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Reducing conditions are the key for efficient production of active ribonuclease inhibitor in Escherichia coli

By Juozas Šiurkus and Peter Neubauer
Topics: Research
Publisher: BioMed Central
OAI identifier: oai:pubmedcentral.nih.gov:3112386
Provided by: PubMed Central

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  1. (2007). al: A dual expression platform to optimize the soluble production of heterologous proteins in the periplasm of Escherichia coli. Appl Microbiol Biotechnol
  2. (2010). al: A novel fed-batch based cultivation method provides high cell-density and improves yield of soluble recombinant proteins in shaken cultures. Microb Cell Fact
  3. (2007). An online monitoring system based on a synthetic sigma32-dependent tandem promoter for visualization of insoluble proteins in the cytoplasm of Escherichia coli. Appl Microbiol Biotechnol
  4. (2001). E: Cosecretion of chaperones and low-molecular-size medium additives increases the yield of recombinant disulfide-bridged proteins. Appl Environ Microbiol
  5. (2008). Enzyme controlled glucose auto-delivery for high cell density cultivations in microplates and shake flasks. Microb Cell Fact
  6. (2011). et al: High level soluble production of functional ribonuclease inhibitor in Escherichia coli by fusing it to soluble partners. Protein Expr Purif
  7. (1990). et al: Protein chemical and kinetic characterization of recombinant porcine ribonuclease inhibitor expressed in Saccharomyces cerevisiae. Biochemistry
  8. (1996). Eukaryotic protein disulfide isomerase complements Escherichia coli dsbA mutants and increases the yield of a heterologous secreted protein with disulfide bonds.
  9. (1990). Folding and aggregation of beta-lactamase in the periplasmic space of Escherichia coli.
  10. (1993). Glockshuber R: In vivo control of redox potential during protein folding catalyzed by bacterial protein disulfide-isomerase (DsbA).
  11. (1994). HF: Effect of redox environment on the in vitro and in vivo folding of RTEM-1 beta-lactamase and Escherichia coli alkaline phosphatase.
  12. (1993). Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulfide bonds in vivo.
  13. (2004). Inclusion bodies: formation and utilisation. Adv Biochem Eng Biotechnol
  14. (2001). Kajava AV: The leucine-rich repeat as a protein recognition motif. Curr Opin Struct Biol
  15. (1997). Localization and characterization of inclusion bodies in recombinant Escherichia coli cells overproducing penicillin G acylase. Appl Microbiol Biotechnol
  16. (1992). LRRCE: a leucine-rich repeat cysteine capping motif unique to the chordate lineage.
  17. (1995). Metabolic load and heterologous gene expression. Biotechnol Adv
  18. (2008). Multiple stressor-induced proteome responses of Escherichia coli BL21(DE3). J Proteome Res
  19. (2010). Novel approach of high cell density recombinant bioprocess development: optimisation and scale-up from microliter to pilot scales while maintaining the fed-batch cultivation mode of E. coli cultures. Microb Cell Fact
  20. (2006). Nystrom T: Conditional and replicative senescence in Escherichia coli. Curr Opin Microbiol
  21. (1990). Production of recombinant human growth hormone in Escherichia coli: expression of different precursors and physiological effects of glucose, acetate, and salts. Biotechnol Bioeng
  22. (1977). Ribonuclease inhibitor from human placenta. Purification and properties. J Biol Chem
  23. (2001). RT: High-level soluble production and characterization of porcine ribonuclease inhibitor. Protein Expr Purif
  24. (2005). RT: Ribonuclease inhibitor: structure and function. Prog Nucleic Acid Res Mol Biol
  25. (1999). Starvation, cessation of growth and bacterial aging. Curr Opin Microbiol
  26. (1989). Vallee BL: Expression of human placental ribonuclease inhibitor in Escherichia coli.
  27. (1998). WE: Generating controlled reducing environments in aerobic recombinant Escherichia coli fermentations: effects on cell growth, oxygen uptake, heat shock protein expression, and in vivo CAT activity. Biotechnol Bioeng