Mocr: A novel fusion tag for enhancing solubility that is compatible with structural biology applications

This publication has 33 references indexed in Scilit:

• Mutations that alter the equilibrium between open and closed conformations of Escherichia coli maltose-binding protein impede its ability to enhance the solubility of passenger proteins
  Biochemical and Biophysical Research Communications, 2007
• The acidity of protein fusion partners predominantly determines the efficacy to improve the solubility of the target proteins expressed in Escherichia coli
  Journal of Biotechnology, 2007
• The yeast Mediator complex and its regulation
  Published by Elsevier ,2005
• Amyloid-like Properties of Bacterial Inclusion Bodies
  Journal of Molecular Biology, 2005
• Mechanism of caveolin filament assembly
  Proceedings of the National Academy of Sciences, 2002
• Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli
  Protein Science, 2002
• Structure of Ocr from Bacteriophage T7, a Protein that Mimics B-Form DNA
  Molecular Cell, 2002
• Escherichia coli maltose‐binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
  Protein Science, 1999
• Design of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMR
  Protein Science, 1997
• Active protection by bacteriophages T3 and T7 againstE. coli B-and K-specific restriction of their DNA
  Molecular Genetics and Genomics, 1977