Search Results - "Kapust, R B"

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  1. 1

    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.

    Published in Protein science (01-08-1999)
    “…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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    Journal Article
  2. 2
  3. 3

    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.

    Published in Protein engineering (01-12-2001)
    “…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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  4. 4

    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.

    Published in The Journal of biological chemistry (27-12-2002)
    “…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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  5. 5

    Controlled Intracellular Processing of Fusion Proteins by TEV Protease by Kapust, Rachel B., Waugh, David S.

    Published in Protein expression and purification (01-07-2000)
    “…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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  6. 6

    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.

    Published in Protein science (01-03-2001)
    “…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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  7. 7

    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

    Published in Protein expression and purification (01-11-2000)
    “…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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  8. 8

    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

    Published in The Journal of biological chemistry (03-07-1998)
    “…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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  9. 9

    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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  10. 10

    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.

    Published in Protein expression and purification (01-11-2004)
    “…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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    Journal Article
  11. 11

    Tobacco etch virus proteinase: crystal structure of the active enzyme and its inactive mutant by Zhdanov, A S, Phan, J, Evdokimov, A G, Tropea, J E, Kapust, R B, Li, M, Wlodawer, A, Waugh, D S

    Published in Bioorganicheskaia khimiia (01-09-2003)
    “…Tobacco Etch Virus Protease (TEV protease) is widely used as a tool for separation of recombinant target proteins from their fusion partners. The crystal…”
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  12. 12

    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.

    Published in Protein expression and purification (01-02-2002)
    “…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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    Journal Article