pubmed-article:16432185 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:16432185 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
pubmed-article:16432185 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
pubmed-article:16432185 | lifeskim:mentions | umls-concept:C1515655 | lld:lifeskim |
pubmed-article:16432185 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:16432185 | pubmed:dateCreated | 2006-2-1 | lld:pubmed |
pubmed-article:16432185 | pubmed:abstractText | To understand the role of RNA-binding proteins (RBPs) in the regulation of gene expression, methods are needed for the in vivo identification of RNA-protein interactions. We have developed the peptide nucleic acid (PNA)-assisted identification of RBP technology to enable the identification of proteins that complex with a target RNA in vivo. Specific regions of the 3' and 5' UTRs of ankylosis mRNA were targeted by antisense PNAs transported into cortical neurons by the cell-penetrating peptide transportan 10. An array of proteins was isolated in complex with or near the targeted regions of the ankylosis mRNA through UV-induced crosslinking of the annealed PNA-RNA-RBP complex. The first evidence for pharmacological modulation of these specific protein-RNA associations was observed. These data show that the PNA-assisted identification of the RBP technique is a reliable method to rapidly identify proteins interacting in vivo with the target RNA. | lld:pubmed |
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pubmed-article:16432185 | pubmed:language | eng | lld:pubmed |
pubmed-article:16432185 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16432185 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:16432185 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16432185 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:16432185 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:16432185 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:16432185 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:16432185 | pubmed:month | Jan | lld:pubmed |
pubmed-article:16432185 | pubmed:issn | 0027-8424 | lld:pubmed |
pubmed-article:16432185 | pubmed:author | pubmed-author:KilkKalleK | lld:pubmed |
pubmed-article:16432185 | pubmed:author | pubmed-author:LangelUloU | lld:pubmed |
pubmed-article:16432185 | pubmed:author | pubmed-author:EberwineJames... | lld:pubmed |
pubmed-article:16432185 | pubmed:author | pubmed-author:MiyashiroKevi... | lld:pubmed |
pubmed-article:16432185 | pubmed:author | pubmed-author:ZielinskiJenn... | lld:pubmed |
pubmed-article:16432185 | pubmed:author | pubmed-author:KannanayakalT... | lld:pubmed |
pubmed-article:16432185 | pubmed:author | pubmed-author:EiríksdóttirE... | lld:pubmed |
pubmed-article:16432185 | pubmed:author | pubmed-author:PeritzTiinaT | lld:pubmed |
pubmed-article:16432185 | pubmed:author | pubmed-author:JochemsJeanin... | lld:pubmed |
pubmed-article:16432185 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:16432185 | pubmed:day | 31 | lld:pubmed |
pubmed-article:16432185 | pubmed:volume | 103 | lld:pubmed |
pubmed-article:16432185 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:16432185 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:16432185 | pubmed:pagination | 1557-62 | lld:pubmed |
pubmed-article:16432185 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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