Frontiers | Bacterial Signal Peptides- Navigating the Journey of Proteins
Table 1 from Lee Secretory and extracellular production of recombinant proteins using Escherichia coli | Semantic Scholar
The targeting pathway of Escherichia coli presecretory and integral membrane proteins is specified by the hydrophobicity of the targeting signal | PNAS
Signal peptide cleavage sites. N‑terminal sequence analysis of purified... | Download Scientific Diagram
Nucleotide and amino acid sequences of the N-terminal regions of the... | Download Scientific Diagram
Increased production of periplasmic proteins in Escherichia coli by directed evolution of the translation initiation region | Microbial Cell Factories | Full Text
OmpA signal peptide leads to heterogenous secretion of B. subtilis chitosanase enzyme from E. coli expression system | SpringerPlus | Full Text
Part:BBa K1989045 - parts.igem.org
OmpA signal peptide leads to heterogenous secretion of B. subtilis chitosanase enzyme from E. coli expression system
Secretory and extracellular production of recombinant proteins using Escherichia coli
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
Frontiers | Enhancing Recombinant Protein Yields in the E. coli Periplasm by Combining Signal Peptide and Production Rate Screening
Transport of Folded Proteins by the Tat System | SpringerLink
Structure and mechanism of Escherichia coli type I signal peptidase - ScienceDirect
Amino acid sequences of the G3 and TA peptides. The recombinant colicin... | Download Scientific Diagram
Signal peptide cleavage sites. N-terminal sequencing of Nat-Csn and... | Download Scientific Diagram
Signal peptides for recombinant protein secretion in bacterial expression systems | Microbial Cell Factories | Full Text
The targeting pathway of Escherichia coli presecretory and integral membrane proteins is specified by the hydrophobicity of the targeting signal | PNAS
Efficient function of signal peptidase 1 of Escherichia coli is partly determined by residues in the mature N-terminus of exported proteins - ScienceDirect
A model depicting possible intracellular fates of OmpA signal... | Download Scientific Diagram
SRP and Sec pathway leader peptides for antibody phage display and antibody fragment production in E. coli - ScienceDirect
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 peptide hydrophobicity modulates interaction with the twin-arginine translocase | bioRxiv
Increased production of periplasmic proteins in Escherichia coli by directed evolution of the translation initiation region | Microbial Cell Factories | Full Text
