2017
Mutations in KDSR Cause Recessive Progressive Symmetric Erythrokeratoderma
Boyden LM, Vincent NG, Zhou J, Hu R, Craiglow BG, Bayliss SJ, Rosman IS, Lucky AW, Diaz LA, Goldsmith LA, Paller AS, Lifton RP, Baserga SJ, Choate KA. Mutations in KDSR Cause Recessive Progressive Symmetric Erythrokeratoderma. American Journal Of Human Genetics 2017, 100: 978-984. PMID: 28575652, PMCID: PMC5473720, DOI: 10.1016/j.ajhg.2017.05.003.Peer-Reviewed Original ResearchConceptsYeast complementation studiesNew genetic determinantsCeramide synthesis pathwayKb inversionComplementation studiesRecessive Mendelian disordersCDNA sequencingGenome sequencingCeramide generationMendelian disordersSynthesis pathwayBase changesGenetic determinantsMutationsSequencingExome sequencingRetinoic acidProgressive symmetric erythrokeratodermaEpidermal functionMultiple probandsAlternative pathwayPathwayScaly skinSplicingExons
2016
Carcinogenesis: UV Radiation
Brash D, Heffernan T, Nghiem P, Cho R. Carcinogenesis: UV Radiation. 2016, 887-902. DOI: 10.1007/978-3-662-47398-6_56.ChaptersLarge-scale sequencing projectsUV-damaged cellsSequencing projectsDNA repairTumor suppressorSomatic point mutationsSurveillance mechanismClonal growthLow-frequency mutationsDNA damageBase changesCell behaviorPoint mutationsMutationsSomatic mutationsFree radical clearanceHuman skin cancerFrequency mutationsSpecific somatic mutationsUltraviolet radiationPTCH mutationsGenetic factorsNOTCH1 mutationsCellsVast number
2015
Carcinogenesis: UV Radiation
Brash D, Heffernan T, Nghiem P, Cho R. Carcinogenesis: UV Radiation. 2015, 1-17. DOI: 10.1007/978-3-642-27814-3_56-2.ChaptersLarge-scale sequencing projectsUV-damaged cellsSequencing projectsDNA repairTumor suppressorSomatic point mutationsSurveillance mechanismClonal growthLow-frequency mutationsDNA damageBase changesCell behaviorPoint mutationsMutationsSomatic mutationsFree radical clearanceHuman skin cancerFrequency mutationsSpecific somatic mutationsUltraviolet radiationPTCH mutationsGenetic factorsNOTCH1 mutationsCellsVast number
2011
MicroRNA Biomarkers in Melanoma
Kozubek J, Altaf F, Dadras S. MicroRNA Biomarkers in Melanoma. Current Clinical Pathology 2011, 113-126. DOI: 10.1007/978-1-60761-433-3_9.Peer-Reviewed Original ResearchGenome-wide association studiesSingle base changeComplex traitsSingle nucleotide polymorphismsSystems biologyAssociation studiesBase changesCell scienceNucleotide polymorphismsRare mutationsCancer cellsCommon setGenomeCellsFunctional alterationsIncognitaBiologyTraitsProteinMutationsMicroRNA biomarkersPolymorphismDogma
1996
Normal Replication of Vesicular Stomatitis Virus without C Proteins
KRETZSCHMAR E, PELUSO R, SCHNELL M, WHITT M, ROSE J. Normal Replication of Vesicular Stomatitis Virus without C Proteins. Virology 1996, 216: 309-316. PMID: 8607260, DOI: 10.1006/viro.1996.0066.Peer-Reviewed Original ResearchConceptsP geneWild-type virusNormal replicationSmall basic proteinP protein sequenceSingle base changeNew Jersey serotypeWild-type virus particlesInsect vectorsVesicular stomatitis virusC proteinStop codonViral mRNAsVSV growthInfectious cloneBase changesMutant virusProteinGenesStomatitis virusViral pathogenesisBasic proteinM proteinVirus particlesTissue culture
1995
Pseudohypoparathyroidism type Ib is not caused by mutations in the coding exons of the human parathyroid hormone (PTH)/PTH-related peptide receptor gene
Schipani E, Weinstein LS, Bergwitz C, Iida-Klein A, Kong XF, Stuhrmann M, Kruse K, Whyte MP, Murray T, Schmidtke J. Pseudohypoparathyroidism type Ib is not caused by mutations in the coding exons of the human parathyroid hormone (PTH)/PTH-related peptide receptor gene. The Journal Of Clinical Endocrinology & Metabolism 1995, 80: 1611-1621. PMID: 7745008, DOI: 10.1210/jcem.80.5.7745008.Peer-Reviewed Original ResearchConceptsPseudohypoparathyroidism type IbPHP-IbCoding exonsExon GNucleotide sequenceBase changesHuman genomic DNA clonesExon E2Receptor geneTemperature gradient gel electrophoresisGenomic DNA clonesRestriction enzyme mappingReceptor cytoplasmic tailPHP-Ib patientsPTH/PTH-related peptideReverse transcriptase-polymerase chain reactionSplice donor sitePTH/PTHrP receptor geneTranscriptase-polymerase chain reactionGradient gel electrophoresisType IbChain reactionDirect nucleotide sequencingWild-type receptorNorthern blot analysis
1992
Recognition of bases in Escherichia coli tRNA(Gln) by glutaminyl‐tRNA synthetase: a complete identity set.
Hayase Y, Jahn M, Rogers M, Sylvers L, Koizumi M, Inoue H, Ohtsuka E, Söll D. Recognition of bases in Escherichia coli tRNA(Gln) by glutaminyl‐tRNA synthetase: a complete identity set. The EMBO Journal 1992, 11: 4159-4165. PMID: 1396597, PMCID: PMC556926, DOI: 10.1002/j.1460-2075.1992.tb05509.x.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseRecognition of basesSet of tRNAsEscherichia coliCognate aminoacyl-tRNA synthetasesAminoacyl-tRNA synthetasesCorrect aminoacylationRecombinant RNA technologySet of nucleotidesNumber of mutantsGlutamine identityTRNA genesTRNA discriminationTransfer RNAExcellent systemGlnRFunctional importanceSingle deletionSpecific contactsRNA technologyBase changesSpecificity constantAminoacylationSpecific guanosineMutantsThree Novel Functional Variants of Human U5 Small Nuclear RNA
Sontheimer E, Steitz J. Three Novel Functional Variants of Human U5 Small Nuclear RNA. Molecular And Cellular Biology 1992, 12: 734-746. DOI: 10.1128/mcb.12.2.734-746.1992.Peer-Reviewed Original ResearchU5 small nuclear RNASmall nuclear RNAHeLa cellsNuclear RNAAffinity-purified spliceosomesSmall nuclear ribonucleoproteinTri-snRNP complexFull-length speciesSaccharomyces cerevisiaeSplicing extractsPrimer extensionUS variantsHeLa extractsAlternative splicingRNA blotsShort speciesNuclear ribonucleoproteinBase changesMinimal domainHigher abundanceNorthern blottingRNAHeLaAbundant formSplicingThree novel functional variants of human U5 small nuclear RNA.
Sontheimer EJ, Steitz JA. Three novel functional variants of human U5 small nuclear RNA. Molecular And Cellular Biology 1992, 12: 734-746. PMID: 1310151, PMCID: PMC364287, DOI: 10.1128/mcb.12.2.734.Peer-Reviewed Original ResearchConceptsU5 small nuclear RNASmall nuclear RNANuclear RNAHeLa cellsSmall nuclear ribonucleoprotein particleTri-snRNP complexOligonucleotide-directed RNase H cleavageNuclear ribonucleoprotein particleNovel functional variantsFull-length speciesAffinity-purified spliceosomesTrimethylguanosine capAlternative splicingShorter speciesRibonucleoprotein particleMinimal domainHeLa extractsPrimer extensionFunctional variantsHigh abundanceBase changesNorthern blottingAbundant formRNASpeciesThree Novel Functional Variants of Human U5 Small Nuclear RNA
Sontheimer E, Steitz J. Three Novel Functional Variants of Human U5 Small Nuclear RNA. Molecular And Cellular Biology 1992, 12: 734-746. DOI: 10.1128/mcb.12.2.734-746.1992.Peer-Reviewed Original ResearchU5 small nuclear RNASmall nuclear RNANuclear RNAHeLa cellsSmall nuclear ribonucleoprotein particleTri-snRNP complexOligonucleotide-directed RNase H cleavageNuclear ribonucleoprotein particleNovel functional variantsFull-length speciesAffinity-purified spliceosomesTrimethylguanosine capAlternative splicingShorter speciesRibonucleoprotein particleMinimal domainHeLa extractsPrimer extensionFunctional variantsHigh abundanceBase changesNorthern blottingAbundant formUS variantsRNA
1990
Direct measurement of oligonucleotide substrate binding to wild-type and mutant ribozymes from Tetrahymena.
Pyle AM, McSwiggen JA, Cech TR. Direct measurement of oligonucleotide substrate binding to wild-type and mutant ribozymes from Tetrahymena. Proceedings Of The National Academy Of Sciences Of The United States Of America 1990, 87: 8187-8191. PMID: 2236030, PMCID: PMC54920, DOI: 10.1073/pnas.87.21.8187.Peer-Reviewed Original ResearchConceptsSingle base changeBase-pairing interactionsGuanosine-binding siteRNA substratesSubstrate bindingRNA cleavageOligonucleotide substratesEfficient RNA cleavageTertiary interactionsBase changesRibozyme variantsTetrahymena ribozymeWeak substrateMutant ribozymesRibozymePolyacrylamide gelsEquilibrium dissociation constantsDeoxyribose sugarCatalytic activityDivalent cationsEnergetic stabilizationMutagenesisDissociation constantsTetrahymenaLow Mg2
1985
supN ochre suppressor gene in Escherichia coli codes for tRNALys
Uemura H, Thorbjarnardóttir S, Gamulin V, Yano J, Andrésson O, Söll D, Eggertsson G. supN ochre suppressor gene in Escherichia coli codes for tRNALys. Journal Of Bacteriology 1985, 163: 1288-1289. PMID: 3897192, PMCID: PMC219277, DOI: 10.1128/jb.163.3.1288-1289.1985.Peer-Reviewed Original ResearchLeucine tRNA family of Escherichia coli: nucleotide sequence of the supP(Am) suppressor gene
Thorbjarnardóttir S, Dingermann T, Rafnar T, Andrésson O, Söll D, Eggertsson G. Leucine tRNA family of Escherichia coli: nucleotide sequence of the supP(Am) suppressor gene. Journal Of Bacteriology 1985, 161: 219-222. PMID: 2981802, PMCID: PMC214859, DOI: 10.1128/jb.161.1.219-222.1985.Peer-Reviewed Original ResearchConceptsSuppressor allelesLeuX geneAmber suppressor allelesMature coding sequenceLeucyl-tRNA synthetaseSingle base changeTRNA familiesCAA anticodonBox sequenceTermination signalDNA sequencesNucleotide sequenceBacteriophage T4Coding sequenceAminoacyl stemSuppressor geneLoop regionTRNABase changesEscherichia coliGenesE. coliSequenceColiAlleles
1984
Mutations affecting excision of the intron from a eukaryotic dimeric tRNA precursor.
Willis I, Hottinger H, Pearson D, Chisholm V, Leupold U, Söll D. Mutations affecting excision of the intron from a eukaryotic dimeric tRNA precursor. The EMBO Journal 1984, 3: 1573-1580. PMID: 6430697, PMCID: PMC557561, DOI: 10.1002/j.1460-2075.1984.tb02013.x.Peer-Reviewed Original ResearchConceptsTRNA precursorsDimeric tRNA precursorSerine tRNA geneEfficiency of splicingPrecursor tRNA processingSingle base changeTRNA genesTRNASer geneTRNA processingGene transcriptionNucleotide sequenceUGA mutationsD-loopMutant geneGenesBase changesExtra armMutationsIntronsTranscriptionVivo systemDimeric precursorSequenceTRNASerSplicing
1979
Constructed Mutants of Simian Virus 40
Shortle D, Pipas J, Lazarowitz S, DiMaio D, Nathans D. Constructed Mutants of Simian Virus 40. Genetic Engineering: Principles And Methods 1979, 73-92. DOI: 10.1007/978-1-4615-7072-1_5.Peer-Reviewed Original ResearchGenetic analysisDNA moleculesNucleic acid biochemistryRegulatory elementsSimian virus 40Such mutantsDNA sequencesNucleotide sequenceRandom mutagenesisPhenotype selectionGenomePhysiological defectsSpontaneous mutationsMutantsSpecific base changesViral genomeBase changesRestriction endonucleasesRestriction sitesMutant virusCleavage mapSite specificitySpecific sitesSequenceRecent advances
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