- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Erschienen in
-
In: 10.1038/s41598-019-45189-w
- Ereignis
-
Veröffentlichung
- (wo)
-
Aachen
- (wer)
-
Universitätsbibliothek der RWTH Aachen
- (wann)
-
2019
- Urheber
-
Schott-Verdugo, Stephan
Müller, Lena
Claßen, Elisa
Gohlke, Holger
Groth, Georg
- DOI
-
10.18154/RWTH-2020-03300
- URN
-
urn:nbn:de:101:1-2020091706452262161568
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
25.03.2025, 13:42 MEZ
Datenpartner
Dieses Objekt wird bereitgestellt von:
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
- Schott-Verdugo, Stephan
- Müller, Lena
- Claßen, Elisa
- Gohlke, Holger
- Groth, Georg
- Universitätsbibliothek der RWTH Aachen
Entstanden
- 2019
Ähnliche Objekte (12)
Mapping the helix arrangement of the reconstituted ETR1 ethylene receptor transmembrane domain by EPR spectroscopy
Signaling through the erythropoietin receptor is promoted by dense packing of the transmembrane domain and regulated by rapid receptor internalization
Crystallisation and functional studies with ethylene receptor ETR1
Structural Model of the mIgM B-Cell Receptor Transmembrane Domain From Self-Association Molecular Dynamics Simulations
Investigation of transmembrane segment self association of erythropoietin receptor
Synthesis, characterisation and sensor-functionalisation of transmembrane β-peptides
Biochemical analysis of SNARE protein interactions : role of transmembrane domain
BLaTM: A novel method to measure transmembrane domain interactions
Biochemical analysis of SNARE protein interactions : role of transmembrane domain
The Dynamic Personality of the Amyloid Precursor Protein’s Transmembrane Domain
Molecular modeling of the transmembrane domain of envelope glycoproteins from flaviviridae viruses
The outer transmembrane domain of the Kesv channel determines its intracellular localization
Mapping the helix arrangement of the reconstituted ETR1 ethylene receptor transmembrane domain by EPR spectroscopy
Signaling through the erythropoietin receptor is promoted by dense packing of the transmembrane domain and regulated by rapid receptor internalization
Crystallisation and functional studies with ethylene receptor ETR1
Structural Model of the mIgM B-Cell Receptor Transmembrane Domain From Self-Association Molecular Dynamics Simulations
Investigation of transmembrane segment self association of erythropoietin receptor
Synthesis, characterisation and sensor-functionalisation of transmembrane β-peptides
Biochemical analysis of SNARE protein interactions : role of transmembrane domain
BLaTM: A novel method to measure transmembrane domain interactions
Biochemical analysis of SNARE protein interactions : role of transmembrane domain
The Dynamic Personality of the Amyloid Precursor Protein’s Transmembrane Domain
Molecular modeling of the transmembrane domain of envelope glycoproteins from flaviviridae viruses
The outer transmembrane domain of the Kesv channel determines its intracellular localization
Mapping the helix arrangement of the reconstituted ETR1 ethylene receptor transmembrane domain by EPR spectroscopy
Signaling through the erythropoietin receptor is promoted by dense packing of the transmembrane domain and regulated by rapid receptor internalization
Crystallisation and functional studies with ethylene receptor ETR1
Structural Model of the mIgM B-Cell Receptor Transmembrane Domain From Self-Association Molecular Dynamics Simulations
Investigation of transmembrane segment self association of erythropoietin receptor
Synthesis, characterisation and sensor-functionalisation of transmembrane β-peptides
Biochemical analysis of SNARE protein interactions : role of transmembrane domain
BLaTM: A novel method to measure transmembrane domain interactions
Biochemical analysis of SNARE protein interactions : role of transmembrane domain
The Dynamic Personality of the Amyloid Precursor Protein’s Transmembrane Domain
Molecular modeling of the transmembrane domain of envelope glycoproteins from flaviviridae viruses