Recombinant protein folding and misfolding in Escherichia coli

By F. Baneyx, Mirna Mujacic. Nature Biotechnology, 2004

1,450 citations recorded by the source corpus.

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins. (2006, background): “, Escherichia coli, Saccharomyces cerevisiae, Pichia pastoris, insect and mammalian cell lines) have been developed to express heterologous proteins [2–7].”
The CamSol method of rational design of protein mutants with enhanced solubility. (2015, background): “Thus, protein aggregation represents also a major biotechnological issue, preventing many proteins to be produced at economically convenient yields [13,20,22].”
Properties, Potentials, and Prospects of Antifreeze Proteins (2008, methodology): “In E. coli, a group of proteins DsbA, DsbB, DsbC, DsbD, DsbE, and DsbG are found in the periplasm and inner membrane and are involved in disulfide bond formation (for a review, see Baneyx and Mujacic, 2004; Tan and Bardwell, 2004).”
Daedalus: a robust, turnkey platform for rapid production of decigram quantities of active recombinant proteins in human cell lines using novel lentiviral vectors (2011, neutral): “However, eukaryotic proteins produced in bacteria often suffer from poor solubility, resulting in aggregation or misfolding, or lack proper post-translational modifications necessary for full biological activity (1,2).”