Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
MD Pierschbacher, E Ruoslahti - Nature, 1984 - nature.com
MD Pierschbacher, E Ruoslahti
Nature, 1984•nature.comThe ability of fibronectin to bind cells can be accounted for by the tetrapeptide L-arginyl-
glycyl-L-aspartyl-L-serine, a sequence which is part of the cell attachment domain of
fibronectin and present in at least five other proteins. This tetrapeptide may constitute a
cellular recognition determinant common to several proteins.
glycyl-L-aspartyl-L-serine, a sequence which is part of the cell attachment domain of
fibronectin and present in at least five other proteins. This tetrapeptide may constitute a
cellular recognition determinant common to several proteins.
Abstract
The ability of fibronectin to bind cells can be accounted for by the tetrapeptide L-arginyl-glycyl-L-aspartyl-L-serine, a sequence which is part of the cell attachment domain of fibronectin and present in at least five other proteins. This tetrapeptide may constitute a cellular recognition determinant common to several proteins.
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