- 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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Alpha-synuclein aggregates are phosphatase resistant ; volume:12 ; number:1 ; day:31 ; month:5 ; year:2024 ; pages:1-13 ; date:12.2024
Acta Neuropathologica Communications ; 12, Heft 1 (31.5.2024), 1-13, 12.2024
- Creator
-
Choi, S. G.
Tittle, T.
Garcia-Prada, D.
Kordower, J. H.
Melki, R.
Killinger, B. A.
- Contributor
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SpringerLink (Online service)
- DOI
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10.1186/s40478-024-01785-0
- URN
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urn:nbn:de:101:1-2408082127562.216977163180
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
14.08.2025, 10:46 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
- Choi, S. G.
- Tittle, T.
- Garcia-Prada, D.
- Kordower, J. H.
- Melki, R.
- Killinger, B. A.
- SpringerLink (Online service)
Other Objects (12)
Alpha-Synuclein aggregate formation in oligodendroglia OLN-t40 cells stably transfected with alpha-Synuclein
A Stable Lipid-Induced Aggregate of alpha-Synuclein
Structural characterization of alpha-synuclein aggregates seeded by patient material
Toxicity of extracellular alpha-synuclein is independent of intracellular alpha-synuclein
Alpha-synuclein inclusion responsive microglia are resistant to CSF1R inhibition
Single‐Molecule Two‐Color Coincidence Detection of Unlabeled alpha‐Synuclein Aggregates
Single‐Molecule Two‐Color Coincidence Detection of Unlabeled alpha‐Synuclein Aggregates
Alpha‐synuclein aggregates activate calcium pump SERCA leading to calcium dysregulation
Multiple Protective Roles of Nanoliposome‐Incorporated Baicalein against Alpha‐Synuclein Aggregates
The Molecular Mechanism of Alpha-Synuclein Dependent Regulation of Protein Phosphatase 2A Activity
Pathogenic alpha-synuclein aggregates preferentially bind to mitochondria and affect cellular respiration
Organotypic slice culture model demonstrates inter-neuronal spreading of alpha-synuclein aggregates
Alpha-Synuclein aggregate formation in oligodendroglia OLN-t40 cells stably transfected with alpha-Synuclein
A Stable Lipid-Induced Aggregate of alpha-Synuclein
Structural characterization of alpha-synuclein aggregates seeded by patient material
Toxicity of extracellular alpha-synuclein is independent of intracellular alpha-synuclein
Alpha-synuclein inclusion responsive microglia are resistant to CSF1R inhibition
Single‐Molecule Two‐Color Coincidence Detection of Unlabeled alpha‐Synuclein Aggregates
Single‐Molecule Two‐Color Coincidence Detection of Unlabeled alpha‐Synuclein Aggregates
Alpha‐synuclein aggregates activate calcium pump SERCA leading to calcium dysregulation
Multiple Protective Roles of Nanoliposome‐Incorporated Baicalein against Alpha‐Synuclein Aggregates
The Molecular Mechanism of Alpha-Synuclein Dependent Regulation of Protein Phosphatase 2A Activity
Pathogenic alpha-synuclein aggregates preferentially bind to mitochondria and affect cellular respiration
Organotypic slice culture model demonstrates inter-neuronal spreading of alpha-synuclein aggregates
Alpha-Synuclein aggregate formation in oligodendroglia OLN-t40 cells stably transfected with alpha-Synuclein
A Stable Lipid-Induced Aggregate of alpha-Synuclein
Structural characterization of alpha-synuclein aggregates seeded by patient material
Toxicity of extracellular alpha-synuclein is independent of intracellular alpha-synuclein
Alpha-synuclein inclusion responsive microglia are resistant to CSF1R inhibition
Single‐Molecule Two‐Color Coincidence Detection of Unlabeled alpha‐Synuclein Aggregates
Single‐Molecule Two‐Color Coincidence Detection of Unlabeled alpha‐Synuclein Aggregates
Alpha‐synuclein aggregates activate calcium pump SERCA leading to calcium dysregulation
Multiple Protective Roles of Nanoliposome‐Incorporated Baicalein against Alpha‐Synuclein Aggregates
The Molecular Mechanism of Alpha-Synuclein Dependent Regulation of Protein Phosphatase 2A Activity
Pathogenic alpha-synuclein aggregates preferentially bind to mitochondria and affect cellular respiration