SecA insertion into phospholipids is stimulated by negatively charged lipids and inhibited by ATP: a monolayer study
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00119a021
Reference33 articles.
1. SecA interacts with secretory proteins by recognizing the positive charge at the amino terminus of the signal peptide in Escherichia coli.
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3. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
4. The enzymatic synthesis of phosphatidylserine and purification by CM-cellulose column chromatography
5. SecA protein, a peripheral protein of the Escherichia coli plasma membrane, is essential for the functional binding and translocation of proOmpA.
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