The Experts below are selected from a list of 46362 Experts worldwide ranked by ideXlab platform

I. Furusawa - One of the best experts on this subject based on the ideXlab platform.

  • Expression and characterization of the 3a movement protein of cowpea chlorotic mottle bromovirus
    Archives of Virology, 1999
    Co-Authors: M. Fujita, K. Mise, I. Furusawa
    Abstract:

     Cowpea chlorotic mottle bromovirus (CCMV) 3a protein is required for cell-to-cell movement of the virus in host plants. The 3a protein was produced in Escherichia coli using an expression vector. Gel retardation analysis and UV cross-linking experiments demonstrated that the CCMV 3a protein (CC3a) bound single-stranded (ss) RNA cooperatively without sequence specificity. Binding Competition analysis showed that CC3a bound ss-nucleic acids more strongly than double-stranded nucleic acids.

  • Nucleic acid-Binding properties and subcellular localization of the 3a protein of brome mosaic bromovirus.
    Journal of General Virology, 1998
    Co-Authors: M. Fujita, K. Mise, Yasuko Kajiura, Koji Dohi, I. Furusawa
    Abstract:

    Brome mosaic bromovirus (BMV) 3a protein is required for cell-to-cell movement of the virus in host plants. The BMV 3a protein (B3a) was produced in Escherichia coli using an expression vector. Gel retardation analysis and UV cross-linking experiments demonstrated that B3a bound single-stranded RNA cooperatively without sequence specificity. Binding Competition analysis showed that B3a bound to single-stranded nucleic acids more strongly than to double-stranded nucleic acids. Deletion mutagenesis located a nucleic acid-Binding domain to amino acids 189-242. Western blot analysis of fractionated proteins of BMV-infected barley using monoclonal antibodies against B3a indicated that B3a may interact with membrane materials and form complexes in the cytoplasm. Immunogold labelling of thin sections of infected barley tissues revealed that B3a was associated with plasmodesmata and cytoplasmic inclusions.

  • Nucleic acid-Binding properties and subcellular localization of the 3a protein of brome mosaic bromovirus
    1998
    Co-Authors: M. Fujita, K. Mise, Yasuko Kajiura, Koji Dohi, I. Furusawa
    Abstract:

    Brome mosaic bromovirus (BMV) 3a protein is required for cell-to-cell movement of the virus in host plants. The BMV 3a protein (B3a) was produced in Escherichia coli using an expression vector. Gel retardation analysis and UV cross-linking experi-ments demonstrated that B3a bound single-stranded RNA cooperatively without sequence spe-cificity. Binding Competition analysis showed that B3a bound to single-stranded nucleic acids more strongly than to double-stranded nucleic acids. De

K W Buck - One of the best experts on this subject based on the ideXlab platform.

  • cooperative Binding of the red clover necrotic mosaic virus movement protein to single stranded nucleic acids
    Journal of General Virology, 1992
    Co-Authors: T. A. M. Osman, R J Hayes, K W Buck
    Abstract:

    The movement protein of red clover necrotic mosaic dianthovirus was produced in Escherichia coli using an expression vector. Gel retardation analysis and u.v. cross-linking studies showed that the movement protein bound cooperatively to ssRNA and ssDNA, but not to dsDNA. Binding Competition experiments established that the movement protein bound to ssRNA and ssDNA with similar affinities and that the Binding was not sequence-specific in the experimental conditions employed. A truncated movement protein lacking the C-terminal 88 amino acids was also shown to bind to ssRNA.

  • Cooperative Binding of the red clover necrotic mosaic virus to single-stranded nucleic acids
    1992
    Co-Authors: T. A. M. Osman, R J Hayes, K W Buck
    Abstract:

    The movement protein of red clover necrotic mosaic dianthovirus was produced in Escherichia coli using an expression vector. Gel retardation analysis and u.v. cross-linking studies showed that the movement protein bound cooperatively to ssRNA and ssDNA, but not to dsDNA. Binding Competition experiments established that the movement protein bound to ssRNA and ssDNA with similar affinities and that the Binding was not sequence-specific in the experimental conditions employed. A truncated movement protein lacking the C-terminal 88 amino acids was also shown to bind to ssRNA

M. Fujita - One of the best experts on this subject based on the ideXlab platform.

  • Expression and characterization of the 3a movement protein of cowpea chlorotic mottle bromovirus
    Archives of Virology, 1999
    Co-Authors: M. Fujita, K. Mise, I. Furusawa
    Abstract:

     Cowpea chlorotic mottle bromovirus (CCMV) 3a protein is required for cell-to-cell movement of the virus in host plants. The 3a protein was produced in Escherichia coli using an expression vector. Gel retardation analysis and UV cross-linking experiments demonstrated that the CCMV 3a protein (CC3a) bound single-stranded (ss) RNA cooperatively without sequence specificity. Binding Competition analysis showed that CC3a bound ss-nucleic acids more strongly than double-stranded nucleic acids.

  • Nucleic acid-Binding properties and subcellular localization of the 3a protein of brome mosaic bromovirus.
    Journal of General Virology, 1998
    Co-Authors: M. Fujita, K. Mise, Yasuko Kajiura, Koji Dohi, I. Furusawa
    Abstract:

    Brome mosaic bromovirus (BMV) 3a protein is required for cell-to-cell movement of the virus in host plants. The BMV 3a protein (B3a) was produced in Escherichia coli using an expression vector. Gel retardation analysis and UV cross-linking experiments demonstrated that B3a bound single-stranded RNA cooperatively without sequence specificity. Binding Competition analysis showed that B3a bound to single-stranded nucleic acids more strongly than to double-stranded nucleic acids. Deletion mutagenesis located a nucleic acid-Binding domain to amino acids 189-242. Western blot analysis of fractionated proteins of BMV-infected barley using monoclonal antibodies against B3a indicated that B3a may interact with membrane materials and form complexes in the cytoplasm. Immunogold labelling of thin sections of infected barley tissues revealed that B3a was associated with plasmodesmata and cytoplasmic inclusions.

  • Nucleic acid-Binding properties and subcellular localization of the 3a protein of brome mosaic bromovirus
    1998
    Co-Authors: M. Fujita, K. Mise, Yasuko Kajiura, Koji Dohi, I. Furusawa
    Abstract:

    Brome mosaic bromovirus (BMV) 3a protein is required for cell-to-cell movement of the virus in host plants. The BMV 3a protein (B3a) was produced in Escherichia coli using an expression vector. Gel retardation analysis and UV cross-linking experi-ments demonstrated that B3a bound single-stranded RNA cooperatively without sequence spe-cificity. Binding Competition analysis showed that B3a bound to single-stranded nucleic acids more strongly than to double-stranded nucleic acids. De

Kohuang Lue - One of the best experts on this subject based on the ideXlab platform.

  • ifn γ induction on carbohydrate Binding module of fungal immunomodulatory protein in human peripheral mononuclear cells
    Journal of Agricultural and Food Chemistry, 2012
    Co-Authors: Yufan Liu, Shihhsien Chang, Hailun Sun, Yuchi Chang, Ilun Hsin, Kohuang Lue
    Abstract:

    FIP-fve is a protein that is isolated from Flammulina velutipes. Its known immunomodulatory activities are elicitation of the production of type II interferon from human peripheral mononuclear cells (hPBMCs) and hemagglutination. How the target receptors mediate activation of FIP-fve-induced immunomodulatory effects remains to be elucidated. This study postulates the three-dimensional structures to determine whether the carbohydrate Binding module family 34 (CBM-34) on FIP-fve is conserved to site N of Thermoactinomyces vulgaris R-47 α-amylase I. Experimental site-directed mutagenesis data as well as ligand-specific Binding Competition assay are adopted to identify the key residues W24, T28, D34, T90, I91, and W111 of FIP-fve that participate in Binding to polysaccharides that are linked to the membrane of immune cells. Treatments of hPBMCs with tunicamycin and deglycosylation enzymes that removed the carbohydrate moieties reduced the secretion of IFN-γ induction from hPBMCs. In conclusion, the experiment...

  • IFN-γ Induction on Carbohydrate Binding Module of Fungal Immunomodulatory Protein in Human Peripheral Mononuclear Cells
    2012
    Co-Authors: Yufan Liu, Shihhsien Chang, Hailun Sun, Yuchi Chang, Ilun Hsin, Kohuang Lue
    Abstract:

    FIP-fve is a protein that is isolated from Flammulina velutipes. Its known immunomodulatory activities are elicitation of the production of type II interferon from human peripheral mononuclear cells (hPBMCs) and hemagglutination. How the target receptors mediate activation of FIP-fve-induced immunomodulatory effects remains to be elucidated. This study postulates the three-dimensional structures to determine whether the carbohydrate Binding module family 34 (CBM-34) on FIP-fve is conserved to site N of Thermoactinomyces vulgaris R-47 α-amylase I. Experimental site-directed mutagenesis data as well as ligand-specific Binding Competition assay are adopted to identify the key residues W24, T28, D34, T90, I91, and W111 of FIP-fve that participate in Binding to polysaccharides that are linked to the membrane of immune cells. Treatments of hPBMCs with tunicamycin and deglycosylation enzymes that removed the carbohydrate moieties reduced the secretion of IFN-γ induction from hPBMCs. In conclusion, the experiments herein demonstrated the ligand-Binding CBM-34 on FIP-fve and ligand-like glycoproteins on the surface of hPBMCs must be required to induce physiological immunomodulatory effects

T. A. M. Osman - One of the best experts on this subject based on the ideXlab platform.

  • cooperative Binding of the red clover necrotic mosaic virus movement protein to single stranded nucleic acids
    Journal of General Virology, 1992
    Co-Authors: T. A. M. Osman, R J Hayes, K W Buck
    Abstract:

    The movement protein of red clover necrotic mosaic dianthovirus was produced in Escherichia coli using an expression vector. Gel retardation analysis and u.v. cross-linking studies showed that the movement protein bound cooperatively to ssRNA and ssDNA, but not to dsDNA. Binding Competition experiments established that the movement protein bound to ssRNA and ssDNA with similar affinities and that the Binding was not sequence-specific in the experimental conditions employed. A truncated movement protein lacking the C-terminal 88 amino acids was also shown to bind to ssRNA.

  • Cooperative Binding of the red clover necrotic mosaic virus to single-stranded nucleic acids
    1992
    Co-Authors: T. A. M. Osman, R J Hayes, K W Buck
    Abstract:

    The movement protein of red clover necrotic mosaic dianthovirus was produced in Escherichia coli using an expression vector. Gel retardation analysis and u.v. cross-linking studies showed that the movement protein bound cooperatively to ssRNA and ssDNA, but not to dsDNA. Binding Competition experiments established that the movement protein bound to ssRNA and ssDNA with similar affinities and that the Binding was not sequence-specific in the experimental conditions employed. A truncated movement protein lacking the C-terminal 88 amino acids was also shown to bind to ssRNA