- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Bibliographic citation
-
In: Taubert, J.; Brüser, T.: Twin-Arginine translocation-Arresting protein regions contact TatA and TatB. In: Biological Chemistry 395 (2014), S. 827-836. DOI: https://doi.org/10.1515/hsz-2014-0170
- Event
-
Veröffentlichung
- (where)
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Hannover, Hannover
- (who)
-
Gottfried Wilhelm Leibniz Universität Hannover, Technische Informationsbibliothek (TIB)
- (when)
-
2014
- DOI
-
10.15488/3162
- URN
-
urn:nbn:de:101:1-2020062307090546469460
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
25.03.2025, 1:43 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.
Associated
- Gottfried Wilhelm Leibniz Universität Hannover, Technische Informationsbibliothek (TIB)
Time of origin
- 2014
Other Objects (12)
The TatA component of the twin-arginine translocation system locally weakens the cytoplasmic membrane of Escherichia coli upon protein substrate binding
Die Twin-Arginine-Translokase : : Charakterisierung der Interaktionen von TatC
Characterisation of the twin-arginine protein translocation pathway of Bacillus subtilis
Characterisation of the twin-arginine protein translocation pathway of bacillus subtilis
Initial assembly steps of the twin-arginine translocation signal peptide receptor complex
The Tat-dependent protein translocation pathway
A potential late stage intermediate of twin-arginine dependent protein translocation in Escherichia coli
The h-region of twin-arginine signal peptides supports productive binding of bacterial Tat precursor proteins to the TatBC receptor complex
TatE is a regular constituent of the bacterial Tat translocase and mediates TatA oligomerization
Neue Einblicke in die Rolle des Membranproteins TatA bei der Tat-abhängigen Proteintranslokation
Structural features of the TatC membrane protein that determine docking and insertion of a twin-arginine signal peptide
Mobility and translocation of TAT peptides in model membranes
The TatA component of the twin-arginine translocation system locally weakens the cytoplasmic membrane of Escherichia coli upon protein substrate binding
Die Twin-Arginine-Translokase : : Charakterisierung der Interaktionen von TatC
Characterisation of the twin-arginine protein translocation pathway of Bacillus subtilis
Characterisation of the twin-arginine protein translocation pathway of bacillus subtilis
Initial assembly steps of the twin-arginine translocation signal peptide receptor complex
The Tat-dependent protein translocation pathway
A potential late stage intermediate of twin-arginine dependent protein translocation in Escherichia coli
The h-region of twin-arginine signal peptides supports productive binding of bacterial Tat precursor proteins to the TatBC receptor complex
TatE is a regular constituent of the bacterial Tat translocase and mediates TatA oligomerization
Neue Einblicke in die Rolle des Membranproteins TatA bei der Tat-abhängigen Proteintranslokation
Structural features of the TatC membrane protein that determine docking and insertion of a twin-arginine signal peptide
Mobility and translocation of TAT peptides in model membranes
The TatA component of the twin-arginine translocation system locally weakens the cytoplasmic membrane of Escherichia coli upon protein substrate binding
Die Twin-Arginine-Translokase : : Charakterisierung der Interaktionen von TatC
Characterisation of the twin-arginine protein translocation pathway of Bacillus subtilis
Characterisation of the twin-arginine protein translocation pathway of bacillus subtilis
Initial assembly steps of the twin-arginine translocation signal peptide receptor complex
The Tat-dependent protein translocation pathway
A potential late stage intermediate of twin-arginine dependent protein translocation in Escherichia coli
The h-region of twin-arginine signal peptides supports productive binding of bacterial Tat precursor proteins to the TatBC receptor complex
TatE is a regular constituent of the bacterial Tat translocase and mediates TatA oligomerization
Neue Einblicke in die Rolle des Membranproteins TatA bei der Tat-abhängigen Proteintranslokation
Structural features of the TatC membrane protein that determine docking and insertion of a twin-arginine signal peptide