Zobrazeno 1 - 10 of 60 pro vyhledávání: '"K. I. Kivirikko"'
1
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
Autor: Timo Hautala, Raili Myllylä, M. Suokas, L Pajunen, K. I. Kivirikko, B. Tebbe, S. Kellokumpu
Publikováno v: DNA and Cell Biology. 17:117-123
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 enzyme required for the post-translational processing of collagens. We have characterized a
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::feddedfe3149e628aed085c264f3ae59
https://doi.org/10.1089/dna.1998.17.117
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2
Markers of collagen and basement membrane metabolism in sera of patients with progressive systemic sclerosis
Autor: K I Kivirikko, V A Nassonova, Leila Risteli, J V Chochlova, N G Guseva, R Myllylä, Juha Risteli, N V Anikina
Publikováno v: Annals of the Rheumatic Diseases. 50:481-486
The concentrations of the amino terminal propeptide of type III procollagen, the 7S domain of type IV collagen, and the fragment P1 of laminin (PIIINP, 7S, and P1 respectively) and the activity of galactosylhydroxylysyl glucosyltransferase (GGT) in s
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c90af2f9c52fa7c1cc395310c4d95ca4
https://doi.org/10.1136/ard.50.7.481
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3
Domains b' and a' of protein disulfide isomerase fulfill the minimum requirement for function as a subunit of prolyl 4-hydroxylase. The N-terminal domains a and b enhances this function and can be substituted in part by those of ERp57
Autor: A, Pirneskoski, L W, Ruddock, P, Klappa, R B, Freedman, K I, Kivirikko, P, Koivunen
Publikováno v: The Journal of biological chemistry. 276(14)
Protein disulfide isomerase (PDI) is a modular polypeptide consisting of four domains, a, b, b', and a', plus an acidic C-terminal extension, c. PDI carries out multiple functions, acting as the beta subunit in the animal prolyl 4-hydroxylases and in
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::56a9caf203962556d47f142bb5685436
https://pubmed.ncbi.nlm.nih.gov/11134056
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4
Evidence for 4-hydroxyproline in viral proteins. Characterization of a viral prolyl 4-hydroxylase and its peptide substrates
Autor: M, Eriksson, J, Myllyharju, H, Tu, M, Hellman, K I, Kivirikko
Publikováno v: The Journal of biological chemistry. 274(32)
4-Hydroxyproline, the characteristic amino acid of collagens and collagen-like proteins in animals, is also found in certain proline-rich proteins in plants but has been believed to be absent from viral and bacterial proteins. We report here on the c
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::dd346f24e31ccdb6975ae886665f9a7e
https://pubmed.ncbi.nlm.nih.gov/10428773
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6
Collagen hydroxylases and the protein disulfide isomerase subunit of prolyl 4-hydroxylases
Autor: K I, Kivirikko, T, Pihlajaniemi
Publikováno v: Advances in enzymology and related areas of molecular biology. 72
Prolyl 4-hydroxylases catalyze the formation of 4-hydroxyproline in collagens and other proteins with an appropriate collagen-like stretch of amino acid residues. The enzyme requires Fe(II), 2-oxoglutarate, molecular oxygen, and ascorbate. This revie
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::492da49a0b04147f0bb2c5a0048ac6bc
https://pubmed.ncbi.nlm.nih.gov/9559057
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7
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
Autor: P, Annunen, T, Helaakoski, J, Myllyharju, J, Veijola, T, Pihlajaniemi, K I, Kivirikko
Publikováno v: The Journal of biological chemistry. 272(28)
Prolyl 4-hydroxylase (proline hydroxylase, EC 1.14.11.2) catalyzes the formation of 4-hydroxyproline in collagens. The vertebrate enzyme is an alpha2beta2 tetramer, the beta subunit of which is identical to protein disulfide-isomerase (PDI, EC 5.3.4.
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::720b95f8e5ae1d0d87eba541acafd324
https://pubmed.ncbi.nlm.nih.gov/9211872
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8
Duplication of seven exons in the lysyl hydroxylase gene is associated with longer forms of a repetitive sequence within the gene and is a common cause for the type VI variant of Ehlers-Danlos syndrome
Autor: J, Heikkinen, T, Toppinen, H, Yeowell, T, Krieg, B, Steinmann, K I, Kivirikko, R, Myllylä
Publikováno v: American journal of human genetics. 60(1)
The type VI variant of the Ehlers-Danlos syndrome (EDS) is a recessively inherited connective tissue disorder which, in most families, is due to a deficiency in lysyl hydroxylase activity. We have recently characterized a homozygous duplication of 8.
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::57b0aa8d73b4fd7f86ad22e86fcac29e
https://pubmed.ncbi.nlm.nih.gov/8981946
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9
Involvement of prolyl 4-hydroxylase in the assembly of trimeric minicollagen XII. Study in a baculovirus expression system
Autor: M, Mazzorana, A, Snellman, K I, Kivirikko, M, van der Rest, T, Pihlajaniemi
Publikováno v: The Journal of biological chemistry. 271(46)
We have shown previously that hydroxylation played a critical role in the trimer assembly and disulfide bonding of the three constituent alpha chains of a minicollagen composed of the extreme C-terminal collagenous (COL1) and noncollagenous (NC1) dom
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d13f32556afab617e012fe0bb0c85d14
https://pubmed.ncbi.nlm.nih.gov/8910551
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10
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
Autor: A, Lamberg, T, Helaakoski, J, Myllyharju, S, Peltonen, H, Notbohm, T, Pihlajaniemi, K I, Kivirikko
Publikováno v: The Journal of biological chemistry. 271(20)
An efficient expression system for recombinant collagens would have numerous scientific and practical applications. Nevertheless, most recombinant systems are not suitable for this purpose, as they do not have sufficient amounts of prolyl 4-hydroxyla
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::367ead050b0c76cb62cd15f70a206082
https://pubmed.ncbi.nlm.nih.gov/8662631
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