Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
2051-5960
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Anmerkungen
-
online resource.
- Erschienen in
-
Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity ; volume:5 ; number:1 ; day:10 ; month:1 ; year:2017 ; pages:1-15 ; date:12.2017
Acta Neuropathologica Communications ; 5, Heft 1 (10.1.2017), 1-15, 12.2017
- Schlagwort
-
Hirnkrankheit
Neuropsychiatrie
Nervenkrankheit
- Urheber
-
Ysselstein, Daniel
- Beteiligte Personen und Organisationen
-
Dehay, Benjamin
Costantino, Isabel M.
McCabe, George P.
Frosch, Matthew P.
George, Julia M.
Bezard, Erwan
Rochet, Jean-Christophe
SpringerLink (Online service)
- DOI
-
10.1186/s40478-016-0403-7
- URN
-
urn:nbn:de:1111-2017020812006
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
14.08.2025, 10:49 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
- Ysselstein, Daniel
- Dehay, Benjamin
- Costantino, Isabel M.
- McCabe, George P.
- Frosch, Matthew P.
- George, Julia M.
- Bezard, Erwan
- Rochet, Jean-Christophe
- SpringerLink (Online service)
Ähnliche Objekte (12)
![Structural features and environmental conditions regulating α-synuclein [alpha-synuclein] aggregation](/assets/placeholder/searchResultMediaNoDigitisedMedia.png)
Structural features and environmental conditions regulating α-synuclein [alpha-synuclein] aggregation
Synuclein Family Members Prevent Membrane Damage by Counteracting α-Synuclein Aggregation
Synuclein Family Members Prevent Membrane Damage by Counteracting α-Synuclein Aggregation
α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice
Functionalization of α-synuclein fibrils
Hyperosmotic stress induces cell-dependent aggregation of α-synuclein
Pharmacological inhibition of α-synuclein aggregation within liquid condensates
Decreased Water Mobility Contributes To Increased α‐Synuclein Aggregation **
Decreased Water Mobility Contributes To Increased α‐Synuclein Aggregation **
Induction of CNS α-synuclein pathology by fibrillar and non-amyloidogenic recombinant α-synuclein
Upregulating β-hexosaminidase activity in rodents prevents α-synuclein lipid associations and protects dopaminergic neurons from α-synuclein-mediated neurotoxicity
Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein
Structural features and environmental conditions regulating α-synuclein [alpha-synuclein] aggregation
Synuclein Family Members Prevent Membrane Damage by Counteracting α-Synuclein Aggregation
Synuclein Family Members Prevent Membrane Damage by Counteracting α-Synuclein Aggregation
α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice
Functionalization of α-synuclein fibrils
Hyperosmotic stress induces cell-dependent aggregation of α-synuclein
Pharmacological inhibition of α-synuclein aggregation within liquid condensates
Decreased Water Mobility Contributes To Increased α‐Synuclein Aggregation **
Decreased Water Mobility Contributes To Increased α‐Synuclein Aggregation **
Induction of CNS α-synuclein pathology by fibrillar and non-amyloidogenic recombinant α-synuclein
Upregulating β-hexosaminidase activity in rodents prevents α-synuclein lipid associations and protects dopaminergic neurons from α-synuclein-mediated neurotoxicity
Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein
Structural features and environmental conditions regulating α-synuclein [alpha-synuclein] aggregation
Synuclein Family Members Prevent Membrane Damage by Counteracting α-Synuclein Aggregation
Synuclein Family Members Prevent Membrane Damage by Counteracting α-Synuclein Aggregation
α-Synuclein fibril-specific nanobody reduces prion-like α-synuclein spreading in mice
Functionalization of α-synuclein fibrils
Hyperosmotic stress induces cell-dependent aggregation of α-synuclein
Pharmacological inhibition of α-synuclein aggregation within liquid condensates
Decreased Water Mobility Contributes To Increased α‐Synuclein Aggregation **
Decreased Water Mobility Contributes To Increased α‐Synuclein Aggregation **
Induction of CNS α-synuclein pathology by fibrillar and non-amyloidogenic recombinant α-synuclein
Upregulating β-hexosaminidase activity in rodents prevents α-synuclein lipid associations and protects dopaminergic neurons from α-synuclein-mediated neurotoxicity