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| http://purl.uniprot.org/citations/17586485 | http://www.w3.org/2000/01/rdf-schema#comment | "Protein disulfide isomerase (PDI) is a multifunctional protein required for many aspects of protein folding and transit through the endoplasmic reticulum. A conserved family of three PDIs has been functionally analysed using genetic mutants of the model organism Caenorhabditis elegans. PDI-1 and PDI-3 are individually non-essential, whereas PDI-2 is required for normal post-embryonic development. In combination, all three genes are synergistically essential for embryonic development in this nematode. Mutations in pdi-2 result in severe body morphology defects, uncoordinated movement, adult sterility, abnormal molting and aberrant collagen deposition. Many of these phenotypes are consistent with a role in collagen biogenesis and extracellular matrix formation. PDI-2 is required for the normal function of prolyl 4-hydroxylase, a key collagen-modifying enzyme. Site-directed mutagenesis indicates that the independent catalytic activity of PDI-2 may also perform an essential developmental function. PDI-2 therefore performs two critical roles during morphogenesis. The role of PDI-2 in collagen biogenesis can be restored following complementation of the mutant with human PDI."xsd:string |
| http://purl.uniprot.org/citations/17586485 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.ydbio.2007.05.041"xsd:string |
| http://purl.uniprot.org/citations/17586485 | http://purl.uniprot.org/core/author | "McCormack G."xsd:string |
| http://purl.uniprot.org/citations/17586485 | http://purl.uniprot.org/core/author | "Page A.P."xsd:string |
| http://purl.uniprot.org/citations/17586485 | http://purl.uniprot.org/core/author | "Winter A.D."xsd:string |
| http://purl.uniprot.org/citations/17586485 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17586485 | http://purl.uniprot.org/core/name | "Dev Biol"xsd:string |
| http://purl.uniprot.org/citations/17586485 | http://purl.uniprot.org/core/pages | "449-461"xsd:string |
| http://purl.uniprot.org/citations/17586485 | http://purl.uniprot.org/core/title | "Protein disulfide isomerase activity is essential for viability and extracellular matrix formation in the nematode Caenorhabditis elegans."xsd:string |
| http://purl.uniprot.org/citations/17586485 | http://purl.uniprot.org/core/volume | "308"xsd:string |
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