Hochschulschrift
The amyloidogenic propensity of human proislet amyloid polypeptide in the presence of lipids
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
Dortmund, Techn. Univ., Diss., 2009
- Creator
-
Jha, Suman
- Handle
-
2003/26516
- URN
-
urn:nbn:de:hbz:290-2003/26516-7
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
25.03.2025, 1:57 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
- Jha, Suman
Other Objects (12)
Lipids and cellular membranes in amyloid diseases
The role of SORLA in islet amyloid polypeptide transport and islet amyloid deposition
Modulation of amyloid self-assembly of ß-amyloid peptide (Aß) and islet amyloid polypeptide (IAPP) via IAPP cross-amyloid interaction surface mimics
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
Systematic studies of the interaction between amyloid β-protein [beta-protein] and lipids
Systematic studies of the interaction between amyloid β-protein [beta-protein] and lipids
Zur neuroprotektiven Wirkung des „Pituitary Adenylate Cyclase-Activating Polypeptide" gegenüber toxischen Alzheimer-Amyloid-Peptiden
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]
Structural identification and quantification of β-amyloid polypeptide-ligand interactions using affinity-mass spectrometric methods
Structural characterization of recombinant fibrillar human Islet Amyloid Polypeptide by solid-state Nuclear Magnetic Resonance Spectroscopy
Gastric inhibitory polypeptide
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]
Lipids and cellular membranes in amyloid diseases
The role of SORLA in islet amyloid polypeptide transport and islet amyloid deposition
Modulation of amyloid self-assembly of ß-amyloid peptide (Aß) and islet amyloid polypeptide (IAPP) via IAPP cross-amyloid interaction surface mimics
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
Systematic studies of the interaction between amyloid β-protein [beta-protein] and lipids
Systematic studies of the interaction between amyloid β-protein [beta-protein] and lipids
Zur neuroprotektiven Wirkung des „Pituitary Adenylate Cyclase-Activating Polypeptide" gegenüber toxischen Alzheimer-Amyloid-Peptiden
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]
Structural identification and quantification of β-amyloid polypeptide-ligand interactions using affinity-mass spectrometric methods
Structural characterization of recombinant fibrillar human Islet Amyloid Polypeptide by solid-state Nuclear Magnetic Resonance Spectroscopy
Gastric inhibitory polypeptide
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]
Lipids and cellular membranes in amyloid diseases
The role of SORLA in islet amyloid polypeptide transport and islet amyloid deposition
Modulation of amyloid self-assembly of ß-amyloid peptide (Aß) and islet amyloid polypeptide (IAPP) via IAPP cross-amyloid interaction surface mimics
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
Systematic studies of the interaction between amyloid β-protein [beta-protein] and lipids
Systematic studies of the interaction between amyloid β-protein [beta-protein] and lipids
Zur neuroprotektiven Wirkung des „Pituitary Adenylate Cyclase-Activating Polypeptide" gegenüber toxischen Alzheimer-Amyloid-Peptiden
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]
Structural identification and quantification of β-amyloid polypeptide-ligand interactions using affinity-mass spectrometric methods
Structural characterization of recombinant fibrillar human Islet Amyloid Polypeptide by solid-state Nuclear Magnetic Resonance Spectroscopy
Gastric inhibitory polypeptide