Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Kati Rautavuoma"'
Autor:
Kati Rautavuoma, Johanna Myllyharju, Asta Pirskanen, Kaisa Passoja, Kati Takaluoma, Ari-Pekka Kvist, Kari I. Kivirikko
Publikováno v:
Journal of Biological Chemistry. 277:23084-23091
Lysyl hydroxylase (LH) catalyzes the formation of hydroxylysine in collagens; three human isoenzymes have been cloned so far. We report here on the purification of all three recombinant isoenzymes to homogeneity from the medium of cultured insect cel
Publikováno v:
Proceedings of the National Academy of Sciences. 95:10482-10486
Lysyl hydroxylase (EC 1.14.11.4 ), a homodimer, catalyzes the formation of hydroxylysine in collagens. Recently, an isoenzyme termed lysyl hydroxylase 2 has been cloned from human sources [M. Valtavaara, H. Papponen, A.-M. Pirttilä, K. Hiltunen, H.
Autor:
Maija Hirsilä, Annika Pasanen, Johanna Myllyharju, Kari I. Kivirikko, Minna Heikkilä, Kati Rautavuoma
Publikováno v:
The international journal of biochemistrycell biology. 42(7)
The hypoxia-inducible transcription factors (HIFs) play a central role in the response of cells to hypoxia. HIFs are alphabeta dimers, the human alpha subunit having three isoforms. HIF-3alpha is unique among the HIF-alpha isoforms in that its gene i
Publikováno v:
Matrix biology : journal of the International Society for Matrix Biology. 19(1)
Lysyl hydroxylase (LH) catalyzes the formation of hydroxylysine in collagens and related proteins by the hydroxylation of lysine residues in peptide linkages. Three isoenzymes of LH have so far been characterized. We report here that the human LH3 ge