2011
Human eIF4AIII interacts with an eIF4G-like partner, NOM1, revealing an evolutionarily conserved function outside the exon junction complex
Alexandrov A, Colognori D, Steitz JA. Human eIF4AIII interacts with an eIF4G-like partner, NOM1, revealing an evolutionarily conserved function outside the exon junction complex. Genes & Development 2011, 25: 1078-1090. PMID: 21576267, PMCID: PMC3093123, DOI: 10.1101/gad.2045411.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsDEAD-box RNA HelicasesEukaryotic Initiation Factor-4AEukaryotic Initiation Factor-4GEvolution, MolecularExonsGene DeletionGenetic Complementation TestHumansModels, MolecularMolecular Sequence DataMutationNuclear ProteinsPhenotypeProtein Structure, TertiaryRNA, Ribosomal, 18SRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentConceptsExon junction complexEIF4GJunction complexDEAD-box helicasePre-rRNA processingDirect physical interactionEIF4G complexExtragenic suppressorsBiogenesis defectsLethal phenotypeGrowth defectTranslation initiationHuman orthologEIF4AIIISaccharomyces cerevisiaeHuman cellsNOM1Physical interactionComplex actsG complexX-ray structureMutationsResiduesComplexesOrthologs
1997
A new method for detecting sites of 2'-O-methylation in RNA molecules.
Yu YT, Shu MD, Steitz JA. A new method for detecting sites of 2'-O-methylation in RNA molecules. RNA 1997, 3: 324-31. PMID: 9056769, PMCID: PMC1369484.Peer-Reviewed Original ResearchConceptsRNA moleculesEukaryotic ribosomal RNALong RNA moleculesSpecific rRNARibosomal RNAModification sitesRRNAMethylationCell nucleoliChimeric oligonucleotideSnoRNAsRNase H cleavagePrecursor moleculesRRNA transportSitesMoleculesRNANucleotidesCytoplasmNucleoliResiduesCleavageOligonucleotideH cleavageNucleus
1968
Isolation of the A protein from bacteriophage R17
Steitz J. Isolation of the A protein from bacteriophage R17. Journal Of Molecular Biology 1968, 33: 937-945. PMID: 5700426, DOI: 10.1016/0022-2836(68)90329-x.Peer-Reviewed Original Research