Results 231 to 240 of about 11,226 (256)
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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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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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Pathologie-biologie, 1992
Fibronectins are complex glycoprotein macromolecules whose molecular weight is 440 kilodaltons. These proteins, found throughout the body, are soluble in biological fluids and insoluble in connective tissue. They contribute to tissue morphogenesis through multiple interactions with cells and extracellular matrix components. Fibronectins play a key role
C, Stamm +3 more
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Fibronectins are complex glycoprotein macromolecules whose molecular weight is 440 kilodaltons. These proteins, found throughout the body, are soluble in biological fluids and insoluble in connective tissue. They contribute to tissue morphogenesis through multiple interactions with cells and extracellular matrix components. Fibronectins play a key role
C, Stamm +3 more
openaire +1 more source