http://purl.uniprot.org/citations/17531811 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/17531811 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/17531811 | http://www.w3.org/2000/01/rdf-schema#comment | "RNA interference is a conserved pathway of sequence-specific gene silencing that depends on small guide RNAs and the action of proteins assembled in the RNA-induced silencing complex (RISC). Minimally, the action of RISC requires the endonucleolytic slicer activity of Argonaute2 (Ago2) directed to RNA targets whose sequences are complementary to RISC-incorporated small RNA. To identify RISC components in human cells, we developed an affinity-purification strategy to isolate siRNA-programmed RISC. Here we report the identification of RNA helicase A (RHA) as a human RISC-associated factor. We show that RHA interacts in human cells with siRNA, Ago2, TRBP, and Dicer and functions in the RNAi pathway. In RHA-depleted cells, RNAi was reduced as a consequence of decreased intracellular concentration of active RISC assembled with the guide-strand RNA and Ago2. Our results identify RHA as a RISC component and demonstrate that RHA functions in RISC as an siRNA-loading factor."xsd:string |
http://purl.uniprot.org/citations/17531811 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.molcel.2007.04.016"xsd:string |
http://purl.uniprot.org/citations/17531811 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.molcel.2007.04.016"xsd:string |
http://purl.uniprot.org/citations/17531811 | http://purl.uniprot.org/core/author | "Rana T.M."xsd:string |
http://purl.uniprot.org/citations/17531811 | http://purl.uniprot.org/core/author | "Rana T.M."xsd:string |
http://purl.uniprot.org/citations/17531811 | http://purl.uniprot.org/core/author | "Robb G.B."xsd:string |
http://purl.uniprot.org/citations/17531811 | http://purl.uniprot.org/core/author | "Robb G.B."xsd:string |
http://purl.uniprot.org/citations/17531811 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
http://purl.uniprot.org/citations/17531811 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
http://purl.uniprot.org/citations/17531811 | http://purl.uniprot.org/core/name | "Mol. Cell"xsd:string |
http://purl.uniprot.org/citations/17531811 | http://purl.uniprot.org/core/name | "Mol. Cell"xsd:string |
http://purl.uniprot.org/citations/17531811 | http://purl.uniprot.org/core/pages | "523-537"xsd:string |
http://purl.uniprot.org/citations/17531811 | http://purl.uniprot.org/core/pages | "523-537"xsd:string |
http://purl.uniprot.org/citations/17531811 | http://purl.uniprot.org/core/title | "RNA helicase A interacts with RISC in human cells and functions in RISC loading."xsd:string |
http://purl.uniprot.org/citations/17531811 | http://purl.uniprot.org/core/title | "RNA helicase A interacts with RISC in human cells and functions in RISC loading."xsd:string |
http://purl.uniprot.org/citations/17531811 | http://purl.uniprot.org/core/volume | "26"xsd:string |
http://purl.uniprot.org/citations/17531811 | http://purl.uniprot.org/core/volume | "26"xsd:string |
http://purl.uniprot.org/citations/17531811 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17531811 |
http://purl.uniprot.org/citations/17531811 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17531811 |
http://purl.uniprot.org/citations/17531811 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/17531811 |
http://purl.uniprot.org/citations/17531811 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/17531811 |
http://purl.uniprot.org/uniprot/Q15633 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/17531811 |
http://purl.uniprot.org/uniprot/Q08211 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/17531811 |