1990
Human Ro ribonucleoprotein particles: characterization of native structure and stable association with the La polypeptide.
Boire G, Craft J. Human Ro ribonucleoprotein particles: characterization of native structure and stable association with the La polypeptide. Journal Of Clinical Investigation 1990, 85: 1182-1190. PMID: 1690756, PMCID: PMC296550, DOI: 10.1172/jci114551.Peer-Reviewed Original ResearchConceptsHY4 RNAStable associationNative structurePossible functional associationRo RNPsCultured HeLa cellsRNA componentHY5 RNAFunctional associationHeLa cellsPolypeptideLa RNPsRNARNPHuman RoDiscrete subpopulationsMacromolecular targetsPotential macromolecular targetsRelated diseasesRNPsRibonucleoproteinHY1Characteristic physicochemical propertiesStable componentHY3
1989
The RNA Processing Enzyme RNase MRP Is Identical to the Th RNP and Related to RNase P
Gold H, Topper J, Clayton D, Craft J. The RNA Processing Enzyme RNase MRP Is Identical to the Th RNP and Related to RNase P. Science 1989, 245: 1377-1380. PMID: 2476849, DOI: 10.1126/science.2476849.Peer-Reviewed Original ResearchConceptsRNA processing enzymesRNase MRPMitochondrial RNA processing enzymeProcessing enzymesRNase MRP activityHuman cell extractsNucleotide sequence analysisRNP enzymeEukaryotic cellsRibonuclease PBiochemical purificationRNase PRNA componentRNA transcriptsSequence analysisCell extractsRNPMRP activityEnzymeMRPTerminusMitochondriaTranscriptsPolypeptideBinds