Increased production of periplasmic proteins in Escherichia coli by directed evolution of the translation initiation region | Microbial Cell Factories | Full Text
Frontiers | Enhancing Recombinant Protein Yields in the E. coli Periplasm by Combining Signal Peptide and Production Rate Screening
Secretory and extracellular production of recombinant proteins using Escherichia coli
Systematic Screening of Optimal Signal Peptides for Secretory Production of Heterologous Proteins in Bacillus subtilis | Journal of Agricultural and Food Chemistry
Addgene: pDJSVT87
Frontiers | Strategies to Enhance Periplasmic Recombinant Protein Production Yields in Escherichia coli
Efficient function of signal peptidase 1 of Escherichia coli is partly determined by residues in the mature N-terminus of exported proteins - ScienceDirect
The targeting pathway of Escherichia coli presecretory and integral membrane proteins is specified by the hydrophobicity of the targeting signal | PNAS
Figure 1.1 from Studies on E. coli membrane protein biogenesis: Mechanism of signal peptide peptidase A and the influence of YidC depletion on cellular processes | Semantic Scholar
OmpA signal peptide leads to heterogenous secretion of B. subtilis chitosanase enzyme from E. coli expression system
OE-PCR protocol for the insertion of the OmpA signal sequence into the... | Download Scientific Diagram
IJMS | Free Full-Text | Take Me Home, Protein Roads: Structural Insights into Signal Peptide Interactions during ER Translocation
Interaction of Periplasmic Fab Production and Intracellular Redox Balance in Escherichia coli Affects Product Yield | ACS Synthetic Biology
The Presence of N-Terminal Secretion Signal Sequences Leads to Strong Stimulation of the Total Expression Levels of Three Tested Medically Important Proteins during High-Cell-Density Cultivations of Escherichia coli | Applied and Environmental
The targeting pathway of Escherichia coli presecretory and integral membrane proteins is specified by the hydrophobicity of the targeting signal | PNAS
Microbioreactor Cultivations of Fab‐Producing Escherichia coli Reveal Genome‐Integrated Systems as Suitable for Prospective Studies on Direct Fab Expression Effects - Fink - 2019 - Biotechnology Journal - Wiley Online Library
The ompA signal peptide directed secretion of Staphylococcal nuclease A by Escherichia coli.
Transport of Folded Proteins by the Tat System | SpringerLink
Secretory and extracellular production of recombinant proteins using Escherichia coli
Signal peptide cleavage sites. N-terminal sequencing of Nat-Csn and... | Download Scientific Diagram
Signal sequences directing cotranslational translocation expand the range of proteins amenable to phage display | Nature Biotechnology
Transport of Folded Proteins by the Tat System | SpringerLink
Structure and mechanism of Escherichia coli type I signal peptidase - ScienceDirect
Functional Analysis of a Rickettsial OmpA Homology Domain of Shigella flexneri IcsA | Journal of Bacteriology
Signal peptidase I: Cleaving the way to mature proteins - Auclair - 2012 - Protein Science - Wiley Online Library
