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Yunfa Chen - One of the best experts on this subject based on the ideXlab platform.

  • Synthesis of Hierarchical Co Micro/Nanocomposites with Hexagonal Plate and Polyhedron Shapes and Their Catalytic Activities in Glycerol Hydrogenolysis
    Crystal Growth & Design, 2011
    Co-Authors: Xing Zhang, Haibao Zhang, Peng Hu, Fangli Yuan, Yunfa Chen
    Abstract:

    Hierarchical Co micro/nanocomposites with hexagonal plate and Polyhedron shapes in micrometer scales are synthesized through polyol reduction. Flower-surfaces Co hexagonal plates (FCHPs) show the edge lengths of the hexagonal plates about 1-2 mu m in micrometer scales, and the flower-like surfaces of each individual hexagonal plate is composed of nanodiscs with diameters of about 200-250 nm and thicknesses about 20 nm. Flower-surfaces Co Polyhedrons (FCPs) show the twin-hexagonal-frustum-pyramid morphology in micrometer scales with diameters of about 2-3 mu m, and the flower-like surfaces of each Polyhedron is also composed of nanodiscs with diameters of about 100-150 nm and thicknesses of about 20-30 nm. An oxidation-dissolution and subsequent reduction mechanism is proposed to explain the formation of their flower-like surface structure. Both FCHPs and FCPs exhibit good catalytic activities in glycerol hydrogenolysis.

  • synthesis of hierarchical co micro nanocomposites with hexagonal plate and Polyhedron shapes and their catalytic activities in glycerol hydrogenolysis
    Crystal Growth & Design, 2011
    Co-Authors: Xing Zhang, Haibao Zhang, Peng Hu, Fangli Yuan, Yunfa Chen
    Abstract:

    Hierarchical Co micro/nanocomposites with hexagonal plate and Polyhedron shapes in micrometer scales are synthesized through polyol reduction. Flower-surfaces Co hexagonal plates (FCHPs) show the edge lengths of the hexagonal plates about 1-2 mu m in micrometer scales, and the flower-like surfaces of each individual hexagonal plate is composed of nanodiscs with diameters of about 200-250 nm and thicknesses about 20 nm. Flower-surfaces Co Polyhedrons (FCPs) show the twin-hexagonal-frustum-pyramid morphology in micrometer scales with diameters of about 2-3 mu m, and the flower-like surfaces of each Polyhedron is also composed of nanodiscs with diameters of about 100-150 nm and thicknesses of about 20-30 nm. An oxidation-dissolution and subsequent reduction mechanism is proposed to explain the formation of their flower-like surface structure. Both FCHPs and FCPs exhibit good catalytic activities in glycerol hydrogenolysis.

S. -y. Lee - One of the best experts on this subject based on the ideXlab platform.

  • A common pathway for p10 and calyx proteins in progressive stages of Polyhedron envelope assembly in AcMNPV-infectedSpodoptera frugiperda larvae
    Archives of Virology, 1996
    Co-Authors: S. -y. Lee, A. Poloumienko, S. Belfry, W. Chen, N. Macafee, B. Morin, C. Lucarotti, M. Krause
    Abstract:

    The assembly of the Polyhedron envelope in baculovirus-infected cells has been the subject of several studies, yet it is still poorly understood. We have used immunogold-labelled antibodies to two baculovirus proteins, p10 and calyx (also referred to as Polyhedron envelope protein or PEP), to follow envelope assembly in AcMNPV-infected tissues of Spodoptera frugiperda larvae. We show that, in wild type virus, both proteins colocalize in fibrillar structures and associated electron-dense spacers which progress to encircle the polyhedra, as well as in completed Polyhedron envelopes. In cells infected with polyhedrin-negative (PH^−) viruses, an unusual proliferation of these spacers was observed suggesting a deregulatory event in the envelope assembly process. Results of Northern and Western blot analysis revealed that synthesis of P10 and calyx mRNA and proteins in PH^− AcMNPV is unaffected as compared to wild type virus. Taken together, the observed physical and compositional connection between fibrillar structures, spacers and Polyhedron envelopes, as well as the abnormal appearance of the spacers in PH^− mutants, provide further evidence in support of a cooperative role of these structures in the assembly of the Polyhedron envelope.

  • A common pathway for p10 and calyx proteins in progressive stages of Polyhedron envelope assembly in AcMNPV-infected Spodoptera frugiperda larvae.
    Archives of virology, 1996
    Co-Authors: S. -y. Lee, A. Poloumienko, S. Belfry, W. Chen, N. Macafee, B. Morin, C. Lucarotti, Margarida O. Krause
    Abstract:

    The assembly of the Polyhedron envelope in baculovirus-infected cells has been the subject of several studies, yet it is still poorly understood. We have used immunogold-labelled antibodies to two baculovirus proteins, p10 and calyx (also referred to as Polyhedron envelope protein or PEP), to follow envelope assembly in AcMNPV-infected tissues ofSpodoptera frugiperda larvae. We show that, in wild type virus, both proteins colocalize in fibrillar structures and associated electron-dense spacers which progress to encircle the polyhedra, as well as in completed Polyhedron envelopes. In cells infected with polyhedrin-negative (PH−) viruses, an unusual proliferation of these spacers was observed suggesting a deregulatory event in the envelope assembly process. Results of Northern and Western blot analysis revealed that synthesis of P10 and calyx mRNA and proteins in PH− AcMNPV is unaffected as compared to wild type virus. Taken together, the observed physical and compositional connection between fibrillar structures, spacers and Polyhedron envelopes, as well as the abnormal appearance of the spacers in PH− mutants, provide further evidence in support of a cooperative role of these structures in the assembly of the Polyhedron envelope.

Xing Zhang - One of the best experts on this subject based on the ideXlab platform.

  • Synthesis of Hierarchical Co Micro/Nanocomposites with Hexagonal Plate and Polyhedron Shapes and Their Catalytic Activities in Glycerol Hydrogenolysis
    Crystal Growth & Design, 2011
    Co-Authors: Xing Zhang, Haibao Zhang, Peng Hu, Fangli Yuan, Yunfa Chen
    Abstract:

    Hierarchical Co micro/nanocomposites with hexagonal plate and Polyhedron shapes in micrometer scales are synthesized through polyol reduction. Flower-surfaces Co hexagonal plates (FCHPs) show the edge lengths of the hexagonal plates about 1-2 mu m in micrometer scales, and the flower-like surfaces of each individual hexagonal plate is composed of nanodiscs with diameters of about 200-250 nm and thicknesses about 20 nm. Flower-surfaces Co Polyhedrons (FCPs) show the twin-hexagonal-frustum-pyramid morphology in micrometer scales with diameters of about 2-3 mu m, and the flower-like surfaces of each Polyhedron is also composed of nanodiscs with diameters of about 100-150 nm and thicknesses of about 20-30 nm. An oxidation-dissolution and subsequent reduction mechanism is proposed to explain the formation of their flower-like surface structure. Both FCHPs and FCPs exhibit good catalytic activities in glycerol hydrogenolysis.

  • synthesis of hierarchical co micro nanocomposites with hexagonal plate and Polyhedron shapes and their catalytic activities in glycerol hydrogenolysis
    Crystal Growth & Design, 2011
    Co-Authors: Xing Zhang, Haibao Zhang, Peng Hu, Fangli Yuan, Yunfa Chen
    Abstract:

    Hierarchical Co micro/nanocomposites with hexagonal plate and Polyhedron shapes in micrometer scales are synthesized through polyol reduction. Flower-surfaces Co hexagonal plates (FCHPs) show the edge lengths of the hexagonal plates about 1-2 mu m in micrometer scales, and the flower-like surfaces of each individual hexagonal plate is composed of nanodiscs with diameters of about 200-250 nm and thicknesses about 20 nm. Flower-surfaces Co Polyhedrons (FCPs) show the twin-hexagonal-frustum-pyramid morphology in micrometer scales with diameters of about 2-3 mu m, and the flower-like surfaces of each Polyhedron is also composed of nanodiscs with diameters of about 100-150 nm and thicknesses of about 20-30 nm. An oxidation-dissolution and subsequent reduction mechanism is proposed to explain the formation of their flower-like surface structure. Both FCHPs and FCPs exhibit good catalytic activities in glycerol hydrogenolysis.

Margarida O. Krause - One of the best experts on this subject based on the ideXlab platform.

  • A common pathway for p10 and calyx proteins in progressive stages of Polyhedron envelope assembly in AcMNPV-infected Spodoptera frugiperda larvae.
    Archives of virology, 1996
    Co-Authors: S. -y. Lee, A. Poloumienko, S. Belfry, W. Chen, N. Macafee, B. Morin, C. Lucarotti, Margarida O. Krause
    Abstract:

    The assembly of the Polyhedron envelope in baculovirus-infected cells has been the subject of several studies, yet it is still poorly understood. We have used immunogold-labelled antibodies to two baculovirus proteins, p10 and calyx (also referred to as Polyhedron envelope protein or PEP), to follow envelope assembly in AcMNPV-infected tissues ofSpodoptera frugiperda larvae. We show that, in wild type virus, both proteins colocalize in fibrillar structures and associated electron-dense spacers which progress to encircle the polyhedra, as well as in completed Polyhedron envelopes. In cells infected with polyhedrin-negative (PH−) viruses, an unusual proliferation of these spacers was observed suggesting a deregulatory event in the envelope assembly process. Results of Northern and Western blot analysis revealed that synthesis of P10 and calyx mRNA and proteins in PH− AcMNPV is unaffected as compared to wild type virus. Taken together, the observed physical and compositional connection between fibrillar structures, spacers and Polyhedron envelopes, as well as the abnormal appearance of the spacers in PH− mutants, provide further evidence in support of a cooperative role of these structures in the assembly of the Polyhedron envelope.

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

  • A common pathway for p10 and calyx proteins in progressive stages of Polyhedron envelope assembly in AcMNPV-infectedSpodoptera frugiperda larvae
    Archives of Virology, 1996
    Co-Authors: S. -y. Lee, A. Poloumienko, S. Belfry, W. Chen, N. Macafee, B. Morin, C. Lucarotti, M. Krause
    Abstract:

    The assembly of the Polyhedron envelope in baculovirus-infected cells has been the subject of several studies, yet it is still poorly understood. We have used immunogold-labelled antibodies to two baculovirus proteins, p10 and calyx (also referred to as Polyhedron envelope protein or PEP), to follow envelope assembly in AcMNPV-infected tissues of Spodoptera frugiperda larvae. We show that, in wild type virus, both proteins colocalize in fibrillar structures and associated electron-dense spacers which progress to encircle the polyhedra, as well as in completed Polyhedron envelopes. In cells infected with polyhedrin-negative (PH^−) viruses, an unusual proliferation of these spacers was observed suggesting a deregulatory event in the envelope assembly process. Results of Northern and Western blot analysis revealed that synthesis of P10 and calyx mRNA and proteins in PH^− AcMNPV is unaffected as compared to wild type virus. Taken together, the observed physical and compositional connection between fibrillar structures, spacers and Polyhedron envelopes, as well as the abnormal appearance of the spacers in PH^− mutants, provide further evidence in support of a cooperative role of these structures in the assembly of the Polyhedron envelope.