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- W2090848574 endingPage "28" @default.
- W2090848574 startingPage "19" @default.
- W2090848574 abstract "Laminins are the most abundant structural non-collagenous glycoproteins ubiquitously present in basement membranes. They are multidomain molecules constituting a family of possibly more than 50 members. Some members such as laminins 5, 6 and 10 are specific of the basal lamina present under stratified epithelia. Although only few intact laminin isoforms have been purified from cultivated cells or tissues, genetic engineering has opened the way for a rapid development of laminin structural biology. Moreover, the phenotypes resulting from gene targeting in mouse or from laminin defects in acquired or inherited human diseases highlight the pivotal role of laminins in morphogenesis, development, and physiology. Indeed, the laminins display a remarkable repertoire of functions, most importantly as structural elements forming a network throughout the basement membrane to which other collagenous or non-collagenous glycoproteins and proteoglycans attach. Furthermore, they are signaling molecules providing adjacent cells with diverse information by interacting with cell surface components." @default.
- W2090848574 created "2016-06-24" @default.
- W2090848574 creator A5030342857 @default.
- W2090848574 creator A5057806385 @default.
- W2090848574 date "1999-02-01" @default.
- W2090848574 modified "2023-09-25" @default.
- W2090848574 title "Laminins of the dermo–epidermal junction" @default.
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- W2090848574 doi "https://doi.org/10.1016/s0945-053x(98)00004-3" @default.