Trimerization of collagen IX α-chains does not require the presence of the COL1 and NC1 domains
نویسندگان
چکیده
Juha JÄÄLINOJA*, Joni YLÖSTALO*†, William BECKETT†1, David J. S. HULMES‡ and Leena ALA-KOKKO*§2 *Collagen Research Unit, Biocenter and Department of Medical Biochemistry and Molecular Biology, Oulu University, P.O. Box 5000, 90014 Oulu, Finland, †Center for Gene Therapy, Tulane University Health Sciences Center, New Orleans, LA, U.S.A., ‡Institut de Biologie et Chimie des Protéines, CNRS/Université Claude Bernard Lyon 1, UMR 5086, IFR 128 Biosciences Lyon-Gerland, Lyon, France, and §Connective Tissue Gene Tests, Allentown, PA, U.S.A.
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A Newly Identified Site of Cross-linking between Collagens Ix and Ii: Insights on Molecular Assembly in Cartilage
Introduction The collagenous framework of articular cartilage matures from a covalently cross-linked heteropolymer of types II, IX and XI collagens. Type IX collagen is a quantitatively minor component of the adult tissue but it has an important role in the assembly and function of the matrix. In cartilage, type IX collagen molecules are bound to the surface of type II collagen fibrils and to e...
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