Characterization of the molecular interaction between α-synuclein and prion protein
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Portugiesisch
- Notes
-
Göttingen, Georg-August Universität, Dissertation, 2023
- Keyword
-
Wechselwirkung
Prionprotein
Proteine
Prion
Pathogenität
Protein-Protein-Wechselwirkung
- Event
-
Veröffentlichung
- (where)
-
Göttingen
- (who)
-
Niedersächsische Staats- und Universitätsbibliothek Göttingen
- (when)
-
2024
- Creator
- Contributor
-
Outeiro, Tiago Fleming
Zweckstetter, Markus
Rizzoli, Silvio O.
Fernandez, Claudio
- URN
-
urn:nbn:de:gbv:7-ediss-15177-5
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
14.08.2025, 11:00 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
- Garcia Domingues, Renato
- Outeiro, Tiago Fleming
- Zweckstetter, Markus
- Rizzoli, Silvio O.
- Fernandez, Claudio
- Niedersächsische Staats- und Universitätsbibliothek Göttingen
Time of origin
- 2024
Other Objects (12)
The interplay between α-synuclein and Rab GTPases: Insights into the molecular basis of synucleinopathies
The Molecular Basis of the Interaction of Cyclophilin A with α‐Synuclein
The Molecular Basis of the Interaction of Cyclophilin A with α‐Synuclein
α-synuclein disrupts neuron network rhythmic activity when overexpressed in cultured neurons
Chicago sky blue 6B inhibits α-synuclein aggregation and propagation
Extending the applicability of P3D for structure determination of small molecules
Extending the applicability of P3D for structure determination of small molecules
Structural characterization of alpha-synuclein aggregates seeded by patient material
Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein
Modulating the aggregation of alpha-synuclein and prion protein with small molecules.
Analysis of the mechanisms of interaction of alpha-synuclein and membranes in cellular models of Parkinson´s Disease
Genetic and Pharmacological Modulation of Alpha-Synuclein Aggregation
The interplay between α-synuclein and Rab GTPases: Insights into the molecular basis of synucleinopathies
The Molecular Basis of the Interaction of Cyclophilin A with α‐Synuclein
The Molecular Basis of the Interaction of Cyclophilin A with α‐Synuclein
α-synuclein disrupts neuron network rhythmic activity when overexpressed in cultured neurons
Chicago sky blue 6B inhibits α-synuclein aggregation and propagation
Extending the applicability of P3D for structure determination of small molecules
Extending the applicability of P3D for structure determination of small molecules
Structural characterization of alpha-synuclein aggregates seeded by patient material
Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein
Modulating the aggregation of alpha-synuclein and prion protein with small molecules.
Analysis of the mechanisms of interaction of alpha-synuclein and membranes in cellular models of Parkinson´s Disease
Genetic and Pharmacological Modulation of Alpha-Synuclein Aggregation
The interplay between α-synuclein and Rab GTPases: Insights into the molecular basis of synucleinopathies
The Molecular Basis of the Interaction of Cyclophilin A with α‐Synuclein
The Molecular Basis of the Interaction of Cyclophilin A with α‐Synuclein
α-synuclein disrupts neuron network rhythmic activity when overexpressed in cultured neurons
Chicago sky blue 6B inhibits α-synuclein aggregation and propagation
Extending the applicability of P3D for structure determination of small molecules
Extending the applicability of P3D for structure determination of small molecules
Structural characterization of alpha-synuclein aggregates seeded by patient material
Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein
Modulating the aggregation of alpha-synuclein and prion protein with small molecules.
Analysis of the mechanisms of interaction of alpha-synuclein and membranes in cellular models of Parkinson´s Disease