2004
Toxoplasma gondii: generation of novel truncation mutations in the linker domain of dihydrofolate reductase–thymidylate synthase
Belperron AA, Fox BA, O’Neil R, Peaslee KA, Horii T, Anderson AC, Bzik DJ. Toxoplasma gondii: generation of novel truncation mutations in the linker domain of dihydrofolate reductase–thymidylate synthase. Experimental Parasitology 2004, 106: 179-182. PMID: 15172226, DOI: 10.1016/j.exppara.2004.03.002.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAntiprotozoal AgentsBlotting, WesternDrug ResistanceHumansModels, GeneticMolecular Sequence DataMultienzyme ComplexesMutagenesis, InsertionalMutationPoint MutationPolymerase Chain ReactionPyrimethamineRestriction MappingSequence AlignmentTetrahydrofolate DehydrogenaseThymidylate SynthaseToxoplasmaTransfectionConceptsHigh-level pyrimethamine resistanceToxoplasma gondiiPyrimethamine resistanceNovel truncation mutationTruncation mutations
1995
A mutation in the epithelial sodium channel causing Liddle disease increases channel activity in the Xenopus laevis oocyte expression system.
Schild L, Canessa C, Shimkets R, Gautschi I, Lifton R, Rossier B. A mutation in the epithelial sodium channel causing Liddle disease increases channel activity in the Xenopus laevis oocyte expression system. Proceedings Of The National Academy Of Sciences Of The United States Of America 1995, 92: 5699-5703. PMID: 7777572, PMCID: PMC41764, DOI: 10.1073/pnas.92.12.5699.Peer-Reviewed Original ResearchConceptsLiddle's diseaseSalt-sensitive hypertensionSalt-sensitive formsChannel activityXenopus laevis oocyte expression systemDirect physiological evidenceChannel beta subunitsEpithelial sodium channelChannel hyperactivityOocyte expression systemPharmacological propertiesSodium channelsGamma subunitsMolecular targetsBeta subunitDiseaseXenopus laevis oocytesHypertensionPremature stop codonPhysiological evidenceHeritable formTruncation mutationsOverall channel activityFunctional consequencesLaevis oocytes
1993
A multisubunit complex associated with the RNA polymerase II CTD and TATA-binding protein in yeast
Thompson C, Koleske A, Chao D, Young R. A multisubunit complex associated with the RNA polymerase II CTD and TATA-binding protein in yeast. Cell 1993, 73: 1361-1375. PMID: 8324825, DOI: 10.1016/0092-8674(93)90362-t.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesDNA Mutational AnalysisDNA-Binding ProteinsFungal ProteinsGene Expression RegulationMediator ComplexMolecular Sequence DataMultienzyme ComplexesRecombinant ProteinsRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTATA-Box Binding ProteinTranscription FactorsTranscription, GeneticConceptsTATA-binding proteinRNA polymerase II carboxy-terminal domainCarboxy-terminal domainMultisubunit complexLarge multisubunit complexFunctional preinitiation complexRNA polymerase IIEfficient transcription initiationTranscription initiation complexSRB proteinsCTD proteinsExtragenic suppressorsCTD functionPolymerase IIPreinitiation complexTranscription initiationInitiation complexComplex bindsTruncation mutationsSRB2Srb5ProteinBiochemical evidenceComplexesSRB4
1992
A novel transcription factor reveals a functional link between the RNA polymerase II CTD and TFIID
Koleske A, Buratowski S, Nonet M, Young R. A novel transcription factor reveals a functional link between the RNA polymerase II CTD and TFIID. Cell 1992, 69: 883-894. PMID: 1591782, DOI: 10.1016/0092-8674(92)90298-q.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceBlotting, WesternChromatography, AffinityFungal ProteinsGenes, SuppressorMediator ComplexMolecular Sequence DataMutationRecombinant Fusion ProteinsRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription Factor TFIIDTranscription FactorsTranscription, GeneticConceptsCarboxy-terminal domainRNA polymerase II carboxy-terminal domainNovel transcription factorTranscription initiation complexInitiation complexTranscription factorsFunctional linkConditional growth phenotypesTranscription initiation apparatusRNA polymerase IITATA-binding factorDominant suppressorsPolymerase IIGrowth phenotypeTranscription initiationGene expressionAllele specificitySRB2Truncation mutationsSame functionSimilar defectsTFIIDSuppressorEfficient establishmentMechanism of action
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