2008
Flexibility in the site of exon junction complex deposition revealed by functional group and RNA secondary structure alterations in the splicing substrate
Mishler DM, Christ AB, Steitz JA. Flexibility in the site of exon junction complex deposition revealed by functional group and RNA secondary structure alterations in the splicing substrate. RNA 2008, 14: 2657-2670. PMID: 18952819, PMCID: PMC2590960, DOI: 10.1261/rna.1312808.Peer-Reviewed Original ResearchConceptsExon junction complexRNA secondary structureEJC depositionSplicing substrateMammalian nonsense-mediated mRNA decayNonsense-mediated mRNA decaySecondary structureStretches of DNATranslational regulationMRNA decayCoimmunoprecipitation assaysJunction complexSecondary structure alterationsDNA nucleotidesStructure alterationsH protectionUpstream shiftToeprintingExonsSitesNucleotidesDNACrystal structureDeposition sitesMRNA
1987
Structural Analysis of the Human U3 Ribonucleoprotein Particle Reveal a Conserved Sequence Available for Base Pairing with Pre-rRna
Parker K, Steitz J. Structural Analysis of the Human U3 Ribonucleoprotein Particle Reveal a Conserved Sequence Available for Base Pairing with Pre-rRna. Molecular And Cellular Biology 1987, 7: 2899-2913. DOI: 10.1128/mcb.7.8.2899-2913.1987.Peer-Reviewed Original ResearchProtein-RNA interactionsSecondary structureSubsequent reverse transcriptionRNA secondary structureHuman U3Phosphorylated proteinsConserved sequencesProcessing eventsPre-rRNAAlternative functionsBase pairsNucleotides -159Specific nucleasesHeLa cellsProtein constituentsRNase ABase pairingRNPProteinNonphosphorylated proteinsRRNAReverse transcriptionSequenceKilodaltonsNucleotides 65Structural analysis of the human U3 ribonucleoprotein particle reveal a conserved sequence available for base pairing with pre-rRNA.
Parker KA, Steitz JA. Structural analysis of the human U3 ribonucleoprotein particle reveal a conserved sequence available for base pairing with pre-rRNA. Molecular And Cellular Biology 1987, 7: 2899-2913. PMID: 2959855, PMCID: PMC367909, DOI: 10.1128/mcb.7.8.2899.Peer-Reviewed Original ResearchConceptsProtein-RNA interactionsSecondary structureSubsequent reverse transcriptionRNA secondary structureHuman U3Phosphorylated proteinsRibonucleoprotein particleProcessing eventsAlternative functionsBase pairsNucleotides -159Specific nucleasesHeLa cellsProtein constituentsRNase ARNPProteinNonphosphorylated proteinsRRNAReverse transcriptionSequenceKilodaltonsNucleotides 65Specific reagentsTranscription