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- W2050656588 abstract "1. Frog integumentary mucins (FIM-A.1, FIM-B.1 and FIM-C.1) consist of typical threonine-rich highly O-glycosylated (semi)repetitive domains, and cysteine-rich modules, i.e. the P-domain, the short consensus repeat and a region with high similarity to the C-terminal end of von Willebrand factor (designated here CC29-motif). 2. These modules are thought to be involved in protein-protein interactions and they have been observed in a variety of extracellular proteins. In FIMs, these modules may be involved in oligomerization processes leading to an entangled mucin network. 3. Polydispersities have been detected in FIM-B.1 and FIM-C.1 within single individuals. Multiple transcripts are probably generated by alternative splicing of a huge array of different (semi)repetitive cassettes encoding the threonine-rich domains. 4. Furthermore, genetic polymorphism is observed between different individuals, probably due to allelic variations in the number of (semi)repetitive cassettes." @default.
- W2050656588 created "2016-06-24" @default.
- W2050656588 creator A5060565688 @default.
- W2050656588 creator A5072091739 @default.
- W2050656588 date "1993-07-01" @default.
- W2050656588 modified "2023-09-29" @default.
- W2050656588 title "Biosynthesis of frog skin mucins: Cysteine-rich shuffled modules, polydispersities and genetic polymorphism" @default.
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- W2050656588 doi "https://doi.org/10.1016/0305-0491(93)90075-g" @default.
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