A potential late stage intermediate of twin-arginine dependent protein translocation in Escherichia coli
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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In: Geise, H.; Heidrich, E.S.; Nikolin, C.S.; Mehner-Breitfeld, D.; Brüser, T.: A potential late stage intermediate of twin-arginine dependent protein translocation in Escherichia coli. In: Frontiers in Microbiology 10 (2019), 1482. DOI: https://doi.org/10.3389/fmicb.2019.01482
- Event
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Veröffentlichung
- (where)
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Hannover
- (who)
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Gottfried Wilhelm Leibniz Universität Hannover
- (when)
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2019
- Event
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Veröffentlichung
- (where)
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Hannover
- (who)
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Technische Informationsbibliothek (TIB)
- (when)
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2019
- Creator
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Geise, Hendrik
Heidrich, Eyleen Sabine
Nikolin, Christoph Stefan
Mehner-Breitfeld, Denise
Brüser, Thomas
- DOI
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10.15488/5218
- URN
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urn:nbn:de:101:1-2020080810273598214702
- Rights
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Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 10:48 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.
Associated
- Geise, Hendrik
- Heidrich, Eyleen Sabine
- Nikolin, Christoph Stefan
- Mehner-Breitfeld, Denise
- Brüser, Thomas
- Gottfried Wilhelm Leibniz Universität Hannover
- Technische Informationsbibliothek (TIB)
Time of origin
- 2019
Other Objects (12)
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Characterisation of the twin-arginine protein translocation pathway of Bacillus subtilis
Twin-Arginine translocation-Arresting protein regions contact TatA and TatB
Initial assembly steps of the twin-arginine translocation signal peptide receptor complex
Oligomerization state of the functional bacterial twin-arginine translocation (Tat) receptor complex
The TatA component of the twin-arginine translocation system locally weakens the cytoplasmic membrane of Escherichia coli upon protein substrate binding
Moraxella catarrhalis uses a twin-arginine translocation system to secrete the β-lactamase BRO-2
Prediction of twin-arginine signal peptides
Pleiotropic effects of the twin-arginine translocation system on biofilm formation, colonization, and virulence in Vibrio cholerae
Die Twin-Arginine-Translokase : : Charakterisierung der Interaktionen von TatC
Metabolic engineering of Escherichia coli for enhanced arginine biosynthesis
A novel strategy for l-arginine production in engineered Escherichia coli
Characterisation of the twin-arginine protein translocation pathway of bacillus subtilis
Characterisation of the twin-arginine protein translocation pathway of Bacillus subtilis
Twin-Arginine translocation-Arresting protein regions contact TatA and TatB
Initial assembly steps of the twin-arginine translocation signal peptide receptor complex
Oligomerization state of the functional bacterial twin-arginine translocation (Tat) receptor complex
The TatA component of the twin-arginine translocation system locally weakens the cytoplasmic membrane of Escherichia coli upon protein substrate binding
Moraxella catarrhalis uses a twin-arginine translocation system to secrete the β-lactamase BRO-2
Prediction of twin-arginine signal peptides
Pleiotropic effects of the twin-arginine translocation system on biofilm formation, colonization, and virulence in Vibrio cholerae
Die Twin-Arginine-Translokase : : Charakterisierung der Interaktionen von TatC
Metabolic engineering of Escherichia coli for enhanced arginine biosynthesis
A novel strategy for l-arginine production in engineered Escherichia coli
Characterisation of the twin-arginine protein translocation pathway of bacillus subtilis
Characterisation of the twin-arginine protein translocation pathway of Bacillus subtilis
Twin-Arginine translocation-Arresting protein regions contact TatA and TatB
Initial assembly steps of the twin-arginine translocation signal peptide receptor complex
Oligomerization state of the functional bacterial twin-arginine translocation (Tat) receptor complex
The TatA component of the twin-arginine translocation system locally weakens the cytoplasmic membrane of Escherichia coli upon protein substrate binding
Moraxella catarrhalis uses a twin-arginine translocation system to secrete the β-lactamase BRO-2
Prediction of twin-arginine signal peptides
Pleiotropic effects of the twin-arginine translocation system on biofilm formation, colonization, and virulence in Vibrio cholerae
Die Twin-Arginine-Translokase : : Charakterisierung der Interaktionen von TatC
Metabolic engineering of Escherichia coli for enhanced arginine biosynthesis