Výsledky vyhledávání - "T, Helaakoski"

Tissue-specific expression of the mouse alpha 2(I) collagen promoter. Studies in transgenic mice and in tissue culture cells

Autor: Gerard Karsenty, Guillermina Lozano, L A Garrett, T Helaakoski, H Goldberg, A Pellegrino, Sankar N. Maity, B de Crombrugghe

Publikováno v: Journal of Biological Chemistry. 267:19622-19630

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 protection assay we first verified that expression of the alpha 2(I) collagen gene is mainl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::53a6fc9ec0d12687e15d057efa64ec18
https://doi.org/10.1016/s0021-9258(18)41820-0

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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

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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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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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

Autor: T, Helaakoski, J, Veijola, K, Vuori, M, Rehn, L T, Chow, P, Taillon-Miller, K I, Kivirikko, T, Pihlajaniemi

Publikováno v: The Journal of biological chemistry. 269(45)

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 hydroxylation of proline in X-Pro-Gly sequences. We report here that the human gene for the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a00b93d1c573eea702e4b534bfb8d944
https://pubmed.ncbi.nlm.nih.gov/7961714

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Tissue-specific expression of the mouse alpha 2(I) collagen promoter. Studies in transgenic mice and in tissue culture cells

Autor: H, Goldberg, T, Helaakoski, L A, Garrett, G, Karsenty, A, Pellegrino, G, Lozano, S, Maity, B, de Crombrugghe

Publikováno v: The Journal of biological chemistry. 267(27)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a400952db888a55cde5558e2f0a30d28
https://pubmed.ncbi.nlm.nih.gov/1527081

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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

Autor: T, Helaakoski, L, Pajunen, K I, Kivirikko, T, Pihlajaniemi

Publikováno v: The Journal of biological chemistry. 265(20)

Mouse F9 teratocarcinoma stem cells differentiate in monolayer cultures in the presence of retinoic acid, dibutyryl cAMP, and isobutyl methylxanthine. This differentiation is associated with a marked increase in the synthesis rates and mRNA concentra

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::dd85b0f14157332030a22074126d63b4
https://pubmed.ncbi.nlm.nih.gov/1694844

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Specific inactivation of prolyl 4-hydroxylase and inhibition of collagen synthesis by oxaproline-containing peptides in cultured human skin fibroblasts

Autor: K, Karvonen, L, Ala-Kokko, T, Pihlajaniemi, T, Helaakoski, S, Henke, V, Günzler, K I, Kivirikko, E R, Savolainen

Publikováno v: The Journal of biological chemistry. 265(15)

The crucial role of collagen in fibrotic disorders has prompted attempts to develop drugs that inhibit collagen accumulation. Peptides containing the unphysiological amino acid 5-oxaproline (Opr) have recently been found to act as specific syncatalyt

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::741766b00c7170c0099aec3be0cf502e
https://pubmed.ncbi.nlm.nih.gov/2160457

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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

Autor: Ellen Solomon, L Pajunen, T. Pihlajaniemi, T. Helaakoski, M. Höyhtyä, Kaisa Tasanen, K.I. Kivirikko, Karl Tryggvason, R. Myllyla

Publikováno v: Cytogenetics and cell genetics. 47(1-2)

The chromosomal location of the human gene coding for both the β-subunit of prolyl 4-hydroxylase (P4HB) and the enzyme disulfide isomerase (PDI) was determined using mouse × human somatic cell hybrids and three different methods for identifying eit

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa588515248f3fb9915a3d8ed6bdd355
https://pubmed.ncbi.nlm.nih.gov/2833378

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