- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
1 Online-Ressource.
- Language
-
Englisch
- Bibliographic citation
-
Elevated α-synuclein levels inhibit mitophagic flux ; volume:10 ; number:1 ; day:9 ; month:4 ; year:2024 ; pages:1-15 ; date:12.2024
npj Parkinson's Disease ; 10, Heft 1 (9.4.2024), 1-15, 12.2024
- Creator
-
Kinnart, Inge
Manders, Liselot
Heyninck, Thibaut
Imberechts, Dorien
Praschberger, Roman
Schoovaerts, Nils
Verfaillie, Catherine
Verstreken, Patrik
Vandenberghe, Wim
- Contributor
-
SpringerLink (Online service)
- DOI
-
10.1038/s41531-024-00696-0
- URN
-
urn:nbn:de:101:1-2406241206185.339208893026
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
- 14.08.2025, 11:02 AM CEST
Data provider
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Associated
- Kinnart, Inge
- Manders, Liselot
- Heyninck, Thibaut
- Imberechts, Dorien
- Praschberger, Roman
- Schoovaerts, Nils
- Verfaillie, Catherine
- Verstreken, Patrik
- Vandenberghe, Wim
- SpringerLink (Online service)
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Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity
Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein
Targeted attenuation of elevated histone marks at SNCA alleviates α‐synuclein in Parkinson's disease
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Cerebrospinal fluid lipoproteins inhibit α-synuclein aggregation by interacting with oligomeric species in seed amplification assays
Charakterisierung der α-Synuclein Oligomerisation in Synucleinopathien
Engineering and characterization of a binder to inhibit in vivo α-synuclein aggregation
α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice
Functionalization of α-synuclein fibrils
Induction of CNS α-synuclein pathology by fibrillar and non-amyloidogenic recombinant α-synuclein
Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity
Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein
Targeted attenuation of elevated histone marks at SNCA alleviates α‐synuclein in Parkinson's disease
Overexpression-Induced α-Synuclein Brain Spreading
α-Synuclein and neuronal cell death
SUMOylation modulates α-synuclein [alpha-synuclein] toxicity and fibril formation
Cerebrospinal fluid lipoproteins inhibit α-synuclein aggregation by interacting with oligomeric species in seed amplification assays
Charakterisierung der α-Synuclein Oligomerisation in Synucleinopathien
Engineering and characterization of a binder to inhibit in vivo α-synuclein aggregation
α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice
Functionalization of α-synuclein fibrils
Induction of CNS α-synuclein pathology by fibrillar and non-amyloidogenic recombinant α-synuclein
Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity
Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein
Targeted attenuation of elevated histone marks at SNCA alleviates α‐synuclein in Parkinson's disease
Overexpression-Induced α-Synuclein Brain Spreading
α-Synuclein and neuronal cell death
SUMOylation modulates α-synuclein [alpha-synuclein] toxicity and fibril formation
Cerebrospinal fluid lipoproteins inhibit α-synuclein aggregation by interacting with oligomeric species in seed amplification assays