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- W2000265611 abstract "Restrictin is a chick neural extracellular matrix protein implicated in neural cell attachment and found to be associated with the cell surface recognition protein F11. Here we show by cDNA cloning that restrictin is a large multidomain protein composed of 4 structural motifs. At the N-terminus restrictin contains a cysteine-rich segment of about 140 as that might link restrictin monomers into oligomers. This region is followed by 4.5 epidermal growth factor-like repeats and then by 9 consecutive motifs that are similar to fibronectin type III motifs. At the C-terminus restrictin is related to the β and γ chains of fibrinogen, including similarity to a calcium-binding segment. Restrictin shows substantial sequence similarity with tenascin (cytotactin) throughout the polypeptide, and like tenascin, it forms oligomeric structures, as revealed by electron microscopy of immunoaffinity-purified restrictin. The cell attachment site of restrictin is mapped to the C-terminal region by antibody perturbation experiments." @default.
- W2000265611 created "2016-06-24" @default.
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- W2000265611 date "1992-05-01" @default.
- W2000265611 modified "2023-10-16" @default.
- W2000265611 title "The chicken neural extracellular matrix molecule restrictin: Similarity with EGF-, fibronectin type III-, and fibrinogen-like motifs" @default.
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- W2000265611 doi "https://doi.org/10.1016/0896-6273(92)90199-n" @default.
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