Cyclophilin-B Modulates Collagen Cross-linking by Differentially Affecting Lysine Hydroxylation in the Helical and Telopeptidyl Domains of Tendon Type I Collagen

Covalent intermolecular cross-linking provides collagen fibrils with stability. The cross-linking chemistry is tissue-specific and determined primarily by the state of lysine hydroxylation at specific sites. A recent study on cyclophilin B (CypB) null mice, a model of recessive osteogenesis imperfec...

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Detalhes bibliográficos
Publicado no:J Biol Chem
Main Authors: Terajima, Masahiko, Taga, Yuki, Chen, Yulong, Cabral, Wayne A., Hou-Fu, Guo, Srisawasdi, Sirivimol, Nagasawa, Masako, Sumida, Noriko, Hattori, Shunji, Kurie, Jonathan M., Marini, Joan C., Yamauchi, Mitsuo
Formato: Artigo
Idioma:Inglês
Publicado em: American Society for Biochemistry and Molecular Biology 2016
Assuntos:
Glycobiology and Extracellular Matrices
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC4850290/
https://ncbi.nlm.nih.gov/pubmed/26934917
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M115.699470
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