Correlation of the steady-state RNA levels among the α-subunit of prolyl 4-hydroxylase and the α1 and α2 chains of type I collagen during growth of chicken embryo tendon fibroblasts
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference35 articles.
1. Conversion of Proline to Collagen Hydroxyproline in a Cell-free System from Chick Embryo
2. The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen
3. Purification and partial characterization of the two nonidentical subunits of prolyl hydroxylase.
4. Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene.
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1. Cloning and Expression Analysis of the ??Subunit of Porcine Prolyl 4-hydroxylase;Asian-Australasian Journal of Animal Sciences;2007-10-30
2. Collagen Hydroxylases and the Protein Disulfide Isomerase Subunit of Prolyl 4-Hydroxylases;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22
3. Microarray analysis of retinoid-dependent gene activity during rat embryogenesis: Increased collagen fibril production in a model of retinoid insufficiency;Developmental Dynamics;2004
4. Cell density regulates prolyl 4-hydroxylase activity independent of mRNA levels;Matrix Biology;2001-01
5. Minoxidil specifically decreases the expression of lysine hydroxylase in cultured human skin fibroblasts;Biochemical Journal;1992-04-01
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