Characterization of the molecular interaction between α-synuclein and prion protein
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
-
Online-Ressource
- Sprache
-
Portugiesisch
- Anmerkungen
-
Göttingen, Georg-August Universität, Dissertation, 2023
- Schlagwort
-
Wechselwirkung
Prionprotein
Proteine
Prion
Pathogenität
Protein-Protein-Wechselwirkung
- Ereignis
-
Veröffentlichung
- (wo)
-
Göttingen
- (wer)
-
Niedersächsische Staats- und Universitätsbibliothek Göttingen
- (wann)
-
2024
- Urheber
- Beteiligte Personen und Organisationen
-
Outeiro, Tiago Fleming
Zweckstetter, Markus
Rizzoli, Silvio O.
Fernandez, Claudio
- URN
-
urn:nbn:de:gbv:7-ediss-15177-5
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
19.04.2025, 07:58 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
- Garcia Domingues, Renato
- Outeiro, Tiago Fleming
- Zweckstetter, Markus
- Rizzoli, Silvio O.
- Fernandez, Claudio
- Niedersächsische Staats- und Universitätsbibliothek Göttingen
Entstanden
- 2024
Ähnliche Objekte (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