Search Results - "Kapust, Rachel B."

The P1 ′ specificity of tobacco etch virus protease by Kapust, Rachel B, Tözsér, József, Copeland, Terry D, Waugh, David S

“…Affinity tags have become indispensable tools for protein expression and purification. Yet, because they have the potential to interfere with structural and…”
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Structural Basis for the Substrate Specificity of Tobacco Etch Virus Protease by Phan, Jason, Zdanov, Alexander, Evdokimov, Artem G., Tropea, Joseph E., Peters, Howard K., Kapust, Rachel B., Li, Mi, Wlodawer, Alexander, Waugh, David S.

“…Because of its stringent sequence specificity, the 3C-type protease from tobacco etch virus (TEV) is frequently used to remove affinity tags from recombinant…”
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Efficient site-specific processing of fusion proteins by tobacco vein mottling virus protease in vivo and in vitro by Nallamsetty, Sreedevi, Kapust, Rachel B., Tözsér, József, Cherry, Scott, Tropea, Joseph E., Copeland, Terry D., Waugh, David S.

“…Affinity tags are widely used as vehicles for the production of recombinant proteins. Yet, because of concerns about their potential to interfere with the…”
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Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency by Kapust, Rachel B., Tözsér, József, Fox, Jeffrey D., Anderson, D.Eric, Cherry, Scott, Copeland, Terry D., Waugh, David S.

“…Because of its stringent sequence specificity, the catalytic domain of the nuclear inclusion protease from tobacco etch virus (TEV) is a useful reagent for…”
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Nitric Oxide-Induced p53 Accumulation and Regulation of Inducible Nitric Oxide Synthase Expression by Wild-Type p53 by Forrester, Kathleen, Ambs, Stefan, Lupold, Shawn E., Kapust, Rachel B., Spillare, Elisa A., Weinberg, Wendy C., Felley-Bosco, Emanuela, Wang, Xin W., Geller, David A., Tzeng, Edith, Billiar, Timothy R., Harris, Curtis C.

“…The tumor suppressor gene product p53 plays an important role in the cellular response to DNA damage from exogenous chemical and physical mutagens. Therefore,…”
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Processive Degradation of Nascent Polypeptides, Triggered by Tandem AGA Codons, Limits the Accumulation of Recombinant Tobacco Etch Virus Protease in Escherichia coli BL21(DE3) by Kapust, Rachel B., Routzahn, Karen M., Waugh, David S.

“…Due to its high degree of sequence specificity, the catalytic domain of the nuclear inclusion protease from tobacco etch virus (TEV protease) is a useful…”
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Expression, Purification, Refolding, and Characterization of Recombinant Human Interleukin-13: Utilization of Intracellular Processing by Eisenmesser, Elan Zohar, Kapust, Rachel B., Nawrocki, Joseph P., Mazzulla, Marie J., Pannell, Lewis K., Waugh, David S., Byrd, R.Andrew

“…Interleukin-13 (IL-13) is a pleiotropic cytokine that elicits both proinflammatory and anti-inflammatory immune responses. Recent studies underscore its role…”
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Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused by KAPUST, RACHEL B., WAUGH, DAVID S.

“…Although it is usually possible to achieve a favorable yield of a recombinant protein in Escherichia coli, obtaining the protein in a soluble, biologically…”
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The Amino-terminal Domain of Human STAT4 by Baden, Holly A., Sarma, Siddhartha P., Kapust, Rachel B., Byrd, R. Andrew, Waugh, David S.

“…The multifunctional signal transducer and activator of transcription (STAT) proteins relay signals from the cell membrane to the nucleus in response to…”
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Controlled Intracellular Processing of Fusion Proteins by TEV Protease by Kapust, Rachel B., Waugh, David S.

“…Here we describe a method for controlled intracellular processing (CIP) of fusion proteins by tobacco etch virus (TEV) protease. A fusion protein containing a…”
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Single amino acid substitutions on the surface of Escherichia coli maltose‐binding protein can have a profound impact on the solubility of fusion proteins by Fox, Jeffrey D., Kapust, Rachel B., Waugh, David S.

“…Proteins are commonly fused to Escherichia coli maltose‐binding protein (MBP) to enhance their yield and facilitate their purification. In addition, the…”
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The amino-terminal domain of human STAT4. Overproduction, purification, and biophysical characterization by Baden, H A, Sarma, S P, Kapust, R B, Byrd, R A, Waugh, D S

“…The multifunctional signal transducer and activator of transcription (STAT) proteins relay signals from the cell membrane to the nucleus in response to…”
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