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http://purl.uniprot.org/citations/28808124http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28808124http://www.w3.org/2000/01/rdf-schema#comment"Mammalian cells respond to double-stranded RNA (dsRNA) by activating a translation-inhibiting endoribonuclease, RNase L. Consensus in the field indicates that RNase L arrests protein synthesis by degrading ribosomal RNAs (rRNAs) and messenger RNAs (mRNAs). However, here we provide evidence for a different and far more efficient mechanism. By sequencing abundant RNA fragments generated by RNase L in human cells, we identify site-specific cleavage of two groups of noncoding RNAs: Y-RNAs, whose function is poorly understood, and cytosolic tRNAs, which are essential for translation. Quantitative analysis of human RNA cleavage versus nascent protein synthesis in lung carcinoma cells shows that RNase L stops global translation when tRNAs, as well as rRNAs and mRNAs, are still intact. Therefore, RNase L does not have to degrade the translation machinery to stop protein synthesis. Our data point to a rapid mechanism that transforms a subtle RNA cleavage into a cell-wide translation arrest."xsd:string
http://purl.uniprot.org/citations/28808124http://purl.org/dc/terms/identifier"doi:10.1261/rna.062000.117"xsd:string
http://purl.uniprot.org/citations/28808124http://purl.uniprot.org/core/author"Rath S."xsd:string
http://purl.uniprot.org/citations/28808124http://purl.uniprot.org/core/author"Donovan J."xsd:string
http://purl.uniprot.org/citations/28808124http://purl.uniprot.org/core/author"Korennykh A."xsd:string
http://purl.uniprot.org/citations/28808124http://purl.uniprot.org/core/author"Kolet-Mandrikov D."xsd:string
http://purl.uniprot.org/citations/28808124http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28808124http://purl.uniprot.org/core/name"RNA"xsd:string
http://purl.uniprot.org/citations/28808124http://purl.uniprot.org/core/pages"1660-1671"xsd:string
http://purl.uniprot.org/citations/28808124http://purl.uniprot.org/core/title"Rapid RNase L-driven arrest of protein synthesis in the dsRNA response without degradation of translation machinery."xsd:string
http://purl.uniprot.org/citations/28808124http://purl.uniprot.org/core/volume"23"xsd:string
http://purl.uniprot.org/citations/28808124http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/28808124
http://purl.uniprot.org/citations/28808124http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/28808124
http://purl.uniprot.org/uniprot/#_Q1A3D9-mappedCitation-28808124http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28808124
http://purl.uniprot.org/uniprot/#_Q05823-mappedCitation-28808124http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28808124
http://purl.uniprot.org/uniprot/#_Q1RLL8-mappedCitation-28808124http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/28808124
http://purl.uniprot.org/uniprot/Q1A3D9http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/28808124
http://purl.uniprot.org/uniprot/Q05823http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/28808124
http://purl.uniprot.org/uniprot/Q1RLL8http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/28808124