Search Results - "Kivirikko, K.I"

Site‐directed mutagenesis of human protein disulphide isomerase: effect on the assembly, activity and endoplasmic reticulum retention of human prolyl 4‐hydroxylase in Spodoptera frugiperda insect cells by Vuori, K., Pihlajaniemi, T., Myllylä, R., Kivirikko, K.I.

“…Protein disulphide isomerase (PDI) is a highly unusual multifunctional polypeptide, identical to the beta‐subunit of prolyl 4‐hydroxylase. It has two…”
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Promoter of the gene for the multifunctional protein disulfide isomerase polypeptide. Functional significance of the six CCAAT boxes and other promoter elements by TASANEN, K, OIKARINEN, J, KIVIRIKKO, K. I, PIHLAJANIEMI, T

“…Protein disulfide isomerase (PDI) is a highly unusual multifunctional polypeptide that is identical to the beta-subunit of prolyl 4-hydroxylase, a cellular…”
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Expression of a human cartilage procollagen gene (COL2A1) in mouse 3T3 cells by ALA-KOKKO, L, HYLAND, J, SMITH, C, KIVIRIKKO, K. I, JIMENEZ, S. A, PROCKOP, D. J

“…Expression in a recombinant system has been difficult to obtain for any of the major fibrillar collagens that require processing by eight or more…”
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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

“…Prolyl 4-hydroxylase catalyzes the formation of 4-hydroxyproline in collagens. The vertebrate enzymes are alpha2beta2 tetramers, whereas the Caenorhabditis…”
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Expression and site-directed mutagenesis of human protein disulfide isomerase in Escherichia coli. This multifunctional polypeptide has two independently acting catalytic sites for the isomerase activity by Vuori, K, Myllylä, R, Pihlajaniemi, T, Kivirikko, K I

“…Protein disulfide isomerase (PDI, EC 5.3.4.1) is a highly unusual multifunctional polypeptide, being identical to the beta subunit of prolyl 4-hydroxylase, a…”
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Molecular cloning of the beta‐subunit of human prolyl 4‐hydroxylase. This subunit and protein disulphide isomerase are products of the same gene by Pihlajaniemi, T., Helaakoski, T., Tasanen, K., Myllylä, R., Huhtala, M.L., Koivu, J., Kivirikko, K.I.

“…Prolyl 4‐hydroxylase (EC 1.14.11.2), an alpha 2 beta 2 tetramer, catalyses the formation of 4‐hydroxyproline in collagens by the hydroxylation of proline…”
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Mutations That Destabilize the a′ Domain of Human Protein-disulfide Isomerase Indirectly Affect Peptide Binding by Klappa, P., Koivunen, P., Pirneskoski, A., Karvonen, P., Ruddock, L.W., Kivirikko, K.I., Freedman, R.B.

“…Protein-disulfide isomerase (PDI) is a catalyst of folding of disulfide-bonded proteins and also a multifunctional polypeptide that acts as the β-subunit in…”
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Expression of recombinant human type I-III collagens in the yeast pichia pastoris by Myllyharju, J, Nokelainen, M, Vuorela, A, Kivirikko, K I

“…An efficient expression system for recombinant human collagens will have numerous scientific and medical applications. However, most recombinant systems are…”
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Molecular Cloning of the α -Subunit of Human Prolyl 4-hydroxylase: The Complete cDNA-Derived Amino Acid Sequence and Evidence for Alternative Splicing of RNA Transcripts by Helaakoski, Tarja, Vuori, Kristina, Myllyla, Raili, Kivirikko, Kari I., Pihlajaniemi, Taina

“…Prolyl 4-hydroxylase [procollagen-proline, 2-oxoglutarate 4-dioxygenase; procollagen-L-proline, 2-oxoglutarate:oxygen oxidoreductase (4-hydroxylating), EC…”
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Site-directed mutagenesis of human lysyl hydroxylase expressed in insect cells by Pirskanen, A., Kaimio, A.-M., Myllylä, R., Kivirikko, K.I.

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A large duplication in the gene for lysyl hydroxylase accounts for the type VI variant of Ehlers-Danlos syndrome in two siblings by Hautala, T, Heikkinen, J, Kivirikko, K I, Myllylä, R

“…Ehlers-Danlos syndrome is a heterogeneous disorder characterized by joint hypermobility, skin hyperextensibility, fragility, and other signs of connective…”
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Structure and expression of the human lysyl hydroxylase gene (PLOD): introns 9 and 16 contain Alu sequences at the sites of recombination in Ehlers-Danlos syndrome type VI patients by Heikkinen, J, Hautala, T, Kivirikko, K I, Myllylä, R

“…Lysyl hydroxylase (EC 1.14.11.4) catalyzes the formation of hydroxylysine in collagens by the hydroxylation of lysine residues in peptide linkages. This enzyme…”
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A fourth example suggests that premature termination codons in the COL2A1 gene are a common cause of the Stickler syndrome: analysis of the COL2A1 gene by denaturing gradient gel electrophoresis by Ritvaniemi, P, Hyland, J, Ignatius, J, Kivirikko, K I, Prockop, D J, Ala-Kokko, L

“…A series of oligonucleotide primers was designed to generate polymerase chain reaction products that contained exons 6 to 49 of the human gene for type II…”
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Expression of mRNAs for Lysyl Oxidase and Type III Procollagen in Cultured Fibroblasts from Patients with the Menkes and Occipital Horn Syndromes as Determined by Quantitative Polymerase Chain Reaction by Kemppainen, R., Hämäläinen, E.-R., Kuivaniemi, H., Tromp, G., Pihlajaniemi, T., Kivirikko, K.I.

“…The Menkes syndrome and the occipital horn syndrome are two X-linked recessively inherited disorders characterized by abnormalities in copper metabolism. These…”
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Chain association and trimer formation of type XIII collagen by Snellman, A., Keränen, M.-R., Väisänen, T., Sormunen, R., Lamber, A., Kivirikko, K.I., Pihlajaniemi, T.

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Structure of the human lysyl oxidase gene by Hämäläinen, E R, Kemppainen, R, Pihlajaniemi, T, Kivirikko, K I

“…Lysyl oxidase (EC 1.4.3.13), an extracellular copper enzyme, initiates the crosslinking of collagens and elastin by catalyzing oxidative deamination of the…”
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Molecular cloning of chick lysyl hydroxylase. Little homology in primary structure to the two types of subunit of prolyl 4-hydroxylase by Myllyla, R. (University of Oulu, Oulu, Finland), Pihlajaniemi, T, Pajunen, L, Turpeenniemi-Hujanen, T, Kivirikko, K.I

“…Lysyl hydroxylase (EC 1.14.11.4), an alpha 2 dimer, catalyzes the formation of hydroxylysine in collagens by the hydroxylation of lysine residues in X-Lys-Gly…”
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A splice-site mutation that induces exon skipping and reduction in lysyl hydroxylase mRNA levels but does not create a nonsense codon in Ehlers-Danlos syndrome type VI by Pajunen, L, Suokas, M, Hautala, T, Kellokumpu, S, Tebbe, B, Kivirikko, K I, Myllylä, R

“…The type VI variant of Ehlers-Danlos syndrome (EDS) is a heritable connective tissue disorder caused by a deficiency in the activity of lysyl hydroxylase, an…”
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Prolyl 4-hydroxylase from Volvox carteri. A low-Mr enzyme antigenically related to the alpha subunit of the vertebrate enzyme by Kaska, D.D, Myllyla, R, Gunzler, V, Gibor, A, Kivirikko, K.I

“…Prolyl 4-hydroxylase was isolated in a highly purified form from a multi-cellular green alga, Volvox carteri, by a procedure consisting of ion-exchange…”
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Purification and characterization of protein disulphide-isomerase from the unicellular green alga Chlamydomonas reinhardii. A 120 kDa dimer antigenically distinct from the vertebrate enzyme by Kaska, D.D, Kivirikko, K.I, Myllyla, R

“…Protein disulphide-isomerase (PDI) has been isolated from the unicellular green alga Chlamydomonas reinhardii and purified by (NH4)2SO4 precipitation, gel…”
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