Hochschulschrift
Identification of sequences of the interaction interface of β-amyloid peptide (Aβ) and islet amyloid polypeptide (IAPP) and synthesis and characterization of IAPP-derived inhibitors of Aβ aggregation
- Alternative title
-
Identifizierung von Sequenzen der Interaktionsdomänen des β-Amyloidpeptids (Aβ) und des Inselamyloid Polypeptids (IAPP) und Synthese und Charakterisierung von IAPP-Analoga als Inhibitoren der Aβ-Aggregation
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
München, Technische Universität München, Diss., 2011
- Keyword
-
Augenheilkunde
Augenkrankheit
- Event
-
Veröffentlichung
- (where)
-
München
- (who)
-
Universitätsbibliothek der TU München
- (when)
-
2011
- Creator
- Contributor
- URN
-
urn:nbn:de:bvb:91-diss-20111128-1091456-1-9
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
25.03.2025, 1:44 PM CET
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
- Andreetto, Erika
- Kapurniotu, Aphrodite
- Kessler, Horst
- Universitätsbibliothek der TU München
Time of origin
- 2011
Other Objects (12)
Modulation of amyloid self-assembly of ß-amyloid peptide (Aß) and islet amyloid polypeptide (IAPP) via IAPP cross-amyloid interaction surface mimics
The role of SORLA in islet amyloid polypeptide transport and islet amyloid deposition
Identification of key residues of the cross-interaction of islet amyloid polypeptide (IAPP) with β-amyloid peptide (Aβ), its amyloid self-assembly and its bioactivity
Identification of sequences of the interaction interface β-amyloid peptide [beta-amyloid peptide] Aβ [Abeta] and islet amyloid polypeptide (IAPP) and synthesis and characterization of IAPP-derived inhibitors of Aβ aggregation [Abeta aggregation]
Identification and characterization of IAPP derived inhibitors of cytotoxic self-assembly and amyloidogenesis of islet amyloid polypeptide (IAPP) and ß-amyloid [beta amyloid] peptide (Aß) [A beta]
Proinflammatory aspects of advanced glycaton endproducts (AGEs) and amyloid-β [amyloid-beta] [(Aβ)]
Folding and aggregation of amyloid peptides
Characterization of novel Amyloid-β [Amyloid-beta] peptide (Aβ) [Abeta] binding ligands
The amyloidogenic propensity of human proislet amyloid polypeptide in the presence of lipids
Investigation of oligomerization of amyloid-β and prion protein
Influence of process factors on the formation and fragmentation of amyloid and amyloid-like aggregates from beta-lactoglobulin
Structural identification and quantification of β-amyloid polypeptide-ligand interactions using affinity-mass spectrometric methods
Modulation of amyloid self-assembly of ß-amyloid peptide (Aß) and islet amyloid polypeptide (IAPP) via IAPP cross-amyloid interaction surface mimics
The role of SORLA in islet amyloid polypeptide transport and islet amyloid deposition
Identification of key residues of the cross-interaction of islet amyloid polypeptide (IAPP) with β-amyloid peptide (Aβ), its amyloid self-assembly and its bioactivity
Identification of sequences of the interaction interface β-amyloid peptide [beta-amyloid peptide] Aβ [Abeta] and islet amyloid polypeptide (IAPP) and synthesis and characterization of IAPP-derived inhibitors of Aβ aggregation [Abeta aggregation]
Identification and characterization of IAPP derived inhibitors of cytotoxic self-assembly and amyloidogenesis of islet amyloid polypeptide (IAPP) and ß-amyloid [beta amyloid] peptide (Aß) [A beta]
Proinflammatory aspects of advanced glycaton endproducts (AGEs) and amyloid-β [amyloid-beta] [(Aβ)]
Folding and aggregation of amyloid peptides
Characterization of novel Amyloid-β [Amyloid-beta] peptide (Aβ) [Abeta] binding ligands
The amyloidogenic propensity of human proislet amyloid polypeptide in the presence of lipids
Investigation of oligomerization of amyloid-β and prion protein
Influence of process factors on the formation and fragmentation of amyloid and amyloid-like aggregates from beta-lactoglobulin
Structural identification and quantification of β-amyloid polypeptide-ligand interactions using affinity-mass spectrometric methods
Modulation of amyloid self-assembly of ß-amyloid peptide (Aß) and islet amyloid polypeptide (IAPP) via IAPP cross-amyloid interaction surface mimics
The role of SORLA in islet amyloid polypeptide transport and islet amyloid deposition
Identification of key residues of the cross-interaction of islet amyloid polypeptide (IAPP) with β-amyloid peptide (Aβ), its amyloid self-assembly and its bioactivity
Identification of sequences of the interaction interface β-amyloid peptide [beta-amyloid peptide] Aβ [Abeta] and islet amyloid polypeptide (IAPP) and synthesis and characterization of IAPP-derived inhibitors of Aβ aggregation [Abeta aggregation]
Identification and characterization of IAPP derived inhibitors of cytotoxic self-assembly and amyloidogenesis of islet amyloid polypeptide (IAPP) and ß-amyloid [beta amyloid] peptide (Aß) [A beta]
Proinflammatory aspects of advanced glycaton endproducts (AGEs) and amyloid-β [amyloid-beta] [(Aβ)]
Folding and aggregation of amyloid peptides
Characterization of novel Amyloid-β [Amyloid-beta] peptide (Aβ) [Abeta] binding ligands
The amyloidogenic propensity of human proislet amyloid polypeptide in the presence of lipids
Investigation of oligomerization of amyloid-β and prion protein
Influence of process factors on the formation and fragmentation of amyloid and amyloid-like aggregates from beta-lactoglobulin