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http://purl.uniprot.org/citations/10587642http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10587642http://www.w3.org/2000/01/rdf-schema#comment"SMAD proteins are phosphorylated by transforming growth factor-beta (TGF-beta) receptors and translocate to the nucleus, where they control transcription. Here we investigate the fate of activated Smad2. We show that receptor-mediated activation leads to multi-ubiquitination and subsequent degradation of Smad2 by the proteasome. Ubiquitination of Smad2 is a consequence of its accumulation in the nucleus. If degradation is averted, the phosphorylated Smad2 remains in the nucleus in an active state. By targeting Smad2 for destruction, TGF-beta ensures the irreversible termination of its own signalling function."xsd:string
http://purl.uniprot.org/citations/10587642http://purl.org/dc/terms/identifier"doi:10.1038/70258"xsd:string
http://purl.uniprot.org/citations/10587642http://purl.uniprot.org/core/author"Lo R.S."xsd:string
http://purl.uniprot.org/citations/10587642http://purl.uniprot.org/core/author"Massague J."xsd:string
http://purl.uniprot.org/citations/10587642http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10587642http://purl.uniprot.org/core/name"Nat Cell Biol"xsd:string
http://purl.uniprot.org/citations/10587642http://purl.uniprot.org/core/pages"472-478"xsd:string
http://purl.uniprot.org/citations/10587642http://purl.uniprot.org/core/title"Ubiquitin-dependent degradation of TGF-beta-activated smad2."xsd:string
http://purl.uniprot.org/citations/10587642http://purl.uniprot.org/core/volume"1"xsd:string
http://purl.uniprot.org/citations/10587642http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/10587642
http://purl.uniprot.org/citations/10587642http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/10587642
http://purl.uniprot.org/uniprot/#_Q13485-mappedCitation-10587642http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/10587642
http://purl.uniprot.org/uniprot/#_P51668-mappedCitation-10587642http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/10587642
http://purl.uniprot.org/uniprot/#_Q15796-mappedCitation-10587642http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/10587642
http://purl.uniprot.org/uniprot/#_P84022-mappedCitation-10587642http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/10587642
http://purl.uniprot.org/uniprot/#_P61077-mappedCitation-10587642http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/10587642
http://purl.uniprot.org/uniprot/Q15796http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/10587642
http://purl.uniprot.org/uniprot/Q13485http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/10587642
http://purl.uniprot.org/uniprot/P61077http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/10587642
http://purl.uniprot.org/uniprot/P51668http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/10587642
http://purl.uniprot.org/uniprot/P84022http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/10587642