The TatA component of the twin-arginine translocation system locally weakens the cytoplasmic membrane of Escherichia coli upon protein substrate binding
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Erschienen in
-
In: Hou, B.; Heidrich, E.S.; Mehner-Breitfeld, D.; Brüser, T.: The TatA component of the twin-arginine translocation system locally weakens the cytoplasmic membrane of Escherichia coli upon protein substrate binding. In: The journal of biological chemistry : JBC 293 (2018), Nr. 20, S. 7592-7605. DOI: https://doi.org/10.1074/jbc.RA118.002205
- Ereignis
-
Veröffentlichung
- (wo)
-
Hannover
- (wer)
-
Gottfried Wilhelm Leibniz Universität Hannover
- (wann)
-
2018
- Ereignis
-
Veröffentlichung
- (wo)
-
Hannover
- (wer)
-
Technische Informationsbibliothek (TIB)
- (wann)
-
2018
- Urheber
-
Hou, Bou
Heidrich, Eyleen S.
Mehner-Breitfeld, Denise
Brüser, Thomas
- DOI
-
10.15488/11113
- URN
-
urn:nbn:de:101:1-2021080502154914295810
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
14.08.2025, 11:00 MESZ
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
- Hou, Bou
- Heidrich, Eyleen S.
- Mehner-Breitfeld, Denise
- Brüser, Thomas
- Gottfried Wilhelm Leibniz Universität Hannover
- Technische Informationsbibliothek (TIB)
Entstanden
- 2018
Ähnliche Objekte (12)
Twin-Arginine translocation-Arresting protein regions contact TatA and TatB
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
Oligomerization state of the functional bacterial twin-arginine translocation (Tat) receptor complex
Nuclear translocation of the cytoplasmic domain of HB-EGF induces gastric cancer invasion
HMGB1 cytoplasmic translocation in patients with acute liver failure
Moraxella catarrhalis uses a twin-arginine translocation system to secrete the β-lactamase BRO-2
Tata vulgo Dotis (Tata, Totis)
Tata
"Tata"
Tata
Twin-Arginine translocation-Arresting protein regions contact TatA and TatB
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
Oligomerization state of the functional bacterial twin-arginine translocation (Tat) receptor complex
Nuclear translocation of the cytoplasmic domain of HB-EGF induces gastric cancer invasion
HMGB1 cytoplasmic translocation in patients with acute liver failure
Moraxella catarrhalis uses a twin-arginine translocation system to secrete the β-lactamase BRO-2
Tata vulgo Dotis (Tata, Totis)
Tata
"Tata"
Tata
Twin-Arginine translocation-Arresting protein regions contact TatA and TatB
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
Oligomerization state of the functional bacterial twin-arginine translocation (Tat) receptor complex
Nuclear translocation of the cytoplasmic domain of HB-EGF induces gastric cancer invasion
HMGB1 cytoplasmic translocation in patients with acute liver failure
Moraxella catarrhalis uses a twin-arginine translocation system to secrete the β-lactamase BRO-2
Tata vulgo Dotis (Tata, Totis)
Tata
"Tata"