Zobrazeno 1 - 10
of 214
pro vyhledávání: '"T, Helaakoski"'
Autor:
Schlauch D; Cellbricks GmbH, Berlin, Germany.; Leibniz University Hannover, Hannover, Germany., Ebbecke JP; Cellbricks GmbH, Berlin, Germany.; Leibniz University Hannover, Hannover, Germany., Meyer J; Leibniz University Hannover, Hannover, Germany., Fleischhammer TM; Leibniz University Hannover, Hannover, Germany., Pirmahboub H; Cellbricks GmbH, Berlin, Germany., Kloke L; Cellbricks GmbH, Berlin, Germany., Kara S; Leibniz University Hannover, Hannover, Germany., Lavrentieva A; Leibniz University Hannover, Hannover, Germany., Pepelanova I; Leibniz University Hannover, Hannover, Germany.
Publikováno v:
Biotechnology journal [Biotechnol J] 2024 Oct; Vol. 19 (10), pp. e202400393.
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
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.
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
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
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)
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
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
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
Publikováno v:
Discover Applied Sciences; Nov2024, Vol. 6 Issue 11, p1-18, 18p
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