Direct Demonstration of ATP-dependent Release of SecA from a Translocating Preprotein by Surface Plasmon Resonance
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference42 articles.
1. SecA protein is required for secretory protein translocation into E. coli membrane vesicles
2. Escherichia coli translocase: the unravelling of a molecular machine
3. SecA, an essential component of the secretory machinery of Escherichiacoli, exists as homodimer
4. SecA, the peripheral subunit of the Escherichia coli precursor protein translocase, is functional as a dimer
5. Reconstitution of an efficient protein translocation machinery comprising SecA and the three membrane proteins, SecY, SecE, and SecG (p12).
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1. Structural basis of SecA-mediated protein translocation;Proceedings of the National Academy of Sciences;2023-01-04
2. Atomic Force Microscopy Reveals Complexity Underlying General Secretory System Activity;International Journal of Molecular Sciences;2022-12-20
3. Trigger factor is a bona fide secretory pathway chaperone that interacts with SecB and the translocase;EMBO reports;2020-04-19
4. Interaction of the motor protein SecA and the bacterial protein translocation channel SecYEG in the absence of ATP;Nanoscale Advances;2020
5. Interaction of the Motor Protein SecA and the Bacterial Protein Translocation Channel SecYEG in the Absence of ATP;2019-10-11
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