Efficient export of prefolded, disulfide-bonded recombinant proteins to the periplasm by the Tat pathway in Escherichia coli CyDisCo strains

High-yield export of a native heterologous protein to the periplasm by the tat translocation pathway in Escherichia coli

(2012) Cristina F.R.O. Matos et al.   BIOTECHNOLOGY AND BIOENGINEERING

Coexpression of molecular chaperone enhances activity and export of organophosphorus hydrolase in Escherichia coli

(2012) Dong Gyun Kang et al.   BIOTECHNOLOGY PROGRESS

Investigation of the impact of Tat export pathway enhancement on E. coli culture, protein production and early stage recovery

(2011) Steven D. Branston et al.   BIOTECHNOLOGY AND BIOENGINEERING

Pre-expression of a sulfhydryl oxidase significantly increases the yields of eukaryotic disulfide bond containing proteins expressed in the cytoplasm of E.coli

(2011) Van Nguyen et al.   Microbial Cell Factories

Mechanisms of Oxidative Protein Folding in the Bacterial Cell Envelope

(2010) Hiroshi Kadokura et al.   ANTIOXIDANTS & REDOX SIGNALING

Transport and proofreading of proteins by the twin-arginine translocation (Tat) system in bacteria

(2010) Colin Robinson et al.   BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES

Post-translational modifications of protein biopharmaceuticals

(2010) Gary Walsh   DRUG DISCOVERY TODAY

High Resolution NMR-based Model for the Structure of a scFv-IL-1β Complex

(2009) Ian C. Wilkinson et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Mutant AhpC Peroxiredoxins Suppress Thiol-Disulfide Redox Deficiencies and Acquire Deglutathionylating Activity

(2008) Yuji Yamamoto et al.   MOLECULAR CELL

Functional plasticity of a peroxidase allows evolution of diverse disulfide-reducing pathways

(2008) M. J. Faulkner et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Exploration of twin-arginine translocation for expression and purification of correctly folded proteins inEscherichia coli

(2008) Adam C. Fisher et al.   Microbial Biotechnology