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Journal Abstract Search

344 related items for PubMed ID: 7753822

  • 21. Characterization of a novel Caenorhabditis elegans prolyl 4-hydroxylase with a unique substrate specificity and restricted expression in the pharynx and excretory duct.
    Keskiaho K, Kukkola L, Page AP, Winter AD, Vuoristo J, Sormunen R, Nissi R, Riihimaa P, Myllyharju J.
    J Biol Chem; 2008 Apr 18; 283(16):10679-89. PubMed ID: 18276589
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  • 22. Cloning of the alpha subunit of prolyl 4-hydroxylase from Drosophila and expression and characterization of the corresponding enzyme tetramer with some unique properties.
    Annunen P, Koivunen P, Kivirikko KI.
    J Biol Chem; 1999 Mar 05; 274(10):6790-6. PubMed ID: 10037780
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  • 23. Prolyl 4-hydroxylase: molecular cloning and the primary structure of the alpha subunit from chicken embryo.
    Bassuk JA, Kao WW, Herzer P, Kedersha NL, Seyer J, DeMartino JA, Daugherty BL, Mark GE, Berg RA.
    Proc Natl Acad Sci U S A; 1989 Oct 05; 86(19):7382-6. PubMed ID: 2552442
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  • 24. Characterization of the human and mouse genes for the alpha subunit of type II prolyl 4-hydroxylase. Identification of a previously unknown alternatively spliced exon and its expression in various tissues.
    Nokelainen M, Nissi R, Kukkola L, Helaakoski T, Myllyharju J.
    Eur J Biochem; 2001 Oct 05; 268(20):5300-9. PubMed ID: 11606192
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  • 25. Three binding sites in protein-disulfide isomerase cooperate in collagen prolyl 4-hydroxylase tetramer assembly.
    Koivunen P, Salo KE, Myllyharju J, Ruddock LW.
    J Biol Chem; 2005 Feb 18; 280(7):5227-35. PubMed ID: 15590633
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  • 27. Characterization of a second Arabidopsis thaliana prolyl 4-hydroxylase with distinct substrate specificity.
    Tiainen P, Myllyharju J, Koivunen P.
    J Biol Chem; 2005 Jan 14; 280(2):1142-8. PubMed ID: 15528200
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  • 29. Prolyl 4-hydroxylase is an essential procollagen-modifying enzyme required for exoskeleton formation and the maintenance of body shape in the nematode Caenorhabditis elegans.
    Winter AD, Page AP.
    Mol Cell Biol; 2000 Jun 14; 20(11):4084-93. PubMed ID: 10805750
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  • 30. The peptide-substrate-binding domain of human collagen prolyl 4-hydroxylases. Backbone assignments, secondary structure, and binding of proline-rich peptides.
    Hieta R, Kukkola L, Permi P, Pirilä P, Kivirikko KI, Kilpeläinen I, Myllyharju J.
    J Biol Chem; 2003 Sep 12; 278(37):34966-74. PubMed ID: 12824157
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  • 32. Cloning of a novel prolyl 4-hydroxylase subunit expressed in the fibrous cap of human atherosclerotic plaque.
    Van Den Diepstraten C, Papay K, Bolender Z, Brown A, Pickering JG.
    Circulation; 2003 Aug 05; 108(5):508-11. PubMed ID: 12874193
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  • 35. Differences in collagen prolyl 4-hydroxylase assembly between two Caenorhabditis nematode species despite high amino acid sequence identity of the enzyme subunits.
    Winter AD, Keskiaho K, Kukkola L, McCormack G, Felix MA, Myllyharju J, Page AP.
    Matrix Biol; 2007 Jun 05; 26(5):382-95. PubMed ID: 17321733
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  • 37. High-level production of human collagen prolyl 4-hydroxylase in Escherichia coli.
    Neubauer A, Neubauer P, Myllyharju J.
    Matrix Biol; 2005 Feb 05; 24(1):59-68. PubMed ID: 15749002
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  • 38. Collagen prolyl 4-hydroxylase tetramers and dimers show identical decreases in Km values for peptide substrates with increasing chain length: mutation of one of the two catalytic sites in the tetramer inactivates the enzyme by more than half.
    Kukkola L, Koivunen P, Pakkanen O, Page AP, Myllyharju J.
    J Biol Chem; 2004 Apr 30; 279(18):18656-61. PubMed ID: 14985345
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  • 39. The structural motifs for substrate binding and dimerization of the α subunit of collagen prolyl 4-hydroxylase.
    Anantharajan J, Koski MK, Kursula P, Hieta R, Bergmann U, Myllyharju J, Wierenga RK.
    Structure; 2013 Dec 03; 21(12):2107-18. PubMed ID: 24207127
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  • 40. Site-directed mutagenesis of the alpha subunit of human prolyl 4-hydroxylase. Identification of three histidine residues critical for catalytic activity.
    Lamberg A, Pihlajaniemi T, Kivirikko KI.
    J Biol Chem; 1995 Apr 28; 270(17):9926-31. PubMed ID: 7730375
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