2012
Association of Argonaute proteins and microRNAs can occur after cell lysis
Riley KJ, Yario TA, Steitz JA. Association of Argonaute proteins and microRNAs can occur after cell lysis. RNA 2012, 18: 1581-1585. PMID: 22836356, PMCID: PMC3425773, DOI: 10.1261/rna.034934.112.Peer-Reviewed Original ResearchConceptsHuman AgosMiRNA-protein complexesMicroRNA target identificationDirect mRNA targetsCore protein componentsArgonaute proteinsAGO proteinsMRNA targetsImmunoprecipitation experimentsProtein componentsMiRNA mimicsRNAEndogenous interactionCell lysisTarget identificationImmunopurification techniquesGlobal analysisProteinInteraction artifactsOrigin of interactionsExperimental approachArgonauteVivoAgoMiRNAs
2002
Exclusive Interaction of the 15.5 kD Protein with the Terminal Box C/D Motif of a Methylation Guide snoRNP
Szewczak LB, DeGregorio SJ, Strobel SA, Steitz JA. Exclusive Interaction of the 15.5 kD Protein with the Terminal Box C/D Motif of a Methylation Guide snoRNP. Cell Chemical Biology 2002, 9: 1095-1107. PMID: 12401494, DOI: 10.1016/s1074-5521(02)00239-9.Peer-Reviewed Original ResearchConceptsBox C/D motifKD proteinD motifBox C/D snoRNAsBox C/D snoRNPsSite-specific methylationSpliceosomal RNAsDeleterious substitutionsD snoRNAsD snoRNPsBox DExclusive interactionsInteraction sitesXenopus oocytesSnoRNPsProteinMotifSnoRNAsVivoMethylationA89Single interaction siteRNAExocyclic amineOocytes
1994
The Epstein-Barr virus (EBV) small RNA EBER1 binds and relocalizes ribosomal protein L22 in EBV-infected human B lymphocytes.
Toczyski DP, Matera AG, Ward DC, Steitz JA. The Epstein-Barr virus (EBV) small RNA EBER1 binds and relocalizes ribosomal protein L22 in EBV-infected human B lymphocytes. Proceedings Of The National Academy Of Sciences Of The United States Of America 1994, 91: 3463-3467. PMID: 8159770, PMCID: PMC43597, DOI: 10.1073/pnas.91.8.3463.Peer-Reviewed Original ResearchConceptsEpstein-Barr virusHuman B lymphocytesB lymphocytesEBV-positive lymphocytesEBV-positive cellsEBER1 RNAUninfected human cellsCertain patientsEBER1Ribosomal protein L22LymphocytesChromosomal translocationsOncogenic herpesvirusProtein L22Situ hybridizationUninfected cell extractsNucleoplasmic stainingVivoCell transformationHigh levelsHuman cellsCellsPatientsLeukemiaCellular proteins
1991
Multiple processing-defective mutations in a mammalian histone pre-mRNA are suppressed by compensatory changes in U7 RNA both in vivo and in vitro.
Bond UM, Yario TA, Steitz JA. Multiple processing-defective mutations in a mammalian histone pre-mRNA are suppressed by compensatory changes in U7 RNA both in vivo and in vitro. Genes & Development 1991, 5: 1709-1722. PMID: 1885007, DOI: 10.1101/gad.5.9.1709.Peer-Reviewed Original ResearchConceptsHistone downstream elementHistone pre-mRNAMammalian histone pre-mRNAsPre-mRNAHeLa cellsBase pair regionMammalian histonesU7 geneSm snRNPsU7 snRNPGenetic evidenceU7 snRNAUnexpected toleranceU7 RNANuclear extractsDownstream elementsSuppressor geneCompensatory changesGenesBlock substitutionsRNAVivoSnRNPsSnRNPCells