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Secondary and tertiary structures of hyaluronan in aqueous solution, investigated by rotary shadowing-electron microscopy and computer simulation. Hyaluronan is a very efficient network-forming
The hyaluronan twofold helix was shown by computer simulation and energy calculations to be sterically capable of extensive duplex formation, probably driven by interactions between the large hydrophobic patches on alternate sides of the tape-like polymer, forming stable aggregates at biological temperatures in water. Expand
Macromolecular organization of chicken type X collagen in vitro
The macromolecular structure of type X collagen in the matrices of primary cultures of chick hypertrophic chondrocytes was initially investigated using immunoelectron microscopy and resulted in the formation of a regular hexagonal lattice, which may play an important role in modifying the cartilage matrix for subsequent events occurring in endochondral bone formation. Expand
Isolation and ultrastructural analysis of microfibrillar structures from foetal bovine elastic tissues. Relative abundance and supramolecular architecture of type VI collagen assemblies and fibrillin.
Analysis of these complex polymers has generated new information on their supramolecular architecture and relative abundance in these tissues and demonstrates that the release of intact collagen VI microfibrils from these tissues is largely dependent on the removal of the major collagen fibrils. Expand
Examination of corneal proteoglycans and glycosaminoglycans by rotary shadowing and electron microscopy.
The results on corneal DS PG confirm and extend the hypothesis that PGs specifically associated with collagen fibrils are tadpole shaped, and it is unsafe to assume the absence of GAGs, based on these techniques, and quantitative measurements of length may be subject to error. Expand
Pleomorphism in type I collagen fibrils produced by persistence of the procollagen N-propeptide.
The assembly of type I collagen and type I pN-collagen was studied in vitro using a system for generating these molecules enzymatically from their immediate biosynthetic precursors in terms of the hypothesis that the N-propeptides are preferentially located on the surface of a growing assembly. Expand
Crystalline regions in collagen fibrils.
A new image processing technique, content-dependent anisotropic spatial frequency filtering, has been developed to visualize the location and orientation of crystalline regions in collagen fibrilExpand
D-periodic assemblies of type I procollagen.
Observations show that intact propeptide domains hinder, but do not prevent, the formation of D-periodic assemblies, which could restrict its lateral growth and limit its final thickness. Expand
Collagen defect of bone in osteogenesis imperfecta (Type I). An electron microscopic study.
Osteogenesis imperfecta (OI) is an inherited disorder of connective tissue metabolism characterized by fragility of the bones, resulting in multiple fractures. In this study electron microscopicExpand
A clinical and ultrastructural study of osteogenesis imperfecta after flavonoid (Catergen) therapy.
After 6 months' treatment with Catergen, the abnormally narrow collagen fibrils found in the osteoid region in a pretreatment bone biopsy specimen from a middle-aged man with the common type 1 (autosomal dominant) form of Ol showed a significant reversion to normal diameters. Expand