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- W4239863351 abstract "This chapter focuses on type IV collagen, which is found exclusively in basement membranes where it provides the major structural support for a matrix. The molecule contains a long triple-helical domain containing approximately 20 short interruptions that are thought to introduce flexibility into the helix. It self-assembles into a meshwork by the antiparallel interaction and extensive disulfide bonding of four molecules at their NH2-termini to form the 7S domain, by the interaction of two molecules at their carboxylic acid-terminal noncollagenous (NC1) domains, and by lateral aggregations. The assembled type IV collagen meshwork provides a scaffold for the assembly of other basement membrane components through specific interactions with laminin, entactin/nidogen, and heparan sulfate proteoglycan. This meshwork endows the basement membrane with a size-selective filtration property. The chapter describes the molecular structure, gene structure, and isolation methods of type IV collagen." @default.
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- W4239863351 date "1998-01-01" @default.
- W4239863351 modified "2023-10-18" @default.
- W4239863351 title "Collagen type IV" @default.
- W4239863351 doi "https://doi.org/10.1016/b978-012068911-8/50109-3" @default.
- W4239863351 hasPublicationYear "1998" @default.
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