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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...
Kaydedildi:
| Yayımlandı: | J Biol Chem |
|---|---|
| Asıl Yazarlar: | , , , , , , , , , , , |
| Materyal Türü: | Artigo |
| Dil: | Inglês |
| Baskı/Yayın Bilgisi: |
American Society for Biochemistry and Molecular Biology
2016
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| Konular: | |
| Online Erişim: | 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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