Results 311 to 320 of about 94,496 (352)
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The International Journal of Biochemistry & Cell Biology, 1997
Fibronectin is a glycoprotein consisting of repeating units of amino acids, which form domains that enable the molecule to interact with a variety of cells through both integrin and non-integrin receptors. It is encoded by a single gene, but alternative splicing of pre-mRNA allows formation of multiple isoforms that have critical roles in cell adhesion,
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Fibronectin is a glycoprotein consisting of repeating units of amino acids, which form domains that enable the molecule to interact with a variety of cells through both integrin and non-integrin receptors. It is encoded by a single gene, but alternative splicing of pre-mRNA allows formation of multiple isoforms that have critical roles in cell adhesion,
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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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Fibronectin and fibronectin fragments
1995Abstract The adhesive glycoprotein fibronectin has provided an important model system for investigating mechanisms of cell-adhesive interactions. Fibronectin binds to a number of biological macromolecules including heparin, collagen, fibrin, and cell surface receptors.
Steven K Akiyama, Kenneth M Yamada
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Structural comparisons of fibronectins isolated from early and late passage cells
Mechanisms of Ageing and Development, 1984J. Sorrentino, A. J. Millis
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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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Fibronectins: structure, functions and receptors
Current Opinion in Cell Biology, 1989Kenneth M. Yamada
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