Untersuchungen über die Effekte von Amyloid-beta und Alpha-Synuclein auf die Nervenzellfunktion bei der Alzheimer- und Parkinson-Krankheit
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Deutsch
- Notes
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München, Ludwig-Maximilians-Universität, Habilitationsschrift, 2022
- Keyword
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Nervenzelle
Parkinson-Krankheit
Amyloid
Nervendegeneration
Krankheit
Alzheimerkrankheit
- Event
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Veröffentlichung
- (where)
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München
- (who)
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Universitätsbibliothek der Ludwig-Maximilians-Universität
- (when)
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2022
- Creator
- DOI
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10.5282/edoc.29299
- URN
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urn:nbn:de:bvb:19-292990
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:37 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
- Köglsperger, Thomas
- Universitätsbibliothek der Ludwig-Maximilians-Universität
Time of origin
- 2022
Other Objects (12)
Amyloid-Beta Peptides Trigger Aggregation of Alpha-Synuclein In Vitro
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Using an NMR metabolomics approach to investigate the pathogenicity of amyloid-beta and alpha-synuclein
Entwicklung neuer Therapieansätze für die Parkinson-Krankheit in einem Alpha-Synuclein Zellmodell
Efficient characterization of multiple binding sites of small molecule imaging ligands on amyloid-beta, tau and alpha-synuclein
Characterization of the amyloid precursor α-synuclein [alpha-synuclein] by NMR spectroscopy
The effect of alpha-synuclein on amyloid plaque pathology
Toxicity of extracellular alpha-synuclein is independent of intracellular alpha-synuclein
Early Stage Alpha-Synuclein Amyloid Fibrils are Reservoirs of Membrane-Binding Species
Alpha-Synuclein aggregate formation in oligodendroglia OLN-t40 cells stably transfected with alpha-Synuclein
The Amplification of Alpha‐Synuclein Amyloid Fibrils is Suppressed under Fully Quiescent Conditions
Truncated and modified amyloid-beta species
Amyloid-Beta Peptides Trigger Aggregation of Alpha-Synuclein In Vitro
Protein Clearance Mechanisms of Alpha-Synuclein and Amyloid-Beta in Lewy Body Disorders
Using an NMR metabolomics approach to investigate the pathogenicity of amyloid-beta and alpha-synuclein
Entwicklung neuer Therapieansätze für die Parkinson-Krankheit in einem Alpha-Synuclein Zellmodell
Efficient characterization of multiple binding sites of small molecule imaging ligands on amyloid-beta, tau and alpha-synuclein
Characterization of the amyloid precursor α-synuclein [alpha-synuclein] by NMR spectroscopy
The effect of alpha-synuclein on amyloid plaque pathology
Toxicity of extracellular alpha-synuclein is independent of intracellular alpha-synuclein
Early Stage Alpha-Synuclein Amyloid Fibrils are Reservoirs of Membrane-Binding Species
Alpha-Synuclein aggregate formation in oligodendroglia OLN-t40 cells stably transfected with alpha-Synuclein
The Amplification of Alpha‐Synuclein Amyloid Fibrils is Suppressed under Fully Quiescent Conditions
Truncated and modified amyloid-beta species
Amyloid-Beta Peptides Trigger Aggregation of Alpha-Synuclein In Vitro
Protein Clearance Mechanisms of Alpha-Synuclein and Amyloid-Beta in Lewy Body Disorders
Using an NMR metabolomics approach to investigate the pathogenicity of amyloid-beta and alpha-synuclein
Entwicklung neuer Therapieansätze für die Parkinson-Krankheit in einem Alpha-Synuclein Zellmodell
Efficient characterization of multiple binding sites of small molecule imaging ligands on amyloid-beta, tau and alpha-synuclein
Characterization of the amyloid precursor α-synuclein [alpha-synuclein] by NMR spectroscopy
The effect of alpha-synuclein on amyloid plaque pathology
Toxicity of extracellular alpha-synuclein is independent of intracellular alpha-synuclein
Early Stage Alpha-Synuclein Amyloid Fibrils are Reservoirs of Membrane-Binding Species
Alpha-Synuclein aggregate formation in oligodendroglia OLN-t40 cells stably transfected with alpha-Synuclein
The Amplification of Alpha‐Synuclein Amyloid Fibrils is Suppressed under Fully Quiescent Conditions