Search Results - "Annunen, P"

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    The Novel Type II Prolyl 4-Hydroxylase Is the Main Enzyme Form in Chondrocytes and Capillary Endothelial Cells, whereas the Type I Enzyme Predominates in Most Cells by Annunen, P, Autio-Harmainen, H, Kivirikko, K I

    Published in The Journal of biological chemistry (13-03-1998)
    “…Procollagen-proline dioxygenase (EC 1.14.11.2 ), an α 2 β 2 tetramer in vertebrates, plays a central role in the synthesis of all collagens. Recently an…”
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    Cloning of the alpha subunit or prolyl 4-hydroxylase from Drosophila and expression and characterization of the corresponding enzyme tetramer with some unique properties by Annunen, P, Koivunen, P, Kivirikko, K.I

    Published in The Journal of biological chemistry (05-03-1999)
    “…Prolyl 4-hydroxylase catalyzes the formation of 4-hydroxyproline in collagens. The vertebrate enzymes are alpha2beta2 tetramers, whereas the Caenorhabditis…”
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    Journal Article
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    ERp60 does not substitute for protein disulphide isomerase as the beta-subunit of prolyl 4-hydroxylase by Koivunen, P, Helaakoski, T, Annunen, P, Veijola, J, Räisänen, S, Pihlajaniemi, T, Kivirikko, K I

    Published in Biochemical journal (01-06-1996)
    “…Prolyl 4-hydroxylase (EC 1.14.11.2) catalyses the formation of 4-hydroxyproline in collagens. The vertebrate enzymes are alpha 2 beta 2 tetramers while the…”
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    Journal Article
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    Baculovirus expression of two protein disulphide isomerase isoforms from Caenorhabditis elegans and characterization of prolyl 4-hydroxylases containing one of these polypeptides as their beta subunit by Veijola, J, Annunen, P, Koivunen, P, Page, A P, Pihlajaniemi, T, Kivirikko, K I

    Published in Biochemical journal (01-08-1996)
    “…Protein disulphide isomerase (PDI; EC 5.3.4.1) is a multifunctional polypeptide that is identical to the beta subunit of prolyl 4-hydroxylases. We report here…”
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    Journal Article
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