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Collagens, modifying enzymes and their mutations in humans, flies and worms.
Myllyharju J, Kivirikko KI. Myllyharju J, et al. Trends Genet. 2004 Jan;20(1):33-43. doi: 10.1016/j.tig.2003.11.004. Trends Genet. 2004. PMID: 14698617 Review.
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.
Lamberg A, Helaakoski T, Myllyharju J, Peltonen S, Notbohm H, Pihlajaniemi T, Kivirikko KI. Lamberg A, et al. Among authors: myllyharju j. J Biol Chem. 1996 May 17;271(20):11988-95. doi: 10.1074/jbc.271.20.11988. J Biol Chem. 1996. PMID: 8662631
Characterization of the iron- and 2-oxoglutarate-binding sites of human prolyl 4-hydroxylase.
Myllyharju J, Kivirikko KI. Myllyharju J, et al. EMBO J. 1997 Mar 17;16(6):1173-80. doi: 10.1093/emboj/16.6.1173. EMBO J. 1997. PMID: 9135134 Free PMC article.
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.
Annunen P, Helaakoski T, Myllyharju J, Veijola J, Pihlajaniemi T, Kivirikko KI. Annunen P, et al. Among authors: myllyharju j. J Biol Chem. 1997 Jul 11;272(28):17342-8. doi: 10.1074/jbc.272.28.17342. J Biol Chem. 1997. PMID: 9211872
Expression of wild-type and modified proalpha chains of human type I procollagen in insect cells leads to the formation of stable [alpha1(I)]2alpha2(I) collagen heterotrimers and [alpha1(I)]3 homotrimers but not [alpha2(I)]3 homotrimers.
Myllyharju J, Lamberg A, Notbohm H, Fietzek PP, Pihlajaniemi T, Kivirikko KI. Myllyharju J, et al. J Biol Chem. 1997 Aug 29;272(35):21824-30. doi: 10.1074/jbc.272.35.21824. J Biol Chem. 1997. PMID: 9268313
Assembly of human prolyl 4-hydroxylase and type III collagen in the yeast pichia pastoris: formation of a stable enzyme tetramer requires coexpression with collagen and assembly of a stable collagen requires coexpression with prolyl 4-hydroxylase.
Vuorela A, Myllyharju J, Nissi R, Pihlajaniemi T, Kivirikko KI. Vuorela A, et al. Among authors: myllyharju j. EMBO J. 1997 Nov 17;16(22):6702-12. doi: 10.1093/emboj/16.22.6702. EMBO J. 1997. PMID: 9362485 Free PMC article.
Expression and characterization of recombinant human type II collagens with low and high contents of hydroxylysine and its glycosylated forms.
Nokelainen M, Helaakoski T, Myllyharju J, Notbohm H, Pihlajaniemi T, Fietzek PP, Kivirikko KI. Nokelainen M, et al. Among authors: myllyharju j. Matrix Biol. 1998 Jan;16(6):329-38. doi: 10.1016/s0945-053x(98)90004-x. Matrix Biol. 1998. PMID: 9503366
Prolyl 4-hydroxylases and their protein disulfide isomerase subunit.
Kivirikko KI, Myllyharju J. Kivirikko KI, et al. Among authors: myllyharju j. Matrix Biol. 1998 Feb;16(7):357-68. doi: 10.1016/s0945-053x(98)90009-9. Matrix Biol. 1998. PMID: 9524356 Review.
Identification of a novel proline-rich peptide-binding domain in prolyl 4-hydroxylase.
Myllyharju J, Kivirikko KI. Myllyharju J, et al. EMBO J. 1999 Jan 15;18(2):306-12. doi: 10.1093/emboj/18.2.306. EMBO J. 1999. PMID: 9889187 Free PMC article.
Evidence for 4-hydroxyproline in viral proteins. Characterization of a viral prolyl 4-hydroxylase and its peptide substrates.
Eriksson M, Myllyharju J, Tu H, Hellman M, Kivirikko KI. Eriksson M, et al. Among authors: myllyharju j. J Biol Chem. 1999 Aug 6;274(32):22131-4. doi: 10.1074/jbc.274.32.22131. J Biol Chem. 1999. PMID: 10428773
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