Upregulating β-hexosaminidase activity in rodents prevents α-synuclein lipid associations and protects dopaminergic neurons from α-synuclein-mediated neurotoxicity
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
2051-5960
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Anmerkungen
-
online resource.
- Erschienen in
-
Upregulating β-hexosaminidase activity in rodents prevents α-synuclein lipid associations and protects dopaminergic neurons from α-synuclein-mediated neurotoxicity ; volume:8 ; number:1 ; day:6 ; month:8 ; year:2020 ; pages:1-14 ; date:12.2020
Acta Neuropathologica Communications ; 8, Heft 1 (6.8.2020), 1-14, 12.2020
- Urheber
-
Brekk, Oeystein R.
Korecka, Joanna A.
Crapart, Cecile C.
Huebecker, Mylene
MacBain, Zachary K.
Rosenthal, Sara Ann
Sena-Esteves, Miguel
Priestman, David A.
Platt, Frances M.
Isacson, Ole
Hallett, Penelope J.
- Beteiligte Personen und Organisationen
-
SpringerLink (Online service)
- DOI
-
10.1186/s40478-020-01004-6
- URN
-
urn:nbn:de:101:1-2020100121143595512335
- Rechteinformation
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
14.08.2025, 10:52 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
- Brekk, Oeystein R.
- Korecka, Joanna A.
- Crapart, Cecile C.
- Huebecker, Mylene
- MacBain, Zachary K.
- Rosenthal, Sara Ann
- Sena-Esteves, Miguel
- Priestman, David A.
- Platt, Frances M.
- Isacson, Ole
- Hallett, Penelope J.
- SpringerLink (Online service)
Ähnliche Objekte (12)
Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity
α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice
Oligomerization of Lrrk controls actin severing and α-synuclein neurotoxicity in vivo
Functionalization of α-synuclein fibrils
SUMOylation modulates α-synuclein [alpha-synuclein] toxicity and fibril formation
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
![Regulation des Proteins α-Synuclein [Alpha-Synuclein] während der zellulären Alterung](/assets/placeholder/searchResultMediaNoDigitisedMedia.png)
Regulation des Proteins α-Synuclein [Alpha-Synuclein] während der zellulären Alterung
Structural features and environmental conditions regulating α-synuclein [alpha-synuclein] aggregation
Synuclein Family Members Prevent Membrane Damage by Counteracting α-Synuclein Aggregation
Domänenstrukturen in Phospholipidmembranen und die Toxizität von α-Synuclein [Alpha-Synuclein]
Synuclein Family Members Prevent Membrane Damage by Counteracting α-Synuclein Aggregation
Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity
α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice
Oligomerization of Lrrk controls actin severing and α-synuclein neurotoxicity in vivo
Functionalization of α-synuclein fibrils
SUMOylation modulates α-synuclein [alpha-synuclein] toxicity and fibril formation
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
Regulation des Proteins α-Synuclein [Alpha-Synuclein] während der zellulären Alterung
Structural features and environmental conditions regulating α-synuclein [alpha-synuclein] aggregation
Synuclein Family Members Prevent Membrane Damage by Counteracting α-Synuclein Aggregation
Domänenstrukturen in Phospholipidmembranen und die Toxizität von α-Synuclein [Alpha-Synuclein]
Synuclein Family Members Prevent Membrane Damage by Counteracting α-Synuclein Aggregation
Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity
α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice
Oligomerization of Lrrk controls actin severing and α-synuclein neurotoxicity in vivo
Functionalization of α-synuclein fibrils
SUMOylation modulates α-synuclein [alpha-synuclein] toxicity and fibril formation
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
Regulation des Proteins α-Synuclein [Alpha-Synuclein] während der zellulären Alterung
Structural features and environmental conditions regulating α-synuclein [alpha-synuclein] aggregation
Synuclein Family Members Prevent Membrane Damage by Counteracting α-Synuclein Aggregation
Domänenstrukturen in Phospholipidmembranen und die Toxizität von α-Synuclein [Alpha-Synuclein]