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1
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0016855515
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Composition and structure of the pericellular environment: Physiological function and chemical composition of pericellular proteoglycan (an evolutionary view)
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Scott, J. E. (1975) Composition and structure of the pericellular environment: Physiological function and chemical composition of pericellular proteoglycan (an evolutionary view). Philos. Trans. R. Soc. London B 271, 235-242.
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Extracellular matrix, supramolecular organisation and shape
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Scott, J. E. (1995) Extracellular matrix, supramolecular organisation and shape. J. Anat. 187, 259-269.
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Proteoglycan:collagen interactions and corneal ultrastructure
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Scott, J. E. (1991) Proteoglycan:collagen interactions and corneal ultrastructure. Biochem. Soc. Trans. 19, 877-881.
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Supramolecular organisation of extracellular matrix glycosaminoglycans, in vitro and in the tissues
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Scott, J. E. (1992) Supramolecular organisation of extracellular matrix glycosaminoglycans, in vitro and in the tissues. FASEB J. 6, 2639-2645.
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FASEB J.
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Proteodermatan and proteokeratan sulfate (decorin, lumican/fibromodulin) proteins are horseshoe shaped: Implications for their interactions with collagen
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Scott, J. E. (1996) Proteodermatan and proteokeratan sulfate (decorin, lumican/fibromodulin) proteins are horseshoe shaped: Implications for their interactions with collagen. Biochemistry 35, 8795-8799.
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Biochemistry
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Extracellular matrix, supramolecular organisation and shape: Dynamic aspects
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C. Balduini, P. Cherubino, and G. De Luca, Eds., La Goliardica Pavese, Pavia
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Scott, J. E. (1996) Extracellular matrix, supramolecular organisation and shape: Dynamic aspects. In "Advances in Biomedical Studies, Vol II, Biology and Physiopathology of the Extracellular Matrix" (C. Balduini, P. Cherubino, and G. De Luca, Eds.), pp. 7 to 19, La Goliardica Pavese, Pavia.
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Scott, J.E.1
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7
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The chemical morphology of extracellular matrix in experimental rat liver fibrosis resembles that of normal developing connective tissue
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Scott, J. E., Bosworth, T. R., Cribb, A. M., and Gressner, A. M. (1994) The chemical morphology of extracellular matrix in experimental rat liver fibrosis resembles that of normal developing connective tissue. Virchow's Arch. 424, 89-98.
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Scott, J.E.1
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8
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0024814778
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Proteoglycan:collagen interactions in dermatosparactic skin and tendon: An electron histochemical study using Cupromeronic blue in a critical electrolyte concentration method
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Scott, J. E., Haigh, M., Nusgens, B., and Lapierre, C. (1989) Proteoglycan:collagen interactions in dermatosparactic skin and tendon: An electron histochemical study using Cupromeronic blue in a critical electrolyte concentration method. Matrix 9, 437-442.
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Matrix
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9
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Osteogenesis imperfecta mutations may probe vital functional domains (e.g., proteoglycan binding sites) of type I collagen fibrils
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Scott, J. E., and Tenni, R. (1997) Osteogenesis imperfecta mutations may probe vital functional domains (e.g., proteoglycan binding sites) of type I collagen fibrils. Cell Biochem. Funct. 15, 283-286.
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Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility
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Danielson, K. G., Baribault, H., Holmes, D. F., Graham, H., Kadler, K., and Iozzo, R. V. (1997) Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility. J. Cell Biol. 136, 729-743.
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Deficient expression of the small proteoglycan decorin in a case of severe/lethal osteogenesis imperfecta
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Dyne, K. M., Valli, M., Forlino, A., Mottes, M., Kresse, H., and Cetta, G. (1996) Deficient expression of the small proteoglycan decorin in a case of severe/lethal osteogenesis imperfecta. Am. J. Med. Genet. 63, 161-166.
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Evidence for altered proteoglycan-collagen interactions in extracellular matrices produced by osteogenesis imperfecta skin fibroblasts
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Dyne, K., Valli, M., Cetta, G., Scott, J. E., Thomlinson, A. M., and Ritchie, M. (1996) Evidence for altered proteoglycan-collagen interactions in extracellular matrices produced by osteogenesis imperfecta skin fibroblasts. Eur. J. Histochem. 40, 246.
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13
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Substitution of cysteine for glycine at residue 415 of one allele of the α1(1) chain of type 1 procollagen in type III/IV osteogeneis imperfecta
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Nicholls, A. C., Oliver, J., Renouf, D. V., Keston, M., and Pope, F. M. (1991) Substitution of cysteine for glycine at residue 415 of one allele of the α1(1) chain of type 1 procollagen in type III/IV osteogeneis imperfecta. J. Med. Genet. 28, 757-764.
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Paternal mosaicism for a COL1A1 dominant mutation (α1 Ser-415) causes recurrent osteogenesis imperfecta
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Extracellular matrix deposition in cultured dermal fibroblasts from four probands affected by osteogenesis imperfecta
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Characterisation of three osteogenesis imperfecta collagen α1(1) glycine to serine mutations demonstrating a position dependant gradient of phenotype severity
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Deduced protein sequence of bone small proteoglycan 1 (biglycan) shows homology with proteoglycan II (decorin) and several known non-connective proteins in a variety of species
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A comparative biochemical and ultrastructural study of proteglycan-collagen interactions in corneal stroma: Functional and metabolic implications
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Scott, J. E., and Bosworth, T. R. (1990) A comparative biochemical and ultrastructural study of proteglycan-collagen interactions in corneal stroma: Functional and metabolic implications. Biochem. J. 270, 491-497.
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The determination of hydroxyproline in tissue and protein samples containing small amounts of this amino acid
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A method for processing tissue sections for staining with Cupromeronic blue and other dyes, using CEC techniques, for light and electron microscopy
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Haigh, M., and Scott, J. E. (1986) A method for processing tissue sections for staining with Cupromeronic blue and other dyes, using CEC techniques, for light and electron microscopy. Basic Appl. Histochem. 30, 479-485.
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Identification of specific binding sites of keratan sulphate and chondroitin/dermatan sulphate proteoglycans on collagen fibrils in cornea, using Cupromeronic blue in critical electrolyte concentration techniques
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Scott, J. E., and Haigh, M. (1988) Identification of specific binding sites of keratan sulphate and chondroitin/dermatan sulphate proteoglycans on collagen fibrils in cornea, using Cupromeronic blue in critical electrolyte concentration techniques. Biochem. J. 253, 607-610.
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Abnormal compartmentalisation of cartilage matrix components in mice lacking collagen X: Implications for function
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Kwan, K. M., Pang, M. K., Zhou, S., Cowan, S. K., Kong, R. Y., Pfordte, T., Olsen, B. R., Sillence, D. O., Tam, P. P., and Cheah, K. S. (1997) Abnormal compartmentalisation of cartilage matrix components in mice lacking collagen X: Implications for function. J. Cell Biol. 136, 459-471.
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Concentration of mutations causing Schmid metaphyseal chondrodysplasia in the C-terminal noncollagenous domain of type X collagen
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McIntosh, I., Abbott, M. H., and Francomano, C. A. (1995) Concentration of mutations causing Schmid metaphyseal chondrodysplasia in the C-terminal noncollagenous domain of type X collagen. Hum. Mutat. 5, 121-125.
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Proteoglycan-collagen arrangements in developing rat tail tendon: An electron microscopical and biochemical study
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Scott, J. E., Orford, C. R., and Hughes, E. W. (1981) Proteoglycan-collagen arrangements in developing rat tail tendon: An electron microscopical and biochemical study. Biochem. J. 195, 573-581.
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The control of collagen fibril diameters in connective tissues
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Scott, J. E., and Parry, D. A. D. (1992) The control of collagen fibril diameters in connective tissues. Int. J. Biol. Macromol. 14, 292-293.
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Nomenclature of dermatan/chondroitin glycans and their proteoglycans
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Scott, J. E. (1993) Nomenclature of dermatan/chondroitin glycans and their proteoglycans. In "Dermatan Sulphate Proteoglycans: Chemistry, Biology, Chemical Pathology" (J. E. Scott, Ed.) pp. 1-11, Portland Press (Biochemical Society), London.
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