Hochschulschrift
Einsatz von Fret-Flim zur Beobachtung von Protein-Protein_Wechselwirkungen in lebenden Zellen: Einblicke in Interaktionen des präsynaptischen Proteins Bassoon : = Investigating protein-protein interactions by fret-flim in living cells: mediated by the presynaptic proteins bassoon
- Alternative title
-
Investigating protein-protein interactions by fret-flim in living cells: mediated by the presynaptic proteins bassoon
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
Magdeburg, Univ., Diss., 2007
- Keyword
-
Biochemische Analyse
Nerv
Nervenfaser
Peripherer Nerv
Zelle
Cytologie
Eukaryoten
Protoplasma
Eukaryontische Zelle
- Creator
- URN
-
urn:nbn:de:101:1-201010182099
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
14.08.2025, 10:54 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
Other Objects (12)
Protein–Protein Affinity Determination by Quantitative FRET Quenching
Interactions of the adaptor proteins AP2 and 14-3-3 with the presynaptic scaffolding protein Bassoon
Examining the role of the presynaptic cytomatrix protein bassoon in cone photoreceptor degeneration in bassoon-deficient mouse lines
Action-FRET of a Gaseous Protein
Single‐Molecule FRET of Membrane Transport Proteins
Development of Two-Hybrid FRET applications to investigate endolysosomal protein-protein interactions
A quantitative FRET approach to characterize protein-protein interactions in living cells
Orientation and organization of the presynaptic active zone protein Bassoon: from the Golgi to the synapse
Nanoscopical Analysis Reveals an Orderly Arrangement of the Presynaptic Scaffold Protein Bassoon at the Golgi-Apparatus
Conformational changes of proteins involved in the chaperone mediated protein folding cycle measured by spFRET
FRET Dyes Significantly Affect SAXS Intensities of Proteins
Towards improved FRET-derived biophysical models of proteins
Protein–Protein Affinity Determination by Quantitative FRET Quenching
Interactions of the adaptor proteins AP2 and 14-3-3 with the presynaptic scaffolding protein Bassoon
Examining the role of the presynaptic cytomatrix protein bassoon in cone photoreceptor degeneration in bassoon-deficient mouse lines
Action-FRET of a Gaseous Protein
Single‐Molecule FRET of Membrane Transport Proteins
Development of Two-Hybrid FRET applications to investigate endolysosomal protein-protein interactions
A quantitative FRET approach to characterize protein-protein interactions in living cells
Orientation and organization of the presynaptic active zone protein Bassoon: from the Golgi to the synapse
Nanoscopical Analysis Reveals an Orderly Arrangement of the Presynaptic Scaffold Protein Bassoon at the Golgi-Apparatus
Conformational changes of proteins involved in the chaperone mediated protein folding cycle measured by spFRET
FRET Dyes Significantly Affect SAXS Intensities of Proteins
Towards improved FRET-derived biophysical models of proteins
Protein–Protein Affinity Determination by Quantitative FRET Quenching
Interactions of the adaptor proteins AP2 and 14-3-3 with the presynaptic scaffolding protein Bassoon
Examining the role of the presynaptic cytomatrix protein bassoon in cone photoreceptor degeneration in bassoon-deficient mouse lines
Action-FRET of a Gaseous Protein
Single‐Molecule FRET of Membrane Transport Proteins
Development of Two-Hybrid FRET applications to investigate endolysosomal protein-protein interactions
A quantitative FRET approach to characterize protein-protein interactions in living cells
Orientation and organization of the presynaptic active zone protein Bassoon: from the Golgi to the synapse
Nanoscopical Analysis Reveals an Orderly Arrangement of the Presynaptic Scaffold Protein Bassoon at the Golgi-Apparatus
Conformational changes of proteins involved in the chaperone mediated protein folding cycle measured by spFRET
FRET Dyes Significantly Affect SAXS Intensities of Proteins