Solubility-enhancing proteins MBP and NusA play a passive role in the folding of their fusion partners

<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

A Thioredoxin Gene Fusion Expression System That Circumvents Inclusion Body Formation in the E. coli Cytoplasm

Edward R. LaVallie, Elizabeth Diblasio, Sharlotte Kovacic et al. · Nature Biotechnology · 1993 · 931 citations

Life Sciences, Genetics, Molecular Biology +11

Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency

Rachel B. Kapust, József Tőzsér, Jeffrey D. Fox et al. · Protein Engineering Design and Selection · 2001 · 879 citations · Full text

Life Sciences, Biochemistry, Molecular Biology +17

The P1′ specificity of tobacco etch virus protease

Rachel B. Kapust, József Tőzsér, Terry D. Copeland et al. · Biochemical and Biophysical Research Communications · 2002 · 395 citations · Full text

Life Sciences, Microbiology, Molecular Biology +10

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