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Collagens, modifying enzymes and their mutations in humans, flies and worms.
Myllyharju J, Kivirikko KI. Myllyharju J, et al. Among authors: kivirikko ki. Trends Genet. 2004 Jan;20(1):33-43. doi: 10.1016/j.tig.2003.11.004. Trends Genet. 2004. PMID: 14698617 Review.
Modification of vertebrate and algal prolyl 4-hydroxylases and vertebrate lysyl hydroxylase by diethyl pyrocarbonate. Evidence for histidine residues in the catalytic site of 2-oxoglutarate-coupled dioxygenases.
Myllylä R, Günzler V, Kivirikko KI, Kaska DD. Myllylä R, et al. Among authors: kivirikko ki. Biochem J. 1992 Sep 15;286 ( Pt 3)(Pt 3):923-7. doi: 10.1042/bj2860923. Biochem J. 1992. PMID: 1329722 Free PMC article.
Prolyl 4-hydroxylase and its role in collagen synthesis.
Pihlajaniemi T, Myllylä R, Kivirikko KI. Pihlajaniemi T, et al. Among authors: kivirikko ki. J Hepatol. 1991;13 Suppl 3:S2-7. doi: 10.1016/0168-8278(91)90002-s. J Hepatol. 1991. PMID: 1667665 Review.
Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase.
Pirneskoski A, Klappa P, Lobell M, Williamson RA, Byrne L, Alanen HI, Salo KE, Kivirikko KI, Freedman RB, Ruddock LW. Pirneskoski A, et al. Among authors: kivirikko ki. J Biol Chem. 2004 Mar 12;279(11):10374-81. doi: 10.1074/jbc.M312193200. Epub 2003 Dec 18. J Biol Chem. 2004. PMID: 14684740
An endoplasmic reticulum transmembrane prolyl 4-hydroxylase is induced by hypoxia and acts on hypoxia-inducible factor alpha.
Koivunen P, Tiainen P, Hyvärinen J, Williams KE, Sormunen R, Klaus SJ, Kivirikko KI, Myllyharju J. Koivunen P, et al. Among authors: kivirikko ki. J Biol Chem. 2007 Oct 19;282(42):30544-52. doi: 10.1074/jbc.M704988200. Epub 2007 Aug 27. J Biol Chem. 2007. PMID: 17726031
Many amino acid substitutions in a hypoxia-inducible transcription factor (HIF)-1alpha-like peptide cause only minor changes in its hydroxylation by the HIF prolyl 4-hydroxylases: substitution of 3,4-dehydroproline or azetidine-2-carboxylic acid for the proline leads to a high rate of uncoupled 2-oxoglutarate decarboxylation.
Li D, Hirsilä M, Koivunen P, Brenner MC, Xu L, Yang C, Kivirikko KI, Myllyharju J. Li D, et al. Among authors: kivirikko ki. J Biol Chem. 2004 Dec 31;279(53):55051-9. doi: 10.1074/jbc.M410287200. Epub 2004 Oct 12. J Biol Chem. 2004. PMID: 15485863
The peptide-substrate-binding domain of collagen prolyl 4-hydroxylases is a tetratricopeptide repeat domain with functional aromatic residues.
Pekkala M, Hieta R, Bergmann U, Kivirikko KI, Wierenga RK, Myllyharju J. Pekkala M, et al. Among authors: kivirikko ki. J Biol Chem. 2004 Dec 10;279(50):52255-61. doi: 10.1074/jbc.M410007200. Epub 2004 Sep 28. J Biol Chem. 2004. PMID: 15456751
Identification and characterization of structural domains of human ERp57: association with calreticulin requires several domains.
Silvennoinen L, Myllyharju J, Ruoppolo M, Orrù S, Caterino M, Kivirikko KI, Koivunen P. Silvennoinen L, et al. Among authors: kivirikko ki. J Biol Chem. 2004 Apr 2;279(14):13607-15. doi: 10.1074/jbc.M313054200. Epub 2004 Jan 19. J Biol Chem. 2004. PMID: 14732712
Catalytic properties of the asparaginyl hydroxylase (FIH) in the oxygen sensing pathway are distinct from those of its prolyl 4-hydroxylases.
Koivunen P, Hirsilä M, Günzler V, Kivirikko KI, Myllyharju J. Koivunen P, et al. Among authors: kivirikko ki. J Biol Chem. 2004 Mar 12;279(11):9899-904. doi: 10.1074/jbc.M312254200. Epub 2003 Dec 29. J Biol Chem. 2004. PMID: 14701857
The peptide-substrate-binding domain of human collagen prolyl 4-hydroxylases. Backbone assignments, secondary structure, and binding of proline-rich peptides.
Hieta R, Kukkola L, Permi P, Pirilä P, Kivirikko KI, Kilpeläinen I, Myllyharju J. Hieta R, et al. Among authors: kivirikko ki. J Biol Chem. 2003 Sep 12;278(37):34966-74. doi: 10.1074/jbc.M303624200. Epub 2003 Jun 24. J Biol Chem. 2003. PMID: 12824157
The Kd values determined by surface plasmon resonance and isothermal titration calorimetry for the binding of several synthetic peptides to the alpha(I) and the corresponding alpha(II) domain were very similar to the Km and Ki values for these peptides as substrates and in …
The Kd values determined by surface plasmon resonance and isothermal titration calorimetry for the binding of several synthetic peptides to …
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