pubmed-article:10512861 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10512861 | lifeskim:mentions | umls-concept:C0681683 | lld:lifeskim |
pubmed-article:10512861 | lifeskim:mentions | umls-concept:C0002345 | lld:lifeskim |
pubmed-article:10512861 | lifeskim:mentions | umls-concept:C0136134 | lld:lifeskim |
pubmed-article:10512861 | lifeskim:mentions | umls-concept:C1428114 | lld:lifeskim |
pubmed-article:10512861 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
pubmed-article:10512861 | lifeskim:mentions | umls-concept:C0162610 | lld:lifeskim |
pubmed-article:10512861 | lifeskim:mentions | umls-concept:C0086597 | lld:lifeskim |
pubmed-article:10512861 | lifeskim:mentions | umls-concept:C0449774 | lld:lifeskim |
pubmed-article:10512861 | pubmed:issue | 10 | lld:pubmed |
pubmed-article:10512861 | pubmed:dateCreated | 1999-12-2 | lld:pubmed |
pubmed-article:10512861 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10512861 | pubmed:abstractText | The unc-52 gene encodes the nematode homologue of mammalian perlecan, the major heparan sulfate proteoglycan of the extracellular matrix. This is a large complex protein with regions similar to low-density lipoprotein receptors, laminin, and neural cell adhesion molecules (NCAMs). In this study, we extend our earlier work and demonstrate that a number of complex isoforms of this protein are expressed through alternative splicing. We identified three major classes of perlecan isoforms: a short form lacking the NCAM region and the C-terminal agrin-like region; a medium form containing the NCAM region, but still lacking the agrin-like region; and a newly identified long form that contains all five domains present in mammalian perlecan. Using region-specific antibodies and unc-52 mutants, we reveal a complex spatial and temporal expression pattern for these UNC-52 isoforms. As well, using a series of mutations affecting different regions and thus different isoforms of UNC-52, we demonstrate that the medium NCAM-containing isoforms are sufficient for myofilament lattice assembly in developing nematode body-wall muscle. Neither short isoforms nor isoforms containing the C-terminal agrin-like region are essential for sarcomere assembly or muscle cell attachment, and their role in development remains unclear. | lld:pubmed |
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pubmed-article:10512861 | pubmed:language | eng | lld:pubmed |
pubmed-article:10512861 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10512861 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10512861 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10512861 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10512861 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10512861 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10512861 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10512861 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10512861 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10512861 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10512861 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10512861 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10512861 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10512861 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10512861 | pubmed:month | Oct | lld:pubmed |
pubmed-article:10512861 | pubmed:issn | 1059-1524 | lld:pubmed |
pubmed-article:10512861 | pubmed:author | pubmed-author:MullerG LGL | lld:pubmed |
pubmed-article:10512861 | pubmed:author | pubmed-author:BushJ AJA | lld:pubmed |
pubmed-article:10512861 | pubmed:author | pubmed-author:MoermanD GDG | lld:pubmed |
pubmed-article:10512861 | pubmed:author | pubmed-author:RogalskiT MTM | lld:pubmed |