Distinct Membrane Binding Properties of N- and C-terminal Domains of Escherichia coli SecA ATPase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference65 articles.
1. TARGETING AND ASSEMBLY OF PERIPLASMIC AND OUTER-MEMBRANE PROTEINS IN ESCHERICHIA COLI
2. The Sec system
3. Protein Translocation in the Three Domains of Life: Variations on a Theme
4. SecA protein is required for secretory protein translocation into E. coli membrane vesicles
5. SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli.
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3. An alternate mode of oligomerization for E. coli SecA;Scientific Reports;2017-09-18
4. Characterization of a polypeptide-binding site in the DEAD Motor of the SecA ATPase;FEBS Letters;2017-09-12
5. Dissecting structures and functions of SecA-only protein-conducting channels: ATPase, pore structure, ion channel activity, protein translocation, and interaction with SecYEG/SecDF•YajC;PLOS ONE;2017-06-02
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