2002
Transgenic Overexpression of Interleukin (IL)-10 in the Lung Causes Mucus Metaplasia, Tissue Inflammation, and Airway Remodeling via IL-13-dependent and -independent Pathways*
Lee CG, Homer RJ, Cohn L, Link H, Jung S, Craft JE, Graham BS, Johnson TR, Elias JA. Transgenic Overexpression of Interleukin (IL)-10 in the Lung Causes Mucus Metaplasia, Tissue Inflammation, and Airway Remodeling via IL-13-dependent and -independent Pathways*. Journal Of Biological Chemistry 2002, 277: 35466-35474. PMID: 12107190, DOI: 10.1074/jbc.m206395200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceChloride ChannelsCloning, MolecularDNA PrimersFluorescent Antibody TechniqueGene Expression RegulationIn Situ HybridizationInflammationInterleukin-10Interleukin-13LungMiceMice, TransgenicMolecular Sequence DataMucoproteinsMucous MembranePhenotypePolymerase Chain ReactionReceptors, Interleukin-4STAT6 Transcription FactorTrans-ActivatorsConceptsMucus metaplasiaIL-10Tissue inflammationIL-13Tumor necrosis factor productionIL-13/ILLipopolysaccharide-induced inflammationNecrosis factor productionAirway fibrosisNeutrophil accumulationAirway remodelingSubepithelial fibrosisGob-5Levels of mRNAMetaplasiaInflammationTransgenic miceFibrosisSTAT-6Effector propertiesTransgenic overexpressionFactor productionMiceInterleukinMultiple mechanisms
2001
Cd4+ T Cells from Lupus-Prone Mice Are Hyperresponsive to T Cell Receptor Engagement with Low and High Affinity Peptide Antigens
Vratsanos G, Jung S, Park Y, Craft J. Cd4+ T Cells from Lupus-Prone Mice Are Hyperresponsive to T Cell Receptor Engagement with Low and High Affinity Peptide Antigens. Journal Of Experimental Medicine 2001, 193: 329-338. PMID: 11157053, PMCID: PMC2195926, DOI: 10.1084/jem.193.3.329.Peer-Reviewed Original ResearchConceptsT cell receptorLupus-prone miceT cellsT cell activationPigeon cytochrome cAlpha/beta T cellsCell activationTransgenic T cell receptorBeta T cellsAntigen-presenting cellsCBA/CaJT cell receptor engagementLow affinityBeta-chain geneMRL/Cell receptor engagementPolyclonal activationSpontaneous lupusAmino acids 88Cognate antigenCell receptorAntigenPeptide ligandsReceptor engagementLupus
1998
Central T cell tolerance in lupus-prone mice: influence of autoimmune background and the lpr mutation.
Fatenejad S, Peng SL, Disorbo O, Craft J. Central T cell tolerance in lupus-prone mice: influence of autoimmune background and the lpr mutation. The Journal Of Immunology 1998, 161: 6427-32. PMID: 9834135, DOI: 10.4049/jimmunol.161.11.6427.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsApoptosisAutoimmune DiseasesCell LineClonal DeletionColumbidaeCytochrome c GroupDown-RegulationFas ReceptorGene Rearrangement, alpha-Chain T-Cell Antigen ReceptorImmune ToleranceLupus NephritisLymphocyte ActivationMiceMice, Inbred C57BLMice, Inbred MRL lprMice, TransgenicMolecular Sequence DataMutationPeptidesReceptors, Antigen, T-Cell, alpha-betaThymus GlandT-Lymphocyte SubsetsConceptsMRL/MpJ miceLupus-prone miceT cell toleranceCentral T cell toleranceT cellsLpr mutationCell toleranceSystemic autoimmune diseaseT cell autoreactivityAutoreactive T cellsB cell helpIntrathymic negative selectionMHC class IIMRL/MpJPeripheral control mechanismsAutoimmune backgroundThymic deletionIntrathymic deletionAutoimmune diseasesNonautoimmune miceCell helpTCR transgeneNonautoimmune strainsPeptide AgImmature CD4
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 oligoribonucleotideNucleoliAutoimmune lpr/lpr mice deficient in CD40 ligand: spontaneous Ig class switching with dichotomy of autoantibody responses.
Ma J, Xu J, Madaio MP, Peng Q, Zhang J, Grewal IS, Flavell RA, Craft J. Autoimmune lpr/lpr mice deficient in CD40 ligand: spontaneous Ig class switching with dichotomy of autoantibody responses. The Journal Of Immunology 1996, 157: 417-26. PMID: 8683147, DOI: 10.4049/jimmunol.157.1.417.Peer-Reviewed Original ResearchConceptsLpr/lpr miceLpr miceIgG autoantibodiesAutoantibody responseCD40 ligandAutoimmune lpr/lpr miceMRL/Mp-lpr/lpr miceHuman systemic lupus erythematosusSystemic lupus erythematosusAge 3 moIgG rheumatoid factorB cell contactSubset of animalsOvert glomerulonephritisLupus erythematosusIgG2b levelsHistologic evidenceRheumatoid factorSerum IgMAb synthesisAutoantibodiesLpr animalsMiceIg classesElevated levelsMHC class I polymorphism in lupus-prone MRL/Mp mice.
Peng SL, Craft J. MHC class I polymorphism in lupus-prone MRL/Mp mice. Immunogenetics 1996, 44: 407-8. PMID: 8781130.Peer-Reviewed Original Research
1995
T cells with gamma/delta T cell receptors (TCR) of intestinal type are preferentially expanded in TCR-alpha-deficient lpr mice.
Hughes DP, Hayday A, Craft JE, Owen MJ, Crispe IN. T cells with gamma/delta T cell receptors (TCR) of intestinal type are preferentially expanded in TCR-alpha-deficient lpr mice. Journal Of Experimental Medicine 1995, 182: 233-241. PMID: 7540652, PMCID: PMC2192080, DOI: 10.1084/jem.182.1.233.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, SurfaceApoptosisBase SequenceCell DivisionCell MovementDNA Transposable ElementsFas ReceptorImmunophenotypingIntestinal MucosaLymph NodesLymphocyte CountLymphoproliferative DisordersMiceMice, KnockoutMice, Mutant StrainsMolecular Sequence DataReceptors, Antigen, T-Cell, alpha-betaReceptors, Antigen, T-Cell, gamma-deltaSpecific Pathogen-Free OrganismsT-Lymphocyte SubsetsConceptsLpr/lpr miceT cell receptorIntestinal intraepithelial lymphocytesLpr miceT cellsIntraepithelial lymphocytesAlpha/beta T cellsGamma/delta T cell receptorGamma/delta T cellsLymph node cell numberTCR gamma/deltaDelta T-cell receptorFas-deficient lpr micePeripheral lymphoid systemT-cell contributionPeripheral lymph nodesBeta T cellsDelta T cellsActivation-induced cell deathGene-ablated miceRole of FasT cell developmentLymph nodesIntestinal typeLymphoid system
1993
Nucleotide sequence analysis of the A protein of the U1 small nuclear ribonucleoprotein particle: the murine protein contains a 5' amino-terminal tag
Bennett M, Baron M, Craft J. Nucleotide sequence analysis of the A protein of the U1 small nuclear ribonucleoprotein particle: the murine protein contains a 5' amino-terminal tag. Nucleic Acids Research 1993, 21: 4404-4404. PMID: 8415008, PMCID: PMC310090, DOI: 10.1093/nar/21.18.4404.Peer-Reviewed Original ResearchIdentification of autoantibodies to RNA polymerase II. Occurrence in systemic sclerosis and association with autoantibodies to RNA polymerases I and III.
Hirakata M, Okano Y, Pati U, Suwa A, Medsger TA, Hardin JA, Craft J. Identification of autoantibodies to RNA polymerase II. Occurrence in systemic sclerosis and association with autoantibodies to RNA polymerases I and III. Journal Of Clinical Investigation 1993, 91: 2665-2672. PMID: 8390487, PMCID: PMC443330, DOI: 10.1172/jci116505.Peer-Reviewed Original ResearchConceptsSystemic sclerosisII antibodiesAnti-RNA polymerase II antibodiesLimited cutaneous diseaseConnective tissue diseaseIdentification of autoantibodiesSera of patientsIndirect immunofluorescence studiesHuman serumTissue diseaseCutaneous diseaseNormal controlsAutoantibodiesSclerosisPatientsHuman antibodiesRNA polymerase IIClinical perspectiveMonoclonal antibodiesAntibodiesSerumRNA polymerase IImmunofluorescence studiesImmunodepletion studiesFurther studiesAutoantigenic epitopes of the B and D polypeptides of the U1 snRNP. Analysis of domains recognized by the Y12 monoclonal anti-Sm antibody and by patient sera.
Hirakata M, Craft J, Hardin JA. Autoantigenic epitopes of the B and D polypeptides of the U1 snRNP. Analysis of domains recognized by the Y12 monoclonal anti-Sm antibody and by patient sera. The Journal Of Immunology 1993, 150: 3592-601. PMID: 7682245, DOI: 10.4049/jimmunol.150.8.3592.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAntibodies, MonoclonalAutoantigensBinding Sites, AntibodyEnzyme-Linked Immunosorbent AssayEpitopesHumansImmune SeraLupus Erythematosus, SystemicMiceMolecular Sequence DataProtein ConformationRibonucleoprotein, U1 Small NuclearRibonucleoproteins, Small NuclearSnRNP Core ProteinsConceptsAnti-Sm antibodiesMonoclonal anti-Sm antibodyPatient seraCross-reactive epitopesAutoantigenic epitopesAnti-Sm seraPolypeptide BD polypeptideAnti-Sm patient seraSerumSpecific markersSm small nuclear ribonucleoproteinsEpitopesEnd deletionsAntibodiesImmunoreactive sitesCorresponding synthetic peptideB'/BMAbsDeletion studiesPresent studyLittle amino acid sequence homologySynthetic peptidesAmino acid sequence homologySLEBinding of Ku protein to DNA. Measurement of affinity for ends and demonstration of binding to nicks.
Blier PR, Griffith AJ, Craft J, Hardin JA. Binding of Ku protein to DNA. Measurement of affinity for ends and demonstration of binding to nicks. Journal Of Biological Chemistry 1993, 268: 7594-7601. PMID: 8463290, DOI: 10.1016/s0021-9258(18)53216-6.Peer-Reviewed Original ResearchComparison of the drosophila melanogaster, human and murine sm b cDNAs: evolutionary conservation
Brunet C, Quan T, Craft J. Comparison of the drosophila melanogaster, human and murine sm b cDNAs: evolutionary conservation. Gene 1993, 124: 269-273. PMID: 7680326, DOI: 10.1016/0378-1119(93)90404-q.Peer-Reviewed Original ResearchConceptsD. melanogaster proteinB polypeptidesConservative aa substitutionsCDNA nucleotide sequenceDeduced aa sequencesC-terminal portionEvolutionary conservationDrosophila melanogasterMouse clonesNucleotide sequenceB proteinSequence identityAa sequencesB cDNAReticulocyte lysateEvolutionary stabilityMurine cellsSpecies linesAmino acidsCDNAProtein BProteinAa substitutionsHuman anti-Sm antibodyCell lines
1992
Autoantigenic epitopes of the b polypeptide of SM small nuclear RNP particles
Ohosone Y, Mimori T, Fujii T, Akizuki M, Matsuoka Y, Irimajiri S, Hardin J, Craft J, Homma M. Autoantigenic epitopes of the b polypeptide of SM small nuclear RNP particles. Arthritis & Rheumatism 1992, 35: 960-966. PMID: 1379432, DOI: 10.1002/art.1780350818.Peer-Reviewed Original ResearchThe 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 tissuesGenesNucleotide sequence and genomic structure analyses of the p70 subunit of the human Ku autoantigen: evidence for a family of genes encoding Ku (p70)-related polypeptides
Griffith A, Craft J, Evans J, Mimori T, Hardin J. Nucleotide sequence and genomic structure analyses of the p70 subunit of the human Ku autoantigen: evidence for a family of genes encoding Ku (p70)-related polypeptides. Molecular Biology Reports 1992, 16: 91-97. PMID: 1608402, DOI: 10.1007/bf00419754.Peer-Reviewed Original ResearchConceptsHuman Ku autoantigenKu autoantigenGenomic structure analysisFamily of genesHomologous DNA sequencesOpen reading frameEntire open reading frameNucleotide sequence analysisAmino acid polymorphismsSouthern blot analysisP70 polypeptidesHuman genomeReading frameDNA sequencesNucleotide sequenceP70 subunitMultiple genesExpression analysisSequence analysisAcid polymorphismsMultiple copiesBlot analysisPolypeptideGenesSequence
1990
New RNPs of higher eukaryotes
Craft J, Gold H. New RNPs of higher eukaryotes. Molecular Biology Reports 1990, 14: 97-101. PMID: 2194112, DOI: 10.1007/bf00360432.Peer-Reviewed Original ResearchsnRNPs 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
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 ResearchMeSH KeywordsAutoantigensBase SequenceCell NucleusEndoribonucleasesHumansMitochondriaMolecular Sequence DataRibonuclease PRibonucleoproteinsRNARNA Processing, Post-TranscriptionalConceptsRNA processing enzymesRNase MRPMitochondrial RNA processing enzymeProcessing enzymesRNase MRP activityHuman cell extractsNucleotide sequence analysisRNP enzymeEukaryotic cellsRibonuclease PBiochemical purificationRNase PRNA componentRNA transcriptsSequence analysisCell extractsRNPMRP activityEnzymeMRPTerminusMitochondriaTranscriptsPolypeptideBindsMolecular cloning of cDNA encoding Sm autoantigen: derivation of a cDNA for a B polypeptide of the U series of small nuclear ribonucleoprotein particles.
Ohosone Y, Mimori T, Griffith A, Akizuki M, Homma M, Craft J, Hardin JA. Molecular cloning of cDNA encoding Sm autoantigen: derivation of a cDNA for a B polypeptide of the U series of small nuclear ribonucleoprotein particles. Proceedings Of The National Academy Of Sciences Of The United States Of America 1989, 86: 4249-4253. PMID: 2524838, PMCID: PMC287428, DOI: 10.1073/pnas.86.11.4249.Peer-Reviewed Original ResearchConceptsSystemic lupus erythematosusSm snRNPsHuman fibroblast cDNA libraryAmino acidsAlternative splicing mechanismLupus erythematosusFibroblast cDNA librarySmall nuclear ribonucleoproteinOpen reading frameAmino acid sequenceSplicing mechanismMolecular cloningCDNA libraryNuclear ribonucleoproteinReading frameAnti-Sm antibodiesB polypeptidesAcid sequenceCOOH terminusNH2 terminusCDNAComplete homologySnRNPsPolypeptide NPolypeptide