Oligomerization state of the functional bacterial twin-arginine translocation (Tat) receptor complex
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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2399-3642
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
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online resource.
- Bibliographic citation
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Oligomerization state of the functional bacterial twin-arginine translocation (Tat) receptor complex ; volume:5 ; number:1 ; day:19 ; month:9 ; year:2022 ; pages:1-13 ; date:12.2022
Communications biology ; 5, Heft 1 (19.9.2022), 1-13, 12.2022
- Creator
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Sharma, Ankith
Chowdhury, Rajdeep
Musser, Siegfried M.
- Contributor
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SpringerLink (Online service)
- DOI
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10.1038/s42003-022-03952-2
- URN
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urn:nbn:de:101:1-2022120621521155994076
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:24 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
- Sharma, Ankith
- Chowdhury, Rajdeep
- Musser, Siegfried M.
- SpringerLink (Online service)
Other Objects (12)
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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
Die Twin-Arginine-Translokase : : Charakterisierung der Interaktionen von TatC
A potential late stage intermediate of twin-arginine dependent protein translocation in Escherichia coli
Moraxella catarrhalis uses a twin-arginine translocation system to secrete the β-lactamase BRO-2
The TatA component of the twin-arginine translocation system locally weakens the cytoplasmic membrane of Escherichia coli upon protein substrate binding
Prediction of twin-arginine signal peptides
Pleiotropic effects of the twin-arginine translocation system on biofilm formation, colonization, and virulence in Vibrio cholerae
Twin-arginine translocase component TatB performs folding quality control via a chaperone-like activity
The h-region of twin-arginine signal peptides supports productive binding of bacterial Tat precursor proteins to the TatBC receptor complex
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
Die Twin-Arginine-Translokase : : Charakterisierung der Interaktionen von TatC
A potential late stage intermediate of twin-arginine dependent protein translocation in Escherichia coli
Moraxella catarrhalis uses a twin-arginine translocation system to secrete the β-lactamase BRO-2
The TatA component of the twin-arginine translocation system locally weakens the cytoplasmic membrane of Escherichia coli upon protein substrate binding
Prediction of twin-arginine signal peptides
Pleiotropic effects of the twin-arginine translocation system on biofilm formation, colonization, and virulence in Vibrio cholerae
Twin-arginine translocase component TatB performs folding quality control via a chaperone-like activity
The h-region of twin-arginine signal peptides supports productive binding of bacterial Tat precursor proteins to the TatBC receptor complex
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
Die Twin-Arginine-Translokase : : Charakterisierung der Interaktionen von TatC
A potential late stage intermediate of twin-arginine dependent protein translocation in Escherichia coli
Moraxella catarrhalis uses a twin-arginine translocation system to secrete the β-lactamase BRO-2
The TatA component of the twin-arginine translocation system locally weakens the cytoplasmic membrane of Escherichia coli upon protein substrate binding
Prediction of twin-arginine signal peptides
Pleiotropic effects of the twin-arginine translocation system on biofilm formation, colonization, and virulence in Vibrio cholerae
Twin-arginine translocase component TatB performs folding quality control via a chaperone-like activity