Signal peptides: exquisitely designed transport promoters
Author:
Publisher
Wiley
Subject
Molecular Biology,Microbiology
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1365-2958.1994.tb00469.x/fullpdf
Reference104 articles.
1. SecA interacts with secretory proteins by recognizing the positive charge at the amino terminus of the signal peptide in Escherichia coli.
2. Predicted secondary structures of amino-terminal extension sequences of secreted proteins
3. Intragenic suppressor mutations that restore export of maltose binding protein with a truncated signal peptide
4. Synthesis of precursor maltose-binding protein with proline in the +1 position of the cleavage site interferes with the activity of Escherichia coli signal peptidase I in vivo.
5. Characterization of the interfacial behavior and structure of the signal sequence of Escherichia coli outer membrane pore protein PhoE.
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