Rachel B. Kapust

<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

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

Nitric oxide-induced p53 accumulation and regulation of inducible nitric oxide synthase expression by wild-type p53.

Kathleen Forrester, Stefan Ambs, Shawn E. Lupold et al. · Proceedings of the National Academy of Sciences · 1996 · 468 citations

Life Sciences, Genetics, Molecular Biology +13

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

Structural Basis for the Substrate Specificity of Tobacco Etch Virus Protease

Jason Phan, Alexander Zdanov, Joseph E. Tropea et al. · Journal of Biological Chemistry · 2002 · 260 citations · Full text

Life Sciences, Biochemistry, Molecular Biology +17