Cyclophilin-B Modulates Collagen Cross-linking by Differentially Affecting Lysine Hydroxylation in the Helical and Telopeptidyl Domains of Tendon Type I Collagen.
Terajima M, Taga Y, Chen Y, Cabral WA, Hou-Fu G, Srisawasdi S, Nagasawa M, Sumida N, Hattori S, Kurie JM, Marini JC, Yamauchi M.
Terajima M, et al. Among authors: yamauchi m.
J Biol Chem. 2016 Apr 29;291(18):9501-12. doi: 10.1074/jbc.M115.699470. Epub 2016 Mar 2.
J Biol Chem. 2016.
PMID: 26934917
Free PMC article.
A recent study on cyclophilin B (CypB) null mice, a model of recessive osteogenesis imperfecta, demonstrated that lysine hydroxylation at the helical cross-linking site of bone type I collagen was diminished in these animals (Cabral, W. A., Perdivara, I., Weis, M., Terajim …
A recent study on cyclophilin B (CypB) null mice, a model of recessive osteogenesis imperfecta, demonstrated that lysine hydroxylation at th …