α-Synuclein Induces the GSK-3-Mediated Phosphorylation and Degradation of NURR1 and Loss of Dopaminergic Hallmarks
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
1559-1182
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Anmerkungen
-
online resource.
- Erschienen in
-
α-Synuclein Induces the GSK-3-Mediated Phosphorylation and Degradation of NURR1 and Loss of Dopaminergic Hallmarks ; volume:58 ; number:12 ; day:5 ; month:10 ; year:2021 ; pages:6697-6711 ; date:12.2021
Molecular neurobiology ; 58, Heft 12 (5.10.2021), 6697-6711, 12.2021
- Urheber
-
García-Yagüe, Ángel Juan
Lastres-Becker, Isabel
Stefanis, Leonidas
Vassilatis, Demetrios K.
Cuadrado, Antonio
- Beteiligte Personen und Organisationen
-
SpringerLink (Online service)
- DOI
-
10.1007/s12035-021-02558-9
- URN
-
urn:nbn:de:101:1-2022020608184985910196
- Rechteinformation
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
15.08.2002, 07:24 MESZ
Datenpartner
Dieses Objekt wird bereitgestellt von:
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
- García-Yagüe, Ángel Juan
- Lastres-Becker, Isabel
- Stefanis, Leonidas
- Vassilatis, Demetrios K.
- Cuadrado, Antonio
- SpringerLink (Online service)
Ähnliche Objekte (12)
![Investigation of in vivo dopaminergic neuronal response to proteasome inhibition and mutant α-synuclein [alpha-synuclein] overexpression](/assets/placeholder/searchResultMediaNoDigitisedMedia.png)
Investigation of in vivo dopaminergic neuronal response to proteasome inhibition and mutant α-synuclein [alpha-synuclein] overexpression
Pathophysiology of α-synuclein spreading along the nigrostriatal dopaminergic pathway and its age-dependency
27-Hydroxycholesterol increases α-synuclein protein levels through proteasomal inhibition in human dopaminergic neurons
α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice
Functionalization of α-synuclein fibrils
Early-onset impairment of the ubiquitin-proteasome system in dopaminergic neurons caused by α-synuclein
Protection from α-Synuclein induced dopaminergic neurodegeneration by overexpression of the mitochondrial import receptor TOM20
Upregulating β-hexosaminidase activity in rodents prevents α-synuclein lipid associations and protects dopaminergic neurons from α-synuclein-mediated neurotoxicity
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
Retraction Note: 27-Hydroxycholesterol increases α-synuclein protein levels through proteasomal inhibition in human dopaminergic neurons
Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein
Investigation of in vivo dopaminergic neuronal response to proteasome inhibition and mutant α-synuclein [alpha-synuclein] overexpression
Pathophysiology of α-synuclein spreading along the nigrostriatal dopaminergic pathway and its age-dependency
27-Hydroxycholesterol increases α-synuclein protein levels through proteasomal inhibition in human dopaminergic neurons
α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice
Functionalization of α-synuclein fibrils
Early-onset impairment of the ubiquitin-proteasome system in dopaminergic neurons caused by α-synuclein
Protection from α-Synuclein induced dopaminergic neurodegeneration by overexpression of the mitochondrial import receptor TOM20
Upregulating β-hexosaminidase activity in rodents prevents α-synuclein lipid associations and protects dopaminergic neurons from α-synuclein-mediated neurotoxicity
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
Retraction Note: 27-Hydroxycholesterol increases α-synuclein protein levels through proteasomal inhibition in human dopaminergic neurons
Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein
Investigation of in vivo dopaminergic neuronal response to proteasome inhibition and mutant α-synuclein [alpha-synuclein] overexpression
Pathophysiology of α-synuclein spreading along the nigrostriatal dopaminergic pathway and its age-dependency
27-Hydroxycholesterol increases α-synuclein protein levels through proteasomal inhibition in human dopaminergic neurons
α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice
Functionalization of α-synuclein fibrils
Early-onset impairment of the ubiquitin-proteasome system in dopaminergic neurons caused by α-synuclein
Protection from α-Synuclein induced dopaminergic neurodegeneration by overexpression of the mitochondrial import receptor TOM20
Upregulating β-hexosaminidase activity in rodents prevents α-synuclein lipid associations and protects dopaminergic neurons from α-synuclein-mediated neurotoxicity
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
Retraction Note: 27-Hydroxycholesterol increases α-synuclein protein levels through proteasomal inhibition in human dopaminergic neurons