α-Synuclein interacts directly but reversibly with psychosine: implications for α-synucleinopathies
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
2045-2322
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
online resource.
- Bibliographic citation
-
α-Synuclein interacts directly but reversibly with psychosine: implications for α-synucleinopathies ; volume:8 ; number:1 ; day:20 ; month:8 ; year:2018 ; pages:1-19 ; date:12.2018
Scientific reports ; 8, Heft 1 (20.8.2018), 1-19, 12.2018
- Creator
-
Abdelkarim, Hazem
- Contributor
-
Marshall, Michael S.
Scesa, Giuseppe
Smith, Rachael A.
Rue, Emily
Marshall, Jeffrey
Elackattu, Vince
Stoskute, Monika
Issa, Yazan
Santos, Marta
Nguyen, Duc
Hauck, Zane
van Breemen, Richard
Celej, Maria S.
Gaponenko, Vadim
Bongarzone, Ernesto R.
SpringerLink (Online service)
- DOI
-
10.1038/s41598-018-30808-9
- URN
-
urn:nbn:de:101:1-2018101200054421565814
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.20252025, 7:35 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Abdelkarim, Hazem
- Marshall, Michael S.
- Scesa, Giuseppe
- Smith, Rachael A.
- Rue, Emily
- Marshall, Jeffrey
- Elackattu, Vince
- Stoskute, Monika
- Issa, Yazan
- Santos, Marta
- Nguyen, Duc
- Hauck, Zane
- van Breemen, Richard
- Celej, Maria S.
- Gaponenko, Vadim
- Bongarzone, Ernesto R.
- SpringerLink (Online service)
Other Objects (12)
α-Synuclein Interacts with Lipoproteins in Plasma
Aplp1 interacts with Lag3 to facilitate transmission of pathologic α-synuclein
Author Correction: Aplp1 interacts with Lag3 to facilitate transmission of pathologic α-synuclein
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
Overexpression-Induced α-Synuclein Brain Spreading
α-Synuclein and neuronal cell death
SUMOylation modulates α-synuclein [alpha-synuclein] toxicity and fibril formation
Charakterisierung der α-Synuclein Oligomerisation in Synucleinopathien
α-Synuclein Interacts with Lipoproteins in Plasma
Aplp1 interacts with Lag3 to facilitate transmission of pathologic α-synuclein
Author Correction: Aplp1 interacts with Lag3 to facilitate transmission of pathologic α-synuclein
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
Overexpression-Induced α-Synuclein Brain Spreading
α-Synuclein and neuronal cell death
SUMOylation modulates α-synuclein [alpha-synuclein] toxicity and fibril formation
Charakterisierung der α-Synuclein Oligomerisation in Synucleinopathien
α-Synuclein Interacts with Lipoproteins in Plasma
Aplp1 interacts with Lag3 to facilitate transmission of pathologic α-synuclein
Author Correction: Aplp1 interacts with Lag3 to facilitate transmission of pathologic α-synuclein
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
Overexpression-Induced α-Synuclein Brain Spreading
α-Synuclein and neuronal cell death
SUMOylation modulates α-synuclein [alpha-synuclein] toxicity and fibril formation