Following the Path of a Twin-arginine Precursor along the TatABC Translocase of Escherichia coli
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference52 articles.
1. The Sec-independent Twin-arginine Translocation System Can Transport Both Tightly Folded and Malfolded Proteins across the Thylakoid Membrane
2. Functional Tat Transport of Unstructured, Small, Hydrophilic Proteins
3. Evidence for a dynamic and transient pathway through the TAT protein transport machinery
4. Isolation and Characterization of Bifunctional Escherichia coli TatA Mutant Proteins That Allow Efficient Tat-dependent Protein Translocation in the Absence of TatB
5. Twin Arginine Translocation (Tat)-dependent Export in the Apparent Absence of TatABC or TatA Complexes Using Modified Escherichia coli TatA Subunits That Substitute for TatB
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1. Characterization of a TatA/TatB binding site on the TatC component of the Escherichia coli twin arginine translocase;Microbiology;2023-02-15
2. Making a chink in their armor: Current and next-generation antimicrobial strategies against the bacterial cell envelope;Advances in Microbial Physiology;2023
3. Characterisation of a TatA/TatB binding site on the TatC component of theEscherichia colitwin arginine translocase;2022-12-12
4. Twin-arginine translocase component TatB performs folding quality control via a chaperone-like activity;Scientific Reports;2022-09-01
5. Twin-arginine translocase component TatB performs folding quality control via a general chaperone activity;2020-05-12
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