TatB and TatC Form a Functional and Structural Unit of the Twin-arginine Translocase from Escherichia coli
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference17 articles.
1. Escherichia coli translocase: the unravelling of a molecular machine
2. Protein translocation into and across the bacterial plasma membrane and the plant thylakoid membrane
3. A new type of signal peptide: central role of a twin-arginine motif in transfer signals for the delta pH-dependent thylakoidal protein translocase.
4. A common export pathway for proteins binding complex redox cofactors?
5. Overlapping functions of components of a bacterial Sec-independent protein export pathway
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1. Preparation of Uniformly Oriented Inverted Inner (Cytoplasmic) Membrane Vesicles from Gram-Negative Bacterial Cells;Methods in Molecular Biology;2023-11-07
2. Cell-penetrating peptides stimulate protein transport on the Twin-arginine translocation pathway: evidence for a membrane thinning and toroidal pore mechanism;2023-07-09
3. Characterization of a TatA/TatB binding site on the TatC component of the Escherichia coli twin arginine translocase;Microbiology;2023-02-15
4. Characterisation of a TatA/TatB binding site on the TatC component of theEscherichia colitwin arginine translocase;2022-12-12
5. New insights into the Tat protein transport cycle from characterizing the assembled Tat translocon;Molecular Microbiology;2022-10-05
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