A novel multi-affinity tag system to produce high levels of soluble and biotinylated proteins in Escherichia coli

<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 minimal peptide substrate in biotin holoenzyme synthetase‐catalyzed biotinylation

Dorothy Beckett, Elena G. Kovaleva, Peter J. Schatz · Protein Science · 1999 · 746 citations · Full text

Life Sciences, Biochemistry, Molecular Biology +13

Use of Peptide Libraries to Map the Substrate Specificity of a Peptide-Modifying Enzyme: A 13 Residue Consensus Peptide Specifies Biotinylation in Escherichia coli

Peter J. Schatz · Nature Biotechnology · 1993 · 589 citations

Life Sciences, Biochemistry, Molecular Biology +17

Efficient biotinylation and single-step purification of tagged transcription factors in mammalian cells and transgenic mice

Ernie de Boer, Patrick Rodriguez, Edgar Bonte et al. · Proceedings of the National Academy of Sciences · 2003 · 413 citations · Full text

Life Sciences, Biochemistry, Molecular Biology +13

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