Unrelated solubility-enhancing fusion partners MBP and NusA utilize a similar mode of action

The Ability to Enhance the Solubility of Its Fusion Partners Is an Intrinsic Property of Maltose-Binding Protein but Their Folding Is Either Spontaneous or Chaperone-Mediated

(2012) Sreejith Raran-Kurussi et al.   PLoS One

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

Isolation of Metarhizium anisopliae carboxypeptidase A with native disulfide bonds from the cytosol of Escherichia coli BL21(DE3)

(2011) Brian P. Austin et al.   PROTEIN EXPRESSION AND PURIFICATION

The dynamics of the MBP–MalFGK2 interaction: A prototype for binding protein dependent ABC-transporter systems

(2007) Brian H. Shilton   BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES

High-throughput screening of soluble recombinant proteins

(2002) Yan-Ping Shih et al.   PROTEIN SCIENCE

Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli

(2002) Martin Hammarström et al.   PROTEIN SCIENCE