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Nidogen-1 is a member of the nidogen family of basement membrane glycoproteins. The protein interacts with several other components of basement membranes. Structurally it (along with perlecan) connects the networks formed by collagens and laminins to each other.[9] It may also play a role in cell interactions with the extracellular matrix.[10][11]
^Zimmermann K, Hoischen S, Hafner M, Nischt R (May 1995). "Genomic sequences and structural organization of the human nidogen gene (NID)". Genomics. 27 (2): 245–50. doi:10.1006/geno.1995.1038. PMID7557988.
^Smith J, Ockleford CD (January 1994). "Laser scanning confocal examination and comparison of nidogen (entactin) with laminin in term human amniochorion". Placenta. 15 (1): 95–106. doi:10.1016/S0143-4004(05)80240-1. PMID8208674.
^Yi XY, Wayner EA, Kim Y, Fish AJ (March 1998). "Adhesion of cultured human kidney mesangial cells to native entactin: role of integrin receptors". Cell Adhes. Commun. 5 (3): 237–48. doi:10.3109/15419069809040294. PMID9686320.
^Adam S, Göhring W, Wiedemann H, Chu ML, Timpl R, Kostka G (September 1997). "Binding of fibulin-1 to nidogen depends on its C-terminal globular domain and a specific array of calcium-binding epidermal growth factor-like (EG) modules". J. Mol. Biol. 272 (2): 226–36. doi:10.1006/jmbi.1997.1244. PMID9299350.
^Tran H, VanDusen WJ, Argraves WS (September 1997). "The self-association and fibronectin-binding sites of fibulin-1 map to calcium-binding epidermal growth factor-like domains". J. Biol. Chem. 272 (36): 22600–6. doi:10.1074/jbc.272.36.22600. PMID9278415.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^Pan TC, Kluge M, Zhang RZ, Mayer U, Timpl R, Chu ML (August 1993). "Sequence of extracellular mouse protein BM-90/fibulin and its calcium-dependent binding to other basement-membrane ligands". Eur. J. Biochem. 215 (3): 733–40. doi:10.1111/j.1432-1033.1993.tb18086.x. PMID8354280.