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BMP\/GDF homo- and hetero-dimers interact with combinations of type\u00a0I and type\u00a0II receptor dimers to produce multiple possible signalling complexes, leading to the activation of one of two competing sets of SMAD transcription factors. BMP\/GDFs have highly specific and localized functions. These are regulated in a number of ways, including the developmental restriction of BMP\/GDF expression and through the secretion of several specific BMP antagonist proteins that bind with high affinity to the cytokines. Curiously, a number of these antagonists are also members of the TGF-\u03b2 superfamily. Finally a number of both the BMP\/GDFs and their antagonists interact with the heparan sulphate side chains of cell-surface and extracellular-matrix proteoglycans.<\/jats:p>","DOI":"10.1042\/bj20100305","type":"journal-article","created":{"date-parts":[[2010,6,15]],"date-time":"2010-06-15T11:17:50Z","timestamp":1276600670000},"page":"1-12","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":188,"title":["Bone morphogenetic protein and growth differentiation factor cytokine families and their protein antagonists"],"prefix":"10.1042","volume":"429","author":[{"given":"Christopher\u00a0C.","family":"Rider","sequence":"first","affiliation":[{"name":"School of Biological Sciences, Royal Holloway University of London, Egham Hill, Egham, Surrey TW20 OEX, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Barbara","family":"Mulloy","sequence":"additional","affiliation":[{"name":"Laboratory for Molecular Structure, National Institute for Biological Standards and Control, Blanche Lane, South Mimms, Potters Bar, Hertfordshire EN6 3QG, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2010,6,14]]},"reference":[{"key":"2021112214410030400_B1","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1038\/nbt0398-247","article-title":"Role of morphogenetic proteins in skeletal tissue engineering and regeneration","volume":"16","author":"Reddi","year":"1998","journal-title":"Nat. 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Biol."},{"key":"2021112214410030400_B46","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1006\/geno.1998.5474","article-title":"Coding sequence and expression patterns of mouse chordin and mapping of the cognate mouse chrd and human CHRD genes","volume":"52","author":"Pappano","year":"1998","journal-title":"Genomics"},{"key":"2021112214410030400_B47","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/S0378-1119(01)00827-7","article-title":"Chordin-like CR domains and the regulation of evolutionarily conserved extracellular signaling systems","volume":"287","author":"Garcia","year":"2002","journal-title":"Gene"},{"key":"2021112214410030400_B48","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1016\/j.bbrc.2004.01.048","article-title":"Human Crossveinless-2 is a novel inhibitor of bone morphogenetic proteins","volume":"315","author":"Binnerts","year":"2004","journal-title":"Biochem. Biophys. Res. 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