| http://purl.uniprot.org/citations/10373504 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10373504 | http://www.w3.org/2000/01/rdf-schema#comment | "The stable globin mRNAs provide an ideal system for studying the mechanism governing mammalian mRNA turnover. alpha-Globin mRNA stability is dictated by sequences in the 3' untranslated region (3'UTR) which form a specific ribonucleoprotein complex (alpha-complex) whose presence correlates with mRNA stability. One of the major protein components within this complex is a family of two polycytidylate-binding proteins, alphaCP1 and alphaCP2. Using an in vitro-transcribed and polyadenylated alpha-globin 3'UTR, we have devised an in vitro mRNA decay assay which reproduces the alpha-complex-dependent mRNA stability observed in cells. Incubation of the RNA with erythroleukemia K562 cytosolic extract results in deadenylation with distinct intermediates containing a periodicity of approximately 30 nucleotides, which is consistent with the binding of poly(A)-binding protein (PABP) monomers. Disruption of the alpha-complex by sequestration of alphaCP1 and alphaCP2 enhances deadenylation and decay of the mRNA, while reconstitution of the alpha-complex stabilizes the mRNA. Similarly, PABP is also essential for the stability of mRNA in vitro, since rapid deadenylation resulted upon its depletion. An RNA-dependent interaction between alphaCP1 and alphaCP2 with PABP suggests that the alpha-complex can directly interact with PABP. Therefore, the alpha-complex is an mRNA stability complex in vitro which could function at least in part by interacting with PABP."xsd:string |
| http://purl.uniprot.org/citations/10373504 | http://purl.org/dc/terms/identifier | "doi:10.1128/mcb.19.7.4552"xsd:string |
| http://purl.uniprot.org/citations/10373504 | http://purl.uniprot.org/core/author | "Wang Z."xsd:string |
| http://purl.uniprot.org/citations/10373504 | http://purl.uniprot.org/core/author | "Kiledjian M."xsd:string |
| http://purl.uniprot.org/citations/10373504 | http://purl.uniprot.org/core/author | "Trifillis P."xsd:string |
| http://purl.uniprot.org/citations/10373504 | http://purl.uniprot.org/core/author | "Day N."xsd:string |
| http://purl.uniprot.org/citations/10373504 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
| http://purl.uniprot.org/citations/10373504 | http://purl.uniprot.org/core/name | "Mol Cell Biol"xsd:string |
| http://purl.uniprot.org/citations/10373504 | http://purl.uniprot.org/core/pages | "4552-4560"xsd:string |
| http://purl.uniprot.org/citations/10373504 | http://purl.uniprot.org/core/title | "An mRNA stability complex functions with poly(A)-binding protein to stabilize mRNA in vitro."xsd:string |
| http://purl.uniprot.org/citations/10373504 | http://purl.uniprot.org/core/volume | "19"xsd:string |
| http://purl.uniprot.org/citations/10373504 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10373504 |
| http://purl.uniprot.org/citations/10373504 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10373504 |
| http://purl.uniprot.org/uniprot/#_Q15365-mappedCitation-10373504 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/10373504 |
| http://purl.uniprot.org/uniprot/#_Q15366-mappedCitation-10373504 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/10373504 |
| http://purl.uniprot.org/uniprot/#_P11940-mappedCitation-10373504 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/10373504 |
| http://purl.uniprot.org/uniprot/Q15365 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/10373504 |
| http://purl.uniprot.org/uniprot/P11940 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/10373504 |
| http://purl.uniprot.org/uniprot/Q15366 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/10373504 |