2014
The Noncoding RNA Revolution—Trashing Old Rules to Forge New Ones
Cech TR, Steitz JA. The Noncoding RNA Revolution—Trashing Old Rules to Forge New Ones. Cell 2014, 157: 77-94. PMID: 24679528, DOI: 10.1016/j.cell.2014.03.008.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsChromatinGene Expression RegulationGenomeHumansRibonucleoproteinsRNA, CatalyticRNA, Long NoncodingRNA, UntranslatedConceptsBiological functionsRNA-protein complexesLevel of transcriptionForeign nucleic acidsMost ncRNAsLong ncRNAsNcRNA researchRNA processingGenome rearrangementsNucleic acidsNoncoding RNAsGene expressionRNA structureNcRNAsBase pairingDNA synthesisRemarkable varietySnoRNPsRiboswitchGenomeSnRNPsRNAsRibosomesTranscriptionTelomerase
2009
Subnuclear compartmentalization of transiently expressed polyadenylated pri-microRNAs: Processing at transcription sites or accumulation in SC35 foci
Pawlicki JM, Steitz JA. Subnuclear compartmentalization of transiently expressed polyadenylated pri-microRNAs: Processing at transcription sites or accumulation in SC35 foci. Cell Cycle 2009, 8: 345-356. PMID: 19177009, PMCID: PMC3004524, DOI: 10.4161/cc.8.3.7494.Peer-Reviewed Original ResearchConceptsPri-miRNA processingPri-miRNAsTranscription sitesPrimary miRNA transcriptsPri-miRNA transcriptsPre-miRNA hairpinsRNA polymerase IIASF/SF2Splicing factor SC35Target messenger RNAsNumber of proteinsMiRNA biogenesisMiRNA transcriptsNuclear organizationMRNA metabolismPolymerase IINuclear fociProlyl isomeraseFactor SC35Subnuclear compartmentalizationPri-microRNAsMammalian cellsSC35 domainsGene expressionSC35
1993
A general two-metal-ion mechanism for catalytic RNA.
Steitz TA, Steitz JA. A general two-metal-ion mechanism for catalytic RNA. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 6498-6502. PMID: 8341661, PMCID: PMC46959, DOI: 10.1073/pnas.90.14.6498.Peer-Reviewed Original ResearchConceptsMetal ionsTwo-metal-ion mechanismCatalytic metal ionPhosphoryl transfer reactionsChemical catalysisLewis acidTransfer reactionsReaction pathwaysTransition stateProtein enzymesCatalytic siteSugar hydroxylsIonsGroup I self-splicing intronCatalytic RNAReactionSelf-splicing intronsP hydrolysisCatalysisBinding sitesOxyanionsHydroxylSpecific binding sitesHydrolysisAcid
1992
Three novel functional variants of human U5 small nuclear RNA.
Sontheimer EJ, Steitz JA. Three novel functional variants of human U5 small nuclear RNA. Molecular And Cellular Biology 1992, 12: 734-746. PMID: 1310151, PMCID: PMC364287, DOI: 10.1128/mcb.12.2.734.Peer-Reviewed Original ResearchConceptsU5 small nuclear RNASmall nuclear RNANuclear RNAHeLa cellsSmall nuclear ribonucleoprotein particleTri-snRNP complexOligonucleotide-directed RNase H cleavageNuclear ribonucleoprotein particleNovel functional variantsFull-length speciesAffinity-purified spliceosomesTrimethylguanosine capAlternative splicingShorter speciesRibonucleoprotein particleMinimal domainHeLa extractsPrimer extensionFunctional variantsHigh abundanceBase changesNorthern blottingAbundant formRNASpecies
1987
Multiple interactions between the splicing substrate and small nuclear ribonucleoproteins in spliceosomes.
Chabot B, Steitz JA. Multiple interactions between the splicing substrate and small nuclear ribonucleoproteins in spliceosomes. Molecular And Cellular Biology 1987, 7: 281-293. PMID: 2951586, PMCID: PMC365068, DOI: 10.1128/mcb.7.1.281.Peer-Reviewed Original Research