2006
Multiple domains of EBER 1, an Epstein-Barr virus noncoding RNA, recruit human ribosomal protein L22
Fok V, Mitton-Fry RM, Grech A, Steitz JA. Multiple domains of EBER 1, an Epstein-Barr virus noncoding RNA, recruit human ribosomal protein L22. RNA 2006, 12: 872-882. PMID: 16556938, PMCID: PMC1440895, DOI: 10.1261/rna.2339606.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesCarrier ProteinsCell LineCross-Linking ReagentsElectrophoretic Mobility Shift AssayHerpesvirus 4, HumanHumansIn Vitro TechniquesMaltose-Binding ProteinsNucleic Acid ConformationPlasmidsProtein BindingProtein Structure, TertiaryRecombinant Fusion ProteinsRibosomal ProteinsRNA-Binding ProteinsRNA, UntranslatedRNA, ViralSequence DeletionTranscription, GeneticTransfectionUltraviolet Rays
1999
Frequent mutation and nuclear localization of beta-catenin in anaplastic thyroid carcinoma.
Garcia-Rostan G, Tallini G, Herrero A, D'Aquila TG, Carcangiu ML, Rimm DL. Frequent mutation and nuclear localization of beta-catenin in anaplastic thyroid carcinoma. Cancer Research 1999, 59: 1811-5. PMID: 10213482.Peer-Reviewed Original ResearchConceptsNuclear localizationSingle-strand conformational polymorphismE-cadherin-mediated cell-cell adhesionBeta-catenin actsFrequent nuclear localizationCell-cell adhesionExon 3Conformational polymorphismBeta-catenin genePhosphorylation sitesWingless pathwayTranscriptional activationCytoplasmic proteinsSubcellular localizationMobility shiftMutational analysisNucleotide sequencingDNA sequencingNuclear translocationSomatic alterationsMutationsAnaplastic thyroid carcinomaSequencingProteinFrequent mutations
1997
Parvovirus initiation factor PIF: a novel human DNA-binding factor which coordinately recognizes two ACGT motifs
Christensen J, Cotmore S, Tattersall P. Parvovirus initiation factor PIF: a novel human DNA-binding factor which coordinately recognizes two ACGT motifs. Journal Of Virology 1997, 71: 5733-5741. PMID: 9223459, PMCID: PMC191825, DOI: 10.1128/jvi.71.8.5733-5741.1997.Peer-Reviewed Original ResearchConceptsDNA-binding factorsACGT motifGel mobility shift assaysReplication initiation processMobility shift assaysHigher-order multimersParvovirus initiation factorSame cellular factorHeLa S3 cellsMouse genomeBinds DNADNA replicationACGT sequenceInitiation factorsOrigin sequencesShift assaysMinimal originMutant oligonucleotidesATP hydrolysisMobility shiftDNase ICellular factorsEssential cofactorMobility assaysSingle binding siteRAG1 and RAG2 Form a Stable Postcleavage Synaptic Complex with DNA Containing Signal Ends in V(D)J Recombination
Agrawal A, Schatz D. RAG1 and RAG2 Form a Stable Postcleavage Synaptic Complex with DNA Containing Signal Ends in V(D)J Recombination. Cell 1997, 89: 43-53. PMID: 9094713, DOI: 10.1016/s0092-8674(00)80181-6.Peer-Reviewed Original ResearchConceptsSignal endsRecombination signalsDNA-dependent protein kinaseProtein-DNA complexesSynaptic complexHMG-2 proteinStable complexesDNA adjacentProtein kinaseProteins RAG1Immunoprecipitation experimentsMobility shiftNuclease sensitivityHMG-1Cleavage systemRAG1RAG2RecombinationComplexesVivo observationsKinaseProteinImportant stepCleavage
1993
Human SR proteins and isolation of a cDNA encoding SRp75.
Zahler A, Neugebauer K, Stolk J, Roth M. Human SR proteins and isolation of a cDNA encoding SRp75. Molecular And Cellular Biology 1993, 13: 4023-4028. PMID: 8321209, PMCID: PMC359951, DOI: 10.1128/mcb.13.7.4023.Peer-Reviewed Original ResearchConceptsRNA recognition motifSR proteinsN-terminal RNA recognition motifLong C-terminal domainPolymerase II transcriptionHuman SR proteinsSR family membersC-terminal domainFamily of proteinsGlycine-rich regionApparent molecular massCDNA clonesRecognition motifSRp75Mobility shiftArginine residuesMolecular massSR domainProteinInternal regionSerineCommon epitopesActive siteFamily membersSRp55Human SR Proteins and Isolation of a cDNA Encoding SRp75
Zahler A, Neugebauer K, Stolk J, Roth M. Human SR Proteins and Isolation of a cDNA Encoding SRp75. Molecular And Cellular Biology 1993, 13: 4023-4028. DOI: 10.1128/mcb.13.7.4023-4028.1993.Peer-Reviewed Original ResearchRNA recognition motifSR proteinsN-terminal RNA recognition motifLong C-terminal domainPolymerase II transcriptionHuman SR proteinsSR family membersC-terminal domainFamily of proteinsGlycine-rich regionApparent molecular massCDNA clonesRecognition motifSRp75Mobility shiftArginine residuesMolecular massSR domainProteinInternal regionSerineCommon epitopesActive siteFamily membersSRp55
1992
A Poly(dA-dT) Upstream Activating Sequence Binds High-Mobility Group I Protein and Contributes to Lymphotoxin (Tumor Necrosis Factor-β) Gene Regulation
Fashena S, Reeves H, Ruddle N. A Poly(dA-dT) Upstream Activating Sequence Binds High-Mobility Group I Protein and Contributes to Lymphotoxin (Tumor Necrosis Factor-β) Gene Regulation. Molecular And Cellular Biology 1992, 12: 894-903. DOI: 10.1128/mcb.12.2.894-903.1992.Peer-Reviewed Original ResearchHigh-mobility group I proteinGroup I proteinLike proteinAbelson murine leukemia virus-transformed pre-B cell linesI proteinActive initiation complexHMG-I proteinDNA-binding proteinsPre-B cell linesPrimer extension analysisLT mRNASame cap siteElectrophoretic mobility shiftChromatin structureGene regulationEarly B cellsHuman HMGInitiation complexMolecular regulationTranscriptional activationExtension analysisCap siteImportant functional componentMobility shiftGene expression
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