The acidity of protein fusion partners predominantly determines the efficacy to improve the solubility of the target proteins expressed in Escherichia coli

This publication has 46 references indexed in Scilit:

• Enhanced soluble protein expression using two new fusion tags
  Protein Expression and Purification, 2006
• Prediction of unfolded segments in a protein sequence based on amino acid composition
  Bioinformatics, 2005
• Production of soluble mammalian proteins in Escherichia coli: identification of protein features that correlate with successful expression
  BMC Biotechnology, 2004
• Protein expression and refolding – A practical guide to getting the most out of inclusion bodies
  Biotechnology Annual Review, 2004
• Genetic Analysis of Calmodulin and Its Targets in Saccharomyces cerevisiae
  Annual Review of Genetics, 2001
• Green fluorescent protein as an indicator to monitor membrane protein overexpression in Escherichia coli
  FEBS Letters, 2001
• Observations of green fluorescent protein as a fusion partner in genetically engineeredEscherichia coli: Monitoring protein expression and solubility
  Biotechnology & Bioengineering, 2000
• New fusion protein systems designed to give soluble expression inEscherichia coli
  Biotechnology & Bioengineering, 1999
• The Anomalous Electrophoretic Behavior of the Human Papillomavirus Type 16 E7 Protein Is Due to the High Content of Acidic Amino Acid Residues
  Biochemical and Biophysical Research Communications, 1993
• Prediction of protein folding class from amino acid composition
  Proteins-Structure Function and Bioinformatics, 1993