- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
2051-5960
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
online resource.
- Bibliographic citation
-
Mechanisms underlying extensive Ser129-phosphorylation in α-synuclein aggregates ; volume:5 ; number:1 ; day:15 ; month:6 ; year:2017 ; pages:1-15 ; date:12.2017
Acta Neuropathologica Communications ; 5, Heft 1 (15.6.2017), 1-15, 12.2017
- Keyword
-
Krebs
Onkologie
- Creator
-
Arawaka, Shigeki
- Contributor
-
Sato, Hiroyasu
Sasaki, Asuka
Koyama, Shingo
Katō, Takeo
SpringerLink (Online service)
- DOI
-
10.1186/s40478-017-0452-6
- URN
-
urn:nbn:de:1111-2017101471
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:37 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
- Arawaka, Shigeki
- Sato, Hiroyasu
- Sasaki, Asuka
- Koyama, Shingo
- Katō, Takeo
- SpringerLink (Online service)
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Functionalization of α-synuclein fibrils
Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity
Induction of CNS α-synuclein pathology by fibrillar and non-amyloidogenic recombinant α-synuclein
Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein
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Phosphorylation and O-GlcNAcylation at the same α-synuclein site generate distinct fibril structures
SUMOylation modulates α-synuclein [alpha-synuclein] toxicity and fibril formation
α-Synuclein serine129 phosphorylation – the physiology of pathology
LRRK2 kinase regulates α-synuclein propagation via RAB35 phosphorylation
Parkinson-related parkin reduces α-Synuclein phosphorylation in a gene transfer model
α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice
Functionalization of α-synuclein fibrils
Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity
Induction of CNS α-synuclein pathology by fibrillar and non-amyloidogenic recombinant α-synuclein
Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein
Overexpression-Induced α-Synuclein Brain Spreading
α-Synuclein and neuronal cell death
Phosphorylation and O-GlcNAcylation at the same α-synuclein site generate distinct fibril structures
SUMOylation modulates α-synuclein [alpha-synuclein] toxicity and fibril formation
α-Synuclein serine129 phosphorylation – the physiology of pathology
LRRK2 kinase regulates α-synuclein propagation via RAB35 phosphorylation
Parkinson-related parkin reduces α-Synuclein phosphorylation in a gene transfer model
α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice
Functionalization of α-synuclein fibrils
Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity
Induction of CNS α-synuclein pathology by fibrillar and non-amyloidogenic recombinant α-synuclein
Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein
Overexpression-Induced α-Synuclein Brain Spreading
α-Synuclein and neuronal cell death
Phosphorylation and O-GlcNAcylation at the same α-synuclein site generate distinct fibril structures