Prolyl 4-hydroxylases, the key enzymes of collagen biosynthesis
Author:
Publisher
Elsevier BV
Subject
Molecular Biology
Reference59 articles.
1. Prolyl 4-hydroxylase α-related proteins in Drosophila melanogaster: tissue-specific embryonic expression of the 99F8-9 cluster;Abrams;Mech. Dev.,2002
2. The NC1/endostatin domain of Caenorhabditis elegans type XVIII collagen affects cell migration and axon guidance;Ackley;J. Cell Biol.,2001
3. Cloning of the human prolyl 4-hydroxylase α subunit isoform α(II) and characterization of the type II enzyme tetramer. The α(I) and α(II) subunits do not form a mixed α(I)α(II)β2 tetramer;Annunen;J. Biol. Chem.,1997
4. The novel type II prolyl 4-hydroxylase is the main enzyme form in chondrocytes and capillary endothelial cells, whereas the type I enzyme predominates in most cells;Annunen;J. Biol. Chem.,1998
5. Cloning of the α subunit of prolyl 4-hydroxylase from Drosophila and expression and characterization of the corresponding enzyme tetramer with some unique properties;Annunen;J. Biol. Chem.,1999
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