tomoyuki
- Oono, Miki
- Kaji, Seiji
- Ayaki, Takashi
- Nishida, Katsuya
- Funakawa, Itaru
- Maki, Takakuni
- Matsuzawa, Shu-ichi
- Takahashi, Ryosuke
- Yamakado, Hodaka
- SpringerLink (Online service)
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Filamentous aggregations of phosphorylated α-synuclein in Schwann cells (Schwann cell cytoplasmic inclusions) in multiple system atrophy
Conformational templating of α-synuclein aggregates in neuronal-glial cultures
Binding of α-synuclein oligomers to Cx32 facilitates protein uptake and transfer in neurons and oligodendrocytes
Association of Glial Activation and α-Synuclein Pathology in Parkinson’s Disease
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Establishment of primary culture models of multiple system atrophy based on expression of α-synuclein [alpha-synuclein] in oligodendrocytes : analysis of α-synuclein aggregation and associated pathologies
Reduced progranulin increases tau and α-synuclein inclusions and alters mouse tauopathy phenotypes via glucocerebrosidase
Detection of giant cytoplasmic inclusions in a pediatric patient with recurrent infections: a case report
Glial senescence enhances α-synuclein pathology owing to its insufficient clearance caused by autophagy dysfunction
Electroacupuncture remediates glial dysfunction and ameliorates neurodegeneration in the astrocytic α-synuclein mutant mouse model
How do oligodendrocytes enwrap axons?
Insights into the pathogenesis of multiple system atrophy: focus on glial cytoplasmic inclusions
Filamentous aggregations of phosphorylated α-synuclein in Schwann cells (Schwann cell cytoplasmic inclusions) in multiple system atrophy
Conformational templating of α-synuclein aggregates in neuronal-glial cultures
Binding of α-synuclein oligomers to Cx32 facilitates protein uptake and transfer in neurons and oligodendrocytes
Association of Glial Activation and α-Synuclein Pathology in Parkinson’s Disease
Autophagy defects and related genetic variations in renal cell carcinoma with eosinophilic cytoplasmic inclusions
Establishment of primary culture models of multiple system atrophy based on expression of α-synuclein [alpha-synuclein] in oligodendrocytes : analysis of α-synuclein aggregation and associated pathologies
Reduced progranulin increases tau and α-synuclein inclusions and alters mouse tauopathy phenotypes via glucocerebrosidase
Detection of giant cytoplasmic inclusions in a pediatric patient with recurrent infections: a case report
Glial senescence enhances α-synuclein pathology owing to its insufficient clearance caused by autophagy dysfunction
Electroacupuncture remediates glial dysfunction and ameliorates neurodegeneration in the astrocytic α-synuclein mutant mouse model