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http://purl.uniprot.org/citations/15158472http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15158472http://www.w3.org/2000/01/rdf-schema#comment"Bone morphogenetic proteins (BMPs) play central roles in differentiation, development, and physiologic tissue remodeling. Recently, we have demonstrated that a protein inhibitor of activated STAT, PIASy, suppresses TGF-beta signaling by interacting with Sma and MAD-related protein 3 (Smad3). In this study, we examined a PIASy-dependent inhibitory effect on BMP signaling. PIASy expression was induced by BMP-2 stimulation and suppressed BMP-2-dependent Smad activity in hepatoma cells. Furthermore, BMP-2-regulated Smads directly bound to PIASy. We also demonstrated that the RING domain of PIASy played an important role in PIASy-mediated suppression of Smad activity. We here provide evidence that the inhibitory action of PIASy on BMP-regulated Smad activity was due to direct physical interactions between Smads and PIASy through its RING domain."xsd:string
http://purl.uniprot.org/citations/15158472http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2004.04.161"xsd:string
http://purl.uniprot.org/citations/15158472http://purl.uniprot.org/core/author"Sugiyama K."xsd:string
http://purl.uniprot.org/citations/15158472http://purl.uniprot.org/core/author"Yamamoto T."xsd:string
http://purl.uniprot.org/citations/15158472http://purl.uniprot.org/core/author"Matsuda T."xsd:string
http://purl.uniprot.org/citations/15158472http://purl.uniprot.org/core/author"Imoto S."xsd:string
http://purl.uniprot.org/citations/15158472http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15158472http://purl.uniprot.org/core/name"Biochem Biophys Res Commun"xsd:string
http://purl.uniprot.org/citations/15158472http://purl.uniprot.org/core/pages"275-282"xsd:string
http://purl.uniprot.org/citations/15158472http://purl.uniprot.org/core/title"The RING domain of PIASy is involved in the suppression of bone morphogenetic protein-signaling pathway."xsd:string
http://purl.uniprot.org/citations/15158472http://purl.uniprot.org/core/volume"319"xsd:string
http://purl.uniprot.org/citations/15158472http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15158472
http://purl.uniprot.org/citations/15158472http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15158472
http://purl.uniprot.org/uniprot/#_B3KMR4-mappedCitation-15158472http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15158472
http://purl.uniprot.org/uniprot/#_Q53H55-mappedCitation-15158472http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15158472
http://purl.uniprot.org/uniprot/#_Q8N2W9-mappedCitation-15158472http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15158472
http://purl.uniprot.org/uniprot/#_Q05DS6-mappedCitation-15158472http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15158472
http://purl.uniprot.org/uniprot/Q53H55http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15158472
http://purl.uniprot.org/uniprot/Q8N2W9http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15158472
http://purl.uniprot.org/uniprot/Q05DS6http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15158472
http://purl.uniprot.org/uniprot/B3KMR4http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/15158472