1996
Association of RNase mitochondrial RNA processing enzyme with ribonuclease P in higher ordered structures in the nucleolus: a possible coordinate role in ribosome biogenesis.
Lee B, Matera AG, Ward DC, Craft J. Association of RNase mitochondrial RNA processing enzyme with ribonuclease P in higher ordered structures in the nucleolus: a possible coordinate role in ribosome biogenesis. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 11471-11476. PMID: 8876159, PMCID: PMC38081, DOI: 10.1073/pnas.93.21.11471.Peer-Reviewed Original ResearchConceptsMitochondrial RNA processing enzymeRibosomal RNA maturationRNA processing enzymesRNA maturationRibonuclease PRNase PProcessing enzymesSitu hybridization experimentsRNA structural motifsRibosome biogenesisRibosome assemblySmall subpopulationRibonucleoprotein particleRNA componentMacromolecular complexesRNA transcriptsHybridization experimentsFractionation experimentsCoordinate roleCytoplasmic structuresAffinity selectionEnzymeStructural motifsMethyl oligoribonucleotideNucleoli
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
An immunological determinant of RNase P protein is conserved between Escherichia coli and humans.
Mamula MJ, Baer M, Craft J, Altman S. An immunological determinant of RNase P protein is conserved between Escherichia coli and humans. Proceedings Of The National Academy Of Sciences Of The United States Of America 1989, 86: 8717-8721. PMID: 2479027, PMCID: PMC298359, DOI: 10.1073/pnas.86.22.8717.Peer-Reviewed Original ResearchThe 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