Parkinson-causing mutations in LRRK2 impair the physiological tetramerization of endogenous α-synuclein in human neurons
- Standort
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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2373-8057
- Umfang
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Online-Ressource
- Sprache
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Englisch
- Anmerkungen
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online resource.
- Erschienen in
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Parkinson-causing mutations in LRRK2 impair the physiological tetramerization of endogenous α-synuclein in human neurons ; volume:8 ; number:1 ; day:16 ; month:9 ; year:2022 ; pages:1-10 ; date:12.2022
npj Parkinson's Disease ; 8, Heft 1 (16.9.2022), 1-10, 12.2022
- Urheber
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Fonseca-Ornelas, Luis
Stricker, Jonathan M. S.
Soriano-Cruz, Stephanie
Weykopf, Beatrice
Dettmer, Ulf
Muratore, Christina R.
Scherzer, Clemens R.
Selkoe, Dennis J.
- Beteiligte Personen und Organisationen
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SpringerLink (Online service)
- DOI
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10.1038/s41531-022-00380-1
- URN
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urn:nbn:de:101:1-2022120309192443652506
- Rechteinformation
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
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15.08.2025, 07:20 MESZ
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Beteiligte
- Fonseca-Ornelas, Luis
- Stricker, Jonathan M. S.
- Soriano-Cruz, Stephanie
- Weykopf, Beatrice
- Dettmer, Ulf
- Muratore, Christina R.
- Scherzer, Clemens R.
- Selkoe, Dennis J.
- SpringerLink (Online service)
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LRRK2 activity does not dramatically alter α-synuclein pathology in primary neurons
Pathological α-synuclein recruits LRRK2 expressing pro-inflammatory monocytes to the brain
LRRK2 interactions with α-synuclein in Parkinson’s disease brains and in cell models
Inhibition of LRRK2 kinase activity promotes anterograde axonal transport and presynaptic targeting of α-synuclein
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LRRK2 kinase regulates α-synuclein propagation via RAB35 phosphorylation
Leucine-rich repeat kinase 2 (LRRK2) regulates α-synuclein clearance in microglia
LRRK2 activity does not dramatically alter α-synuclein pathology in primary neurons
Pathological α-synuclein recruits LRRK2 expressing pro-inflammatory monocytes to the brain
LRRK2 interactions with α-synuclein in Parkinson’s disease brains and in cell models
Inhibition of LRRK2 kinase activity promotes anterograde axonal transport and presynaptic targeting of α-synuclein
α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice
LRRK2 inhibition does not impart protection from α-synuclein pathology and neuron death in non-transgenic 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