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http://purl.uniprot.org/citations/17591922http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17591922http://www.w3.org/2000/01/rdf-schema#comment"Fibronectin (FN) is secreted as a disulfide-bonded FN dimer. Each subunit contains three types of repeating modules: FN-I, FN-II, and FN-III. The interactions of alpha5beta1 or alphav integrins with the RGD motif of FN-III repeat 10 (FN-III10) are considered an essential step in the assembly of FN fibrils. To test this hypothesis in vivo, we replaced the RGD motif with the inactive RGE in mice. FN-RGE homozygous embryos die at embryonic day 10 with shortened posterior trunk, absent tail bud-derived somites, and severe vascular defects resembling the phenotype of alpha5 integrin-deficient mice. Surprisingly, the absence of a functional RGD motif in FN did not compromise assembly of an FN matrix in mutant embryos or on mutant cells. Matrix assembly assays and solid-phase binding assays reveal that alphavbeta3 integrin assembles FN-RGE by binding an isoDGR motif in FN-I5, which is generated by the nonenzymatic rearrangement of asparagines (N) into an iso-aspartate (iso-D). Our findings demonstrate that FN contains a novel motif for integrin binding and fibril formation whose activity is controlled by amino acid modification."xsd:string
http://purl.uniprot.org/citations/17591922http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200703021"xsd:string
http://purl.uniprot.org/citations/17591922http://purl.uniprot.org/core/author"Erickson H.P."xsd:string
http://purl.uniprot.org/citations/17591922http://purl.uniprot.org/core/author"Kessler H."xsd:string
http://purl.uniprot.org/citations/17591922http://purl.uniprot.org/core/author"Takahashi S."xsd:string
http://purl.uniprot.org/citations/17591922http://purl.uniprot.org/core/author"Pfeifer A."xsd:string
http://purl.uniprot.org/citations/17591922http://purl.uniprot.org/core/author"Heckmann D."xsd:string
http://purl.uniprot.org/citations/17591922http://purl.uniprot.org/core/author"Ohashi T."xsd:string
http://purl.uniprot.org/citations/17591922http://purl.uniprot.org/core/author"Takagi J."xsd:string
http://purl.uniprot.org/citations/17591922http://purl.uniprot.org/core/author"Moser M."xsd:string
http://purl.uniprot.org/citations/17591922http://purl.uniprot.org/core/author"Kitao T."xsd:string
http://purl.uniprot.org/citations/17591922http://purl.uniprot.org/core/author"Fassler R."xsd:string
http://purl.uniprot.org/citations/17591922http://purl.uniprot.org/core/author"Leiss M."xsd:string
http://purl.uniprot.org/citations/17591922http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17591922http://purl.uniprot.org/core/name"J Cell Biol"xsd:string
http://purl.uniprot.org/citations/17591922http://purl.uniprot.org/core/pages"167-178"xsd:string
http://purl.uniprot.org/citations/17591922http://purl.uniprot.org/core/title"The RGD motif in fibronectin is essential for development but dispensable for fibril assembly."xsd:string
http://purl.uniprot.org/citations/17591922http://purl.uniprot.org/core/volume"178"xsd:string
http://purl.uniprot.org/citations/17591922http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17591922
http://purl.uniprot.org/citations/17591922http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17591922
http://purl.uniprot.org/uniprot/#_A0A087WQE0-mappedCitation-17591922http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17591922
http://purl.uniprot.org/uniprot/#_A0A087WS56-mappedCitation-17591922http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17591922
http://purl.uniprot.org/uniprot/#_A0A087WS99-mappedCitation-17591922http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17591922
http://purl.uniprot.org/uniprot/#_A0A087WSN6-mappedCitation-17591922http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17591922