Hochschulschrift
Early conformational changes control spontaneous polyQ-mediated huntingtin polymerization
- Alternative title
-
Frühe Konformationsänderungen kontrollieren die spontane polyQ-vermittelte Huntingtin Aggregation
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
Berlin, Freie Universität Berlin, Diss., 2012
- Keyword
-
Histologie
Cytologie
- Event
-
Veröffentlichung
- (where)
-
Berlin
- (who)
-
Freie Universität Berlin
- (when)
-
2012
- Creator
-
Wagner, Anne Sophie
- URN
-
urn:nbn:de:kobv:188-fudissthesis000000037661-8
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:32 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.
Object type
- Hochschulschrift
Associated
- Wagner, Anne Sophie
- Freie Universität Berlin
Time of origin
- 2012
Other Objects (12)
Early conformational changes control spontaneous polyQ-mediated huntingtin polymerization
Conformational dynamics and aggregation of Huntingtin Exon 1 in living cells
Nucleation of Huntingtin Aggregation Proceeds via Conformational Conversion of Pre‐Formed, Sparsely‐Populated Tetramers
Huntingtin assoziierte Proteine
Huntingtin Lowering Strategies
Tuning Aqueous Supramolecular Polymerization by an Acid‐Responsive Conformational Switch
Stereoregular Functionalized Poly(dienes) from Catalytic Polymerization
The protein SS18L1 is a potent suppressor of polyQmediated huntingtin aggregation and toxicity
Pathological polyQ expansion does not alter the conformation of the Huntingtin-HAP40 complex
Renewable resource-based poly(dodecyloate) by carbonylation polymerization
Amyloid modifier SERF1a interacts with polyQ-expanded huntingtin-exon 1 via helical interactions and exacerbates polyQ-induced toxicity
The protein SS18L1 is a potent suppressor of polyQ-mediated huntingtin aggregation and toxicity
Early conformational changes control spontaneous polyQ-mediated huntingtin polymerization
Conformational dynamics and aggregation of Huntingtin Exon 1 in living cells
Nucleation of Huntingtin Aggregation Proceeds via Conformational Conversion of Pre‐Formed, Sparsely‐Populated Tetramers
Huntingtin assoziierte Proteine
Huntingtin Lowering Strategies
Tuning Aqueous Supramolecular Polymerization by an Acid‐Responsive Conformational Switch
Stereoregular Functionalized Poly(dienes) from Catalytic Polymerization
The protein SS18L1 is a potent suppressor of polyQmediated huntingtin aggregation and toxicity
Pathological polyQ expansion does not alter the conformation of the Huntingtin-HAP40 complex
Renewable resource-based poly(dodecyloate) by carbonylation polymerization
Amyloid modifier SERF1a interacts with polyQ-expanded huntingtin-exon 1 via helical interactions and exacerbates polyQ-induced toxicity
The protein SS18L1 is a potent suppressor of polyQ-mediated huntingtin aggregation and toxicity
Early conformational changes control spontaneous polyQ-mediated huntingtin polymerization
Conformational dynamics and aggregation of Huntingtin Exon 1 in living cells
Nucleation of Huntingtin Aggregation Proceeds via Conformational Conversion of Pre‐Formed, Sparsely‐Populated Tetramers
Huntingtin assoziierte Proteine
Huntingtin Lowering Strategies
Tuning Aqueous Supramolecular Polymerization by an Acid‐Responsive Conformational Switch
Stereoregular Functionalized Poly(dienes) from Catalytic Polymerization
The protein SS18L1 is a potent suppressor of polyQmediated huntingtin aggregation and toxicity
Pathological polyQ expansion does not alter the conformation of the Huntingtin-HAP40 complex
Renewable resource-based poly(dodecyloate) by carbonylation polymerization
Amyloid modifier SERF1a interacts with polyQ-expanded huntingtin-exon 1 via helical interactions and exacerbates polyQ-induced toxicity