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http://purl.uniprot.org/citations/1423604http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1423604http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1423604http://www.w3.org/2000/01/rdf-schema#comment"The low density lipoprotein receptor-related protein (LRP) is a large multifunctional clearance receptor that has been implicated in the hepatic uptake of chylomicron remnants and in the removal of protease-inhibitor complexes from the circulation and from the extracellular space. Disruption of the LRP gene in mice blocks development of LRP-/-embryos around the implantation stage. The expression pattern of LRP in the postimplantation stage embryo is identical to that of urokinase, a plasminogen activator that confers invasive properties to migrating cells. We demonstrate that LRP mediates uptake and degradation of urokinase-type plasminogen activator-plasminogen activator inhibitor 1 complexes and propose that the inability of the giant cells to remove the inactive protease complexes from their surfaces interferes with implantation of the embryo."xsd:string
http://purl.uniprot.org/citations/1423604http://purl.org/dc/terms/identifier"doi:10.1016/0092-8674(92)90511-a"xsd:string
http://purl.uniprot.org/citations/1423604http://purl.org/dc/terms/identifier"doi:10.1016/0092-8674(92)90511-a"xsd:string
http://purl.uniprot.org/citations/1423604http://purl.uniprot.org/core/author"Herz J."xsd:string
http://purl.uniprot.org/citations/1423604http://purl.uniprot.org/core/author"Herz J."xsd:string
http://purl.uniprot.org/citations/1423604http://purl.uniprot.org/core/author"Hammer R.E."xsd:string
http://purl.uniprot.org/citations/1423604http://purl.uniprot.org/core/author"Hammer R.E."xsd:string
http://purl.uniprot.org/citations/1423604http://purl.uniprot.org/core/author"Clouthier D.E."xsd:string
http://purl.uniprot.org/citations/1423604http://purl.uniprot.org/core/author"Clouthier D.E."xsd:string
http://purl.uniprot.org/citations/1423604http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1423604http://purl.uniprot.org/core/date"1992"xsd:gYear
http://purl.uniprot.org/citations/1423604http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/1423604http://purl.uniprot.org/core/name"Cell"xsd:string
http://purl.uniprot.org/citations/1423604http://purl.uniprot.org/core/pages"411-421"xsd:string
http://purl.uniprot.org/citations/1423604http://purl.uniprot.org/core/pages"411-421"xsd:string
http://purl.uniprot.org/citations/1423604http://purl.uniprot.org/core/title"LDL receptor-related protein internalizes and degrades uPA-PAI-1 complexes and is essential for embryo implantation."xsd:string
http://purl.uniprot.org/citations/1423604http://purl.uniprot.org/core/title"LDL receptor-related protein internalizes and degrades uPA-PAI-1 complexes and is essential for embryo implantation."xsd:string
http://purl.uniprot.org/citations/1423604http://purl.uniprot.org/core/volume"71"xsd:string
http://purl.uniprot.org/citations/1423604http://purl.uniprot.org/core/volume"71"xsd:string
http://purl.uniprot.org/citations/1423604http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1423604
http://purl.uniprot.org/citations/1423604http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1423604
http://purl.uniprot.org/citations/1423604http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/1423604
http://purl.uniprot.org/citations/1423604http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/1423604