1985
Transfer RNA is an essential component of the ubiquitin- and ATP-dependent proteolytic system.
Ciechanover A, Wolin SL, Steitz JA, Lodish HF. Transfer RNA is an essential component of the ubiquitin- and ATP-dependent proteolytic system. Proceedings Of The National Academy Of Sciences Of The United States Of America 1985, 82: 1341-1345. PMID: 2983338, PMCID: PMC397256, DOI: 10.1073/pnas.82.5.1341.Peer-Reviewed Original ResearchConceptsATP-dependent proteolytic systemProteolytic systemATP-dependent degradationATP-requiring reactionATP-dependent pathwayProteolytic activityProgression of cellsProtein substratesTransfer RNAGene activationMammalian cellsUncharged tRNAReticulocyte extractsProtein degradationTRNA fractionReticulocyte systemMouse cellsCell cycleUbiquitinEssential componentRNAGel electrophoresisTRNAConjugated proteinsAutoimmune sera
1983
A mammalian tRNA His-Containing antigen is recognized by the polymyosits-specific antibody antijo-1
Rosa M, Hendrick J, Lerner M, Steitz J, Reichlin M. A mammalian tRNA His-Containing antigen is recognized by the polymyosits-specific antibody antijo-1. Nucleic Acids Research 1983, 11: 853-870. PMID: 6188108, PMCID: PMC325757, DOI: 10.1093/nar/11.3.853.Peer-Reviewed Original ResearchConceptsMammalian cell cytoplasmWobble positionMammalian tRNAHuman HeLaProteinase K treatmentRNA sequencesBase queuineTerminal nucleotidesCell extractsTRNACell cytoplasmAntigenic proteinsImmunofluorescence studiesPhenol extractionK treatmentSephacryl SMethylated guaninesAntigenic formsTRNAHisAntigenic complexQueuineAnticodonUnusual featuresColumn chromatographyNucleotidesStructure and Function of Small Ribonucleoproteins from Eukaryotic Cells
Steitz JA, Berg C, Gottlieb E, Hardin JA, Hashimoto C, Hendrick JP, Hinterberger M, Krikeles M, Lerner MR, Mount SM, Pettersson I, Rinke J, Rosa M, Wolin S. Structure and Function of Small Ribonucleoproteins from Eukaryotic Cells. 1983, 12: 309-317. PMID: 7166547, DOI: 10.1016/b978-0-12-501650-6.50023-7.Peer-Reviewed Original ResearchConceptsSmall ribonucleoproteinLa proteinRNA polymerase III transcription factorSmall RNA-protein complexesDrosophila U1 RNAU1 small nuclearRNA-protein complexesHnRNA splicingEukaryotic cellsSmall cytoplasmicMammalian cellsRRNA precursorTranscription factorsSmall nuclearU1 RNASplice junctionsRibonucleoproteinLa ribonucleoproteinsFurther characterizationProteinRelated diseasesCellsSplicingTRNARNA
1974
High resolution proton NMR study of an isolated fragment of R17 bacteriophage mRNA
HILBERS CW, SHULMAN RG, YAMANE T, STEITZ JA. High resolution proton NMR study of an isolated fragment of R17 bacteriophage mRNA. Nature 1974, 248: 225-226. PMID: 4819416, DOI: 10.1038/248225a0.Peer-Reviewed Original ResearchConceptsHelical regionBase pairsBase pairingWatson-Crick base pairingIsolated fragmentsSecondary structureNMR spectraModel systemNuclear magnetic resonance spectraHigh-resolution nuclear magnetic resonance spectraNucleic acidsHydrogen-bonded protonsMagnetic resonance spectraProton NMR studiesAdjacent basesLeaf modelFragmentsNH protonsNMR studiesTRNAResonance spectraHigh-resolution proton NMR studiesHelixPairingGuanine