Search Results - "Helaakoski, T"

A single polypeptide acts both as the beta subunit of prolyl 4-hydroxylase and as a protein disulfide-isomerase by Koivu, J, Myllylä, R, Helaakoski, T, Pihlajaniemi, T, Tasanen, K, Kivirikko, K I

“…A single polypeptide is shown to act both as the beta subunit of the proline hydroxylase (EC 1.14.11.2) and as a protein disulfide-isomerase (EC 5.3.4.1). When…”
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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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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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Tissue-specific expression of the mouse alpha 2(I) collagen promoter. Studies in transgenic mice and in tissue culture cells by Goldberg, H, Helaakoski, T, Garrett, L A, Karsenty, G, Pellegrino, A, Lozano, G, Maity, S, de Crombrugghe, B

“…We sought to determine the cis-acting elements responsible for the pattern of tissue specific expression of the mouse alpha 2(I) collagen gene. Using an RNase…”
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Characterization of recombinant type II collagen: arthritogenicity and tolerogenicity in DBA/1 mice by Myers, L K, Brand, D D, Ye, X J, Cremer, M A, Rosloniec, E F, Bodo, M, Myllyharju, J, Helaakoski, T, Nokelainen, M, Pihlajaniemi, T, Kivirikko, K, Yang, C L, Ala-Kokko, L, Prockop, D J, Notbohm, H, Fietzek, P, Stuart, J M, Kang, A H

“…Recombinant human type II collagen (rhCII) was produced using both the HT1080 mammalian cell expression system (rhCIIht) and a baculovirus expression system…”
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Structure and expression of the human gene for the alpha subunit of prolyl 4-hydroxylase. The two alternatively spliced types of mRNA correspond to two homologous exons the sequences of which are expressed in a variety of tissues by Helaakoski, T, Veijola, J, Vuori, K, Rehn, M, Chow, L T, Taillon-Miller, P, Kivirikko, K I, Pihlajaniemi, T

“…Prolyl 4-hydroxylase, an alpha 2 beta 2 tetramer, plays a central role in collagen synthesis as it catalyzes the formation of 4-hydroxyproline residues by the…”
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Cloning, baculovirus expression, and characterization of a second mouse prolyl 4-hydroxylase alpha-subunit isoform: formation of an alpha 2 beta 2 tetramer with the protein disulfide-isomerase/beta subunit by Helaakoski, T, Annunen, P, Vuori, K, MacNeil, I A, Pihlajaniemi, T, Kivirikko, K I

“…Prolyl 4-hydroxylase (EC 1.14.11.2) catalyzes the posttranslational formation of 4-hydroxyproline in collagens. The vertebrate enzyme is an alpha 2 beta 2…”
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Matrix metalloproteinase-8 is expressed in rheumatoid synovial fibroblasts and endothelial cells. Regulation by tumor necrosis factor-alpha and doxycycline by Hanemaaijer, R, Sorsa, T, Konttinen, Y T, Ding, Y, Sutinen, M, Visser, H, van Hinsbergh, V W, Helaakoski, T, Kainulainen, T, Rönkä, H, Tschesche, H, Salo, T

“…Neutrophil collagenase (matrix metalloproteinase-8 or MMP-8) is regarded as being synthesized exclusively by polymorphonuclear neutrophils (PMN). However, in…”
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Increases in mRNA concentrations of the alpha and beta subunits of prolyl 4-hydroxylase accompany increased gene expression of type IV collagen during differentiation of mouse F9 cells by HELAAKOSKI, T, PAJUNEN, L, KIVIRIKKO, K. I, PIHLAJANIEMI, T

“…Mouse F9 teratocarcinoma stem cells differentiate in monolayer cultures in the presence of retinoic acid, dibutyryl cAMP, and isobutyl methylxanthine. This…”
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Specific inactivation of prolyl 4-hydroxylase and inhibition of collagen synthesis by oxaproline-containing peptides in cultured human skin fibroblasts by KARVONEN, K, ALA-KOKKO, L, PIHLAJANIEMI, T, HELAAKOSKI, T, HENKE, S, GÜNZLER, V, KIVIRIKKO, K. I, SAVOLAINEN, E.-R

“…The crucial role of collagen in fibrotic disorders has prompted attempts to develop drugs that inhibit collagen accumulation. Peptides containing the…”
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Assignment of the gene coding for both the beta-subunit of prolyl 4-hydroxylase and the enzyme disulfide isomerase to human chromosome region 17p11----qter by Pajunen, L, Myllylä, R, Helaakoski, T, Pihlajaniemi, T, Tasanen, K, Höyhtyä, M, Tryggvason, K, Solomon, E, Kivirikko, K I

“…The chromosomal location of the human gene coding for both the beta-subunit of prolyl 4-hydroxylase (P4HB) and the enzyme disulfide isomerase (PDI) was…”
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Characterization of human type III collagen expressed in a baculovirus system. Production of a protein with a stable triple helix requires coexpression with the two types of recombinant prolyl 4-hydroxylase subunit by Lamberg, A, Helaakoski, T, Myllyharju, J, Peltonen, S, Notbohm, H, Pihlajaniemi, T, Kivirikko, K I

“…An efficient expression system for recombinant collagens would have numerous scientific and practical applications. Nevertheless, most recombinant systems are…”
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The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide by Koivunen, Peppi, Pirneskoski, Annamari, Karvonen, Päivi, Ljung, Johanna, Helaakoski, Tarja, Notbohm, Holger, Kivirikko, Kari I.

“…Protein disulfide isomerase (PDI) is a multifunctional polypeptide that acts as a subunit in the animal prolyl 4‐hydroxylases and the microsomal triglyceride…”
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Expression and characterization of recombinant human type II collagens with low and high contents of hydroxylysine and its glycosylated forms by Nokelainen, Minna, Helaakoski, Tarja, Myllyharju, Johanna, Notbohm, Holger, Pihlajaniemi, Taina, Fietzek, Peter P., Kivirikko, Kari I.

“…Insect cells coinfected with two baculoviruses, one coding for the proα chains of human type II procollagen and the other for both the α and β subunits of…”
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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

“…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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Tissue-specific expression of the mouse α2(I) collagen promoter : studies in transgenic mice and in tissue culture cells by GOLDBERG, H, HELAAKOSKI, T, GARRETT, L. A, KARSENTY, G, PELLEGRINO, A, LOZANO, G, MAITY, S, DE CROMBRUGGHE, B

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Complete exon–intron organization of the gene for human lysyl hydroxylase 3 (LH3) by Rautavuoma, Kati, Passoja, Kaisa, Helaakoski, Tarja, Kivirikko, Kari I.

“…Lysyl hydroxylase (LH) catalyzes the formation of hydroxylysine in collagens and related proteins by the hydroxylation of lysine residues in peptide linkages…”
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Structures of the Human Gene for the Protein Disulfide Isomerase-Related Polypeptide ERp60 and a Processed Gene and Assignment of These Genes to 15q15 and 1q21 by Koivunen, Peppi, Horelli-Kuitunen, Nina, Helaakoski, Tarja, Karvonen, Päivi, Jaakkola, Marko, Palotie, Aarno, Kivirikko, Kari I.

“…ERp60 (also known as ERp61 or GRP58) is an isoform of protein disulfide isomerase (PDI) that has two thioredoxin-like domainsaanda′ in positions corresponding…”
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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 by Nokelainen, M, Nissi, R, Kukkola, L, Helaakoski, T, Myllyharju, J

“…Prolyl 4-hydroxylase (4-PH) catalyzes the formation of 4-hydroxyproline in -X-Pro-Gly- sequences and has a central role in the synthesis of all collagens. We…”
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Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) and characterization of the type II enzyme tetramer. The alpha(I) and alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer by Annunen, P, Helaakoski, T, Myllyharju, J, Veijola, J, Pihlajaniemi, T, Kivirikko, K I

“…Prolyl 4-hydroxylase (proline hydroxylase, EC 1.14.11.2) catalyzes the formation of 4-hydroxyproline in collagens. The vertebrate enzyme is an alpha2beta2…”
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