Hochschulschrift
Understanding membrane identity, ceramide homeostasis and transport across lipid bilayers : cryo-EM of membrane proteins
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Dimensions
-
30 cm
- Extent
-
VII, 236 Seiten
- Language
-
Englisch
- Notes
-
Illustrationen, Diagramme
Kumulative Dissertation mit 7 Einzelbeiträgen
Osnabrück University, Dissertation, 2024
- Classification
-
Biowissenschaften, Biologie
- Event
-
Veröffentlichung
- (where)
-
Osnabrück
- (when)
-
April 2024
- Creator
- Contributor
- Table of contents
- Rights
-
Bei diesem Objekt liegt nur das Inhaltsverzeichnis digital vor. Der Zugriff darauf ist unbeschränkt möglich.
- Last update
-
08.06.2022, 2:26 PM 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
Time of origin
- April 2024
Other Objects (12)
CryoEM reveals how the complement membrane attack complex ruptures lipid bilayers
Cryo-EM structures of the membrane repair protein dysferlin
Single-particle cryo-EM structures of oligomeric membrane protein complexes
Structural investigation of druggable membrane proteins via SPA cryo-EM
Structural characterization of membrane protein complexes by single-particle cryo-EM
Cryo-EM architecture of a near-native stretch-sensitive membrane microdomain
Cryo-EM studies of tubular membrane shaping by the N-BAR protein amphiphysin
Cryo-EM analysis of mammalian co-translational membrane protein insertion and N-linked glycosylation
CryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin
LipIDens: simulation assisted interpretation of lipid densities in cryo-EM structures of membrane proteins
Cryo-EM elucidates the uroplakin complex structure within liquid-crystalline lipids in the porcine urothelial membrane
Creating supported plasma membrane bilayers using acoustic pressure
CryoEM reveals how the complement membrane attack complex ruptures lipid bilayers
Cryo-EM structures of the membrane repair protein dysferlin
Single-particle cryo-EM structures of oligomeric membrane protein complexes
Structural investigation of druggable membrane proteins via SPA cryo-EM
Structural characterization of membrane protein complexes by single-particle cryo-EM
Cryo-EM architecture of a near-native stretch-sensitive membrane microdomain
Cryo-EM studies of tubular membrane shaping by the N-BAR protein amphiphysin
Cryo-EM analysis of mammalian co-translational membrane protein insertion and N-linked glycosylation
CryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin
LipIDens: simulation assisted interpretation of lipid densities in cryo-EM structures of membrane proteins
Cryo-EM elucidates the uroplakin complex structure within liquid-crystalline lipids in the porcine urothelial membrane
Creating supported plasma membrane bilayers using acoustic pressure
CryoEM reveals how the complement membrane attack complex ruptures lipid bilayers
Cryo-EM structures of the membrane repair protein dysferlin
Single-particle cryo-EM structures of oligomeric membrane protein complexes
Structural investigation of druggable membrane proteins via SPA cryo-EM
Structural characterization of membrane protein complexes by single-particle cryo-EM
Cryo-EM architecture of a near-native stretch-sensitive membrane microdomain
Cryo-EM studies of tubular membrane shaping by the N-BAR protein amphiphysin
Cryo-EM analysis of mammalian co-translational membrane protein insertion and N-linked glycosylation
CryoEM structures of membrane pore and prepore complex reveal cytolytic mechanism of Pneumolysin
LipIDens: simulation assisted interpretation of lipid densities in cryo-EM structures of membrane proteins
Cryo-EM elucidates the uroplakin complex structure within liquid-crystalline lipids in the porcine urothelial membrane