Twin-arginine translocase mutations that suppress folding quality control and permit export of misfolded substrate proteins
Author:
Publisher
Proceedings of the National Academy of Sciences
Subject
Multidisciplinary
Reference32 articles.
1. The Bacterial Twin-Arginine Translocation Pathway
2. The Tat pathway in bacteria and chloroplasts (Review)
3. Folding quality control in the export of proteins by the bacterial twin-arginine translocation pathway
4. Transport of cytochrome c derivatives by the bacterial Tat protein translocation system
5. Genetic selection for protein solubility enabled by the folding quality control feature of the twin-arginine translocation pathway
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1. Twin-arginine translocase component TatB performs folding quality control via a chaperone-like activity;Scientific Reports;2022-09-01
2. Engineering a Supersecreting Strain of Escherichia coli by Directed Coevolution of the Multiprotein Tat Translocation Machinery;ACS Synthetic Biology;2021-11-10
3. TAR RNA Mediated Folding of a Single-Arginine-Mutant HIV-1 Tat Protein within HeLa Cells Experiencing Intracellular Crowding;International Journal of Molecular Sciences;2021-09-16
4. Engineering a super-secreting strain of Escherichia coli by directed co-evolution of the multiprotein Tat translocation machinery;2021-04-26
5. Twin-arginine translocase component TatB performs folding quality control via a general chaperone activity;2020-05-12
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