2016
Development of a Quantitative PCR Assay for Detection of Human Insulin-Like Growth Factor Receptor and Insulin Receptor Isoforms
Flannery CA, Rowzee AM, Choe GH, Saleh FL, Radford CC, Taylor HS, Wood TL. Development of a Quantitative PCR Assay for Detection of Human Insulin-Like Growth Factor Receptor and Insulin Receptor Isoforms. Endocrinology 2016, 157: 1702-1708. PMID: 26862994, PMCID: PMC4816738, DOI: 10.1210/en.2015-1698.Peer-Reviewed Original ResearchConceptsSplice variantsInsulin-like growth factor (IGF) ligandsInsulin-like growth factor receptorGrowth factor ligandsSpecific molecular signaturesQuantitative PCR assaysGrowth factor receptorHigh homologyMRNA sequencesQuantitative RT-PCRIGF-1 receptorFactor ligandInsulin receptor isoformsCompetition assaysPrimer pairsRelative abundanceInsulin receptorMolecular signaturesCell typesDifferent tissuesIGF-1R mRNAFactor receptorExpression levelsGel electrophoresisReceptor isoforms
2013
Transport assays in filamentous fungi: Kinetic characterization of the UapC purine transporter of Aspergillus nidulans
Krypotou E, Diallinas G. Transport assays in filamentous fungi: Kinetic characterization of the UapC purine transporter of Aspergillus nidulans. Fungal Genetics And Biology 2013, 63: 1-8. PMID: 24355588, DOI: 10.1016/j.fgb.2013.12.004.Peer-Reviewed Original ResearchConceptsFilamentous ascomycete Aspergillus nidulansUric acid-xanthine transporterSpecificity profileAscomycete Aspergillus nidulansTransport assaysNucleobase-ascorbate transporter familySubstrate specificity profileMeasured apparent KmGenetic null mutantsAspergillus nidulansA. nidulansNull mutantsFilamentous fungiGerminating conidiosporesTransporter familyKinetic characterizationGenetic backgroundCompetition assaysVmax valuesMaximal expressionApparent KmUapCMorphological stagesAssayKinetic analysis
1999
A dimer of the lymphoid protein RAG1 recognizes the recombination signal sequence and the complex stably incorporates the high mobility group protein HMG2
Rodgers K, Villey I, Ptaszek L, Corbett E, Schatz D, Coleman J. A dimer of the lymphoid protein RAG1 recognizes the recombination signal sequence and the complex stably incorporates the high mobility group protein HMG2. Nucleic Acids Research 1999, 27: 2938-2946. PMID: 10390537, PMCID: PMC148510, DOI: 10.1093/nar/27.14.2938.Peer-Reviewed Original ResearchConceptsRecombination signal sequencesSignal sequenceCore RAG1RAG1/RAG2 complexAbsence of RAG2Lymphoid-specific proteinsElectrophoretic mobility shift assaysSingle recombination signal sequencesMobility shift assaysRAG1 proteinProteins RAG1DNA sequencesMinimal speciesShift assaysOligomeric complexesHeptamer sequenceCompetition assaysRAG1Escherichia coliOligomeric formsRAG2Cleavage activityHMG2ProteinJ region
1993
Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor.
Lechleider R, Sugimoto S, Bennett A, Kashishian A, Cooper J, Shoelson S, Walsh C, Neel B. Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor. Journal Of Biological Chemistry 1993, 268: 21478-21481. PMID: 7691811, DOI: 10.1016/s0021-9258(20)80562-6.Peer-Reviewed Original ResearchConceptsSH-PTP2Platelet-derived growth factor receptorGrowth factor receptorPhosphotyrosyl peptidesFactor receptorSrc homology 2 domainHuman platelet-derived growth factor receptorIntrinsic tyrosine kinase activityPeptide competition assaysTyrosine kinase activitySH2 domainPhosphorylation sitesSignal transductionKinase activityMajor binding siteImmunoprecipitation studiesCompetition assaysTyrosyl residuesBinding sitesEarly eventsProteinLigand additionActivity 5ReceptorsDocking point
1992
Competition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation
Sherman J, Rogers M, Söll D. Competition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation. Nucleic Acids Research 1992, 20: 2847-2852. PMID: 1377381, PMCID: PMC336931, DOI: 10.1093/nar/20.11.2847.Peer-Reviewed Original ResearchConceptsAccuracy of aminoacylationAminoacyl-tRNA synthetasesTyrosyl-tRNA synthetaseE. coli tyrosyl-tRNA synthetaseEscherichia coli tyrosyl-tRNA synthetaseGlutaminyl-tRNA synthetaseLevel of aminoacylationProtein biosynthesisTRNASynthetasesAminoacylationCompetition assaysDiscriminator baseDifferent synthetasesConcurrent overexpressionCorrect aminoacylationSynthetaseFirst baseRelative affinityVivoMisacylationAssaysAnticodonBiosynthesisCompetitionCompetition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation
Sherman J, Rogers M, Söll D. Competition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation. Nucleic Acids Research 1992, 20: 1547-1552. PMID: 16617497, PMCID: PMC312236, DOI: 10.1093/nar/20.7.1547.Peer-Reviewed Original ResearchAccuracy of aminoacylationAminoacyl-tRNA synthetasesTyrosyl-tRNA synthetaseE. coli tyrosyl-tRNA synthetaseEscherichia coli tyrosyl-tRNA synthetaseGlutaminyl-tRNA synthetaseLevel of aminoacylationProtein biosynthesisTRNASynthetasesAminoacylationCompetition assaysDiscriminator baseDifferent synthetasesConcurrent overexpressionCorrect aminoacylationSynthetaseFirst baseRelative affinityVivoMisacylationAssaysAnticodonBiosynthesisCompetition
1986
N protein is the predominant antigen recognized by vesicular stomatitis virus-specific cytotoxic T cells
Puddington L, Bevan M, Rose J, Lefrançois L. N protein is the predominant antigen recognized by vesicular stomatitis virus-specific cytotoxic T cells. Journal Of Virology 1986, 60: 708-717. PMID: 3022003, PMCID: PMC288945, DOI: 10.1128/jvi.60.2.708-717.1986.Peer-Reviewed Original ResearchConceptsN proteinCell linesAnti-vesicular stomatitis virusEL4 cell linePlasma membraneG proteinsVSV genesCompetition assaysProteinNucleocapsid proteinInfected cellsStomatitis virusSodium butyrateGenesEfficient competitorsVSVEL4 cellsCold target competition assaysCellsT cellsCompetition studiesTarget cellsCytotoxic T cellsAssaysImmunoprecipitation
1983
Transcription of eukaryotic tRNA genes in vitro. I. Analysis of control regions using a competition assay.
Sharp S, Dingermann T, Schaack J, DeFranco D, Söll D. Transcription of eukaryotic tRNA genes in vitro. I. Analysis of control regions using a competition assay. Journal Of Biological Chemistry 1983, 258: 2440-2446. PMID: 6549757, DOI: 10.1016/s0021-9258(18)32945-4.Peer-Reviewed Original ResearchConceptsT-control regionD-control regionTRNA gene transcriptionTRNAArg geneControl regionTranscription factorsCompetitive abilityDeletion mutantsGene transcriptionEukaryotic tRNA gene transcriptionDrosophila tRNAArg geneEukaryotic tRNA genesStem regionIntragenic control regionEfficiency of transcriptionTRNA genesTranscription extractTRNA productD-loopTranscription levelsWild typeTranscriptionT-loopGenesCompetition assays
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