Search Results - "Kapust, R B"
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Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
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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Nitric Oxide-Induced p53 Accumulation and Regulation of Inducible Nitric Oxide Synthase Expression by Wild-Type p53
Published in Proceedings of the National Academy of Sciences - PNAS (19-03-1996)“…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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Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency
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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Structural Basis for the Substrate Specificity of Tobacco Etch Virus Protease
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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Controlled Intracellular Processing of Fusion Proteins by TEV Protease
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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Single amino acid substitutions on the surface of Escherichia coli maltose‐binding protein can have a profound impact on the solubility of fusion proteins
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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Expression, Purification, Refolding, and Characterization of Recombinant Human Interleukin-13: Utilization of Intracellular Processing
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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The amino-terminal domain of human STAT4. Overproduction, purification, and biophysical characterization
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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The P1 ′ specificity of tobacco etch virus protease
Published in Biochemical and biophysical research communications (28-06-2002)“…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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Efficient site-specific processing of fusion proteins by tobacco vein mottling virus protease in vivo and in vitro
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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Tobacco etch virus proteinase: crystal structure of the active enzyme and its inactive mutant
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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Processive Degradation of Nascent Polypeptides, Triggered by Tandem AGA Codons, Limits the Accumulation of Recombinant Tobacco Etch Virus Protease in Escherichia coli BL21(DE3)
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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