1992
The murine gene encoding the highly conserved Sm B protein contains a nonfunctional alternative 3′ splice site
Griffith A, Schmauss C, Craft J. The murine gene encoding the highly conserved Sm B protein contains a nonfunctional alternative 3′ splice site. Gene 1992, 114: 195-201. PMID: 1376292, DOI: 10.1016/0378-1119(92)90574-9.Peer-Reviewed Original ResearchConceptsSplice site consensus sequenceAlternative splice sitesSplice siteGenomic sequencesSplice junctionsGenomic nucleotide sequencesAmino acid sequenceSite consensus sequencePutative branch pointGenomic lociMurine geneMurine mRNAHuman genesSm polypeptidesB geneNucleotide sequenceB polypeptidesB proteinAcid sequenceConsensus sequenceExon sequencesHuman cellsSecondary structureMurine tissuesGenes
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 componentHY3snRNPs and scRNPs as autoantigens: clues to the etiology of the connective tissue diseases
Craft J, Mamula M, Ohosone Y, Boire G, Gold H, Hardin J. snRNPs and scRNPs as autoantigens: clues to the etiology of the connective tissue diseases. Clinical Rheumatology 1990, 9: 10-19. PMID: 1697517, DOI: 10.1007/bf02205547.Peer-Reviewed Original Research
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 activityEnzymeMRPTerminusMitochondriaTranscriptsPolypeptideBindsBiochemical and immunological heterogeneity of the Ro ribonucleoprotein particles. Analysis with sera specific for the RohY5 particle.
Boire G, Craft J. Biochemical and immunological heterogeneity of the Ro ribonucleoprotein particles. Analysis with sera specific for the RohY5 particle. Journal Of Clinical Investigation 1989, 84: 270-279. PMID: 2472427, PMCID: PMC303979, DOI: 10.1172/jci114150.Peer-Reviewed Original ResearchConceptsSystemic lupus erythematosusRelated diseasesRo particleAnti-Ro autoantibodiesAnti-Ro seraCell fractionRo antibodiesSystemic lupusLupus erythematosusPatient seraImmunological heterogeneityAutoantibodiesSpecific serumRo responseNonhuman cell linesSerumAntigenic determinantsAntibodiesCell linesInhibition assaysDiseaseEpitopesCompetitive inhibitionSuch extractsErythematosus
1988
Antibodies in human serum that precipitate ribonuclease P.
Gold HA, Craft J, Hardin JA, Bartkiewicz M, Altman S. Antibodies in human serum that precipitate ribonuclease P. Proceedings Of The National Academy Of Sciences Of The United States Of America 1988, 85: 5483-5487. PMID: 2456570, PMCID: PMC281781, DOI: 10.1073/pnas.85.15.5483.Peer-Reviewed Original Research