Search Results - "Sugawara, Yasutake"

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  1. 1

    Development of desiccation tolerance and vitrification by preculture treatment in suspension-cultured cells of the liverwort Marchantia polymorpha by Hatanaka, Rie, Sugawara, Yasutake

    Published in Planta (01-03-2010)
    “…Some cultured plant cells are able to acquire tolerance to various stresses when they are cultured under suitably controlled conditions. Induction of a high…”
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    Journal Article
  2. 2

    Biochemical and structural characterization of an endoplasmic reticulum-localized late embryogenesis abundant (LEA) protein from the liverwort Marchantia polymorpha by Hatanaka, Rie, Furuki, Takao, Shimizu, Tempei, Takezawa, Daisuke, Kikawada, Takahiro, Sakurai, Minoru, Sugawara, Yasutake

    “…•We characterized a novel LEA protein from Marchantiales that localizes in the ER.•MpLEA1 has a signal peptide and the ER retention sequence HEEL.•MpLEA1…”
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  3. 3

    Induction of multinucleation by β-glucosyl Yariv reagent in regenerated cells from Marchantia polymorpha protoplasts and involvement of arabinogalactan proteins in cell plate formation by Shibaya, Taeko, Sugawara, Yasutake

    Published in Planta (01-08-2009)
    “…Arabinogalactan proteins (AGPs) are abundant plant cell surface proteoglycans widely distributed in plant species. Since high concentrations of β-glucosyl…”
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    Journal Article
  4. 4

    Involvement of arabinogalactan proteins in the regeneration process of cultured protoplasts of Marchantia polymorpha by Shibaya, Taeko, Sugawara, Yasutake

    Published in Physiologia plantarum (01-06-2007)
    “…Protoplasts of Marchantia polymorpha L. (liverwort) regenerated new cell walls in initial culture. However, the survival rate of regenerated cells decreased…”
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  5. 5

    Induction of multinucleation by [beta]-glucosyl Yariv reagent in regenerated cells from Marchantia polymorpha protoplasts and involvement of arabinogalactan proteins in cell plate formation by Shibaya, Taeko, Sugawara, Yasutake

    Published in Planta (01-08-2009)
    “…Arabinogalactan proteins (AGPs) are abundant plant cell surface proteoglycans widely distributed in plant species. Since high concentrations of β-glucosyl…”
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    Journal Article
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  7. 7

    133 Development of desiccation tolerance and long-term preservation after desiccation of suspension-cultured cells of Citrus reticulata by Sugawara, Yasutake, Mukae, Kyosuke, Hatanaka, Rie, Kunitake, Hisato

    Published in Cryobiology (01-12-2013)
    “…Plant cells are able to acquire tolerance to various stresses such as freezing and desiccation when cultured under suitable controlled conditions.We previously…”
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    Involvement of arabinogalactan proteins in protonemata development from cultured cells of Marchantia polymorpha by Shibaya, Taeko, Kaneko, Yasuko, Sugawara, Yasutake

    Published in Physiologia plantarum (01-08-2005)
    “…Arabinogalactan proteins (AGPs) are abundant plant cell‐surface proteoglycans widely distributed in plant species. Crossed electrophoresis patterns of AGPs…”
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    Journal Article
  12. 12

    Ultrastructural implications of pretreatment for successful cryopreservation of Oncidium protocorm-like body by Miao, Nae-Hwey, Kaneko, Yasuko, Sugawara, Yasutake

    Published in Cryo-Letters (01-09-2005)
    “…By applying pre-treatment with high concentrations of sucrose and glycerol prior to desiccation and subsequent freezing in liquid nitrogen, successful…”
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  13. 13

    A simple and rapid method for determining cell survival in the cryopreserved shoot apex using luciferin–luciferase ATP assay by Sugawara, Yasutake, Takeuchi, Masayuki

    Published in Plant science (Limerick) (05-12-1997)
    “…A new method was developed to estimate the survival rate of cells in the shoot apex using an ATP assay with luciferin–luciferase. Shoot apices isolated as…”
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    Purification and properties of aldehyde dehydrogenase from Proteus vulgaris by Sugawara, Y, Sasaki, S

    Published in Biochimica et biophysica acta (09-02-1977)
    “…NADP-linked aldehyde dehydrogenase (aldehyde : NADP+ oxidoreductase, EC 1.2.1.4) was purified from Proteus vulgaris to the stage of homogeneity as judged by…”
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