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- W83086325 abstract "This chapter presents an overview of the structural chemistry and the biological aspects of ADAMTS endopeptidases. The Human Gene Nomenclature Committee (HGNC) adopted the acronym ADAMTS (a disintegrin-like and metalloprotease domain (reprolysin type) with thrombospondin type 1 motifs) to designate a new gene and enzyme family distinct from ADAMs. Like the related matrix metalloproteinase (MMP) and ADAM (a disintegrin and metalloprotease) families, ADAMTS enzymes are bipartite, consisting of a prometalloprotease domain attached to a complex array of ancillary domains. ADAMTS enzymes are present in invertebrates and have been shown to have major roles in morphogenesis. Caenorhabditis elegans Adt-1 mutants have abnormal ray formation, possibly because of defective cuticle ECM remodeling, and show altered male copulatory behavior. The adt-1 gene encodes an ADAMTS that is structurally quite different in some respects from mammalian ADAMTS. In contrast, gon-1 closely resembles ADAMTS9 and ADAMTS20. Naturally occurring mutations in gon-1 result in defects in gonadal morphogenesis owing to the failure of migration of distal tip cells in the developing gonad. This suggests a role for GON-1 in cell migration, basement membrane remodeling or processing of migration cues." @default.
- W83086325 created "2016-06-24" @default.
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- W83086325 date "2004-01-01" @default.
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- W83086325 title "The ADAMTS endopeptidases" @default.
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