Results 211 to 220 of about 201,822 (256)
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Journal of Oral Pathology & Medicine, 1981
Abstract The current knowledge of the structure, expression and functions of fibronectin is reviewed.Fibronectin is a high molecular weight glycoprotein present in the blood, connective tissue and at cell surfaces. It is synthesized by many types of differentiated cells and is believed to be involved in the attachment of cells to the surrounding ...
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Abstract The current knowledge of the structure, expression and functions of fibronectin is reviewed.Fibronectin is a high molecular weight glycoprotein present in the blood, connective tissue and at cell surfaces. It is synthesized by many types of differentiated cells and is believed to be involved in the attachment of cells to the surrounding ...
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Steroids, 1989
The fibronectin (FN) levels in human follicular fluids have been shown to correlate well with follicular size and oocyte maturity, suggesting a role of FN in oocyte maturation. When added to the culture medium, the synthetic peptide Gly-Arg-Gly-Asp-Ser (GRGDS), which specifically inhibits the cell-binding of FN, has been shown to inhibit both ...
T T, Hung, A, Tsuiki, M, Yemini
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The fibronectin (FN) levels in human follicular fluids have been shown to correlate well with follicular size and oocyte maturity, suggesting a role of FN in oocyte maturation. When added to the culture medium, the synthetic peptide Gly-Arg-Gly-Asp-Ser (GRGDS), which specifically inhibits the cell-binding of FN, has been shown to inhibit both ...
T T, Hung, A, Tsuiki, M, Yemini
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Dermatologica, 2009
In the skin organ culture model of pemphigus, fibronectin concentrations of 300 and 500 μg/ml inhibited pemphigus plasma-induced acantholysis and intraepidermal binding of the pemphigus antibodies examined by direct immunofluorescence. A direct interaction of fibronectin with pemphigus antibodies could not be demonstrated by chromatography of pemphigus
T, Hunziker +2 more
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In the skin organ culture model of pemphigus, fibronectin concentrations of 300 and 500 μg/ml inhibited pemphigus plasma-induced acantholysis and intraepidermal binding of the pemphigus antibodies examined by direct immunofluorescence. A direct interaction of fibronectin with pemphigus antibodies could not be demonstrated by chromatography of pemphigus
T, Hunziker +2 more
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Journal of Cell Science, 2002
Fibronectin (FN) mediates a wide variety of cellular interactions with the extracellular matrix (ECM) and plays important roles in cell adhesion, migration, growth and differentiation ( [Mosher, 1989][1]; [Carsons, 1989][2]; [Hynes, 1990][3]; [Yamada and Clark, 1996][4]).
Roumen, Pankov, Kenneth M, Yamada
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Fibronectin (FN) mediates a wide variety of cellular interactions with the extracellular matrix (ECM) and plays important roles in cell adhesion, migration, growth and differentiation ( [Mosher, 1989][1]; [Carsons, 1989][2]; [Hynes, 1990][3]; [Yamada and Clark, 1996][4]).
Roumen, Pankov, Kenneth M, Yamada
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Current Protocols in Cell Biology, 1999
AbstractThis unit describes the purification of the multifunctional adhesive glycoprotein fibronectin from plasma or of cell‐derived fibronectin from cell surfaces and from conditioned medium. Fibronectin can be used in cell adhesion and migration assays, and can be obtained in relatively high purity using simple affinity chromatography techniques ...
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AbstractThis unit describes the purification of the multifunctional adhesive glycoprotein fibronectin from plasma or of cell‐derived fibronectin from cell surfaces and from conditioned medium. Fibronectin can be used in cell adhesion and migration assays, and can be obtained in relatively high purity using simple affinity chromatography techniques ...
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Annual Review of Medicine, 1984
Fibronectin is a major protein of blood and tissues. It has been intensively studied because of its many interactions with cells and other macromolecules. Fibronectin is a principal component of the extracellular matrix, and its most important function seems to be in tissue remodelling during embryogenesis and wound healing.
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Fibronectin is a major protein of blood and tissues. It has been intensively studied because of its many interactions with cells and other macromolecules. Fibronectin is a principal component of the extracellular matrix, and its most important function seems to be in tissue remodelling during embryogenesis and wound healing.
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Seminars in Cancer Biology, 2002
Fibronectin (Fn) was the first 'structural' glycoprotein intensively studied as an ubiquitous matrix component of early phylogenetic appearance. Its age-dependent increase in plasma and tissues may be accompanied in pathological states, especially in tumor growth, by its proteolytic breakdown by a number of neutral proteases.
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Fibronectin (Fn) was the first 'structural' glycoprotein intensively studied as an ubiquitous matrix component of early phylogenetic appearance. Its age-dependent increase in plasma and tissues may be accompanied in pathological states, especially in tumor growth, by its proteolytic breakdown by a number of neutral proteases.
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2003
Fibronectin (FN) matrix fibrils assembled in cell culture have been observed to stretch in response to cell movements, and when broken relax to 1/3 to 1/4 of their rest length. Two molecular mechanisms have been proposed, for the elasticity. One proposes that FN molecules in relaxed fibers are bent and looped into a compact conformation, and stretching
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Fibronectin (FN) matrix fibrils assembled in cell culture have been observed to stretch in response to cell movements, and when broken relax to 1/3 to 1/4 of their rest length. Two molecular mechanisms have been proposed, for the elasticity. One proposes that FN molecules in relaxed fibers are bent and looped into a compact conformation, and stretching
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Plasma fibronectin contributes to fibronectin in tissues.
Acta chirurgica Scandinavica, 1985Fibronectin is produced by several cell types, with hepatocytes currently recognized as the main source of plasma fibronectin. Mesenchymal cells produce fibronectin in vitro and probably do so even in vivo. But it is not clear if these cells represent the sole source of tissue fibronectin.
T, Gauperaa, R, Seljelid
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