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http://purl.uniprot.org/citations/16289642http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16289642http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16289642http://www.w3.org/2000/01/rdf-schema#comment"RNA silencing processes are guided by small RNAs known as siRNAs and microRNAs (miRNAs) . They reside in ribonucleoprotein complexes, which guide the cleavage of complementary mRNAs or affect stability and translation of partial complementary mRNAs . Argonaute (Ago) proteins are at the heart of silencing effector complexes and bind the single-stranded siRNA and miRNA . Our biochemical analysis revealed that Ago2 is present in a pre-miRNA processing complex that is able to transfer the miRNA into a target-mRNA cleaving complex. To gain insight into the function and composition of RNA silencing complexes, we purified Ago1- and Ago2-containing complexes from human cells. Several known Ago1-and/or Ago2-associated proteins including Dicer were identified, but also two novel factors, the putative RNA helicase MOV10, and the RNA recognition motif (RRM)-containing protein TNRC6B/KIAA1093. The new proteins localize, similar to Ago proteins, to mRNA-degrading cytoplasmic P bodies, and they are functionally required to mediate miRNA-guided mRNA cleavage."xsd:string
http://purl.uniprot.org/citations/16289642http://purl.org/dc/terms/identifier"doi:10.1016/j.cub.2005.10.048"xsd:string
http://purl.uniprot.org/citations/16289642http://purl.org/dc/terms/identifier"doi:10.1016/j.cub.2005.10.048"xsd:string
http://purl.uniprot.org/citations/16289642http://purl.uniprot.org/core/author"Peters L."xsd:string
http://purl.uniprot.org/citations/16289642http://purl.uniprot.org/core/author"Peters L."xsd:string
http://purl.uniprot.org/citations/16289642http://purl.uniprot.org/core/author"Tuschl T."xsd:string
http://purl.uniprot.org/citations/16289642http://purl.uniprot.org/core/author"Tuschl T."xsd:string
http://purl.uniprot.org/citations/16289642http://purl.uniprot.org/core/author"Meister G."xsd:string
http://purl.uniprot.org/citations/16289642http://purl.uniprot.org/core/author"Meister G."xsd:string
http://purl.uniprot.org/citations/16289642http://purl.uniprot.org/core/author"Urlaub H."xsd:string
http://purl.uniprot.org/citations/16289642http://purl.uniprot.org/core/author"Urlaub H."xsd:string
http://purl.uniprot.org/citations/16289642http://purl.uniprot.org/core/author"Chen P.Y."xsd:string
http://purl.uniprot.org/citations/16289642http://purl.uniprot.org/core/author"Chen P.Y."xsd:string
http://purl.uniprot.org/citations/16289642http://purl.uniprot.org/core/author"Landthaler M."xsd:string
http://purl.uniprot.org/citations/16289642http://purl.uniprot.org/core/author"Landthaler M."xsd:string
http://purl.uniprot.org/citations/16289642http://purl.uniprot.org/core/author"Luehrmann R."xsd:string
http://purl.uniprot.org/citations/16289642http://purl.uniprot.org/core/author"Luehrmann R."xsd:string
http://purl.uniprot.org/citations/16289642http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16289642http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16289642http://purl.uniprot.org/core/name"Curr. Biol."xsd:string
http://purl.uniprot.org/citations/16289642http://purl.uniprot.org/core/name"Curr. Biol."xsd:string
http://purl.uniprot.org/citations/16289642http://purl.uniprot.org/core/pages"2149-2155"xsd:string
http://purl.uniprot.org/citations/16289642http://purl.uniprot.org/core/pages"2149-2155"xsd:string