Bacterial expression and purification of Interleukin-2 Tyrosine kinase: Single step separation of the chaperonin impurity

<i>Escherichia coli</i> maltose‐binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused

Rachel B. Kapust, David S. Waugh · Protein Science · 1999 · 964 citations · Full text

Life Sciences, Biochemistry, Molecular Biology +16

Chaperone Coexpression Plasmids: Differential and Synergistic Roles of DnaK-DnaJ-GrpE and GroEL-GroES in Assisting Folding of an Allergen of Japanese Cedar Pollen, Cryj2, in <i>Escherichia coli</i>

Kazuyo Nishihara, Masaaki Kanemori, Masanari Kitagawa et al. · Applied and Environmental Microbiology · 1998 · 432 citations · Full text

Life Sciences, Biotechnology, Molecular Biology +17

Chaperonin-facilitated refolding of ribulose bisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are potassium dependent

Paul V. Viitanen, Thomas Lübben, J. N. Reed et al. · Biochemistry · 1990 · 382 citations

Life Sciences, Biochemistry, Molecular Biology +17

Rapid screening for improved solubility of small human proteins produced as fusion proteins in <i>Escherichia coli</i>

M. Hammarstrom, Niklas Hellgren, Susanne van den Berg et al. · Protein Science · 2002 · 335 citations · Full text

Life Sciences, Biotechnology, Molecular Biology +15

The conformational quality of insoluble recombinant proteins is enhanced at low growth temperatures

Andrea Vera, Núria González‐Montalbán, Antonio Villaverde · Biotechnology and Bioengineering · 2006 · 258 citations

Life Sciences, Biochemistry, Biotechnology +17