2025
Engineering a genomically recoded organism with one stop codon
Grome M, Nguyen M, Moonan D, Mohler K, Gurara K, Wang S, Hemez C, Stenton B, Cao Y, Radford F, Kornaj M, Patel J, Prome M, Rogulina S, Sozanski D, Tordoff J, Rinehart J, Isaacs F. Engineering a genomically recoded organism with one stop codon. Nature 2025, 639: 512-521. PMID: 39910296, PMCID: PMC11903333, DOI: 10.1038/s41586-024-08501-x.Peer-Reviewed Original Research
2024
Engineered mRNA–ribosome fusions for facile biosynthesis of selenoproteins
Thaenert A, Sevostyanova A, Chung C, Vargas-Rodriguez O, Melnikov S, Söll D. Engineered mRNA–ribosome fusions for facile biosynthesis of selenoproteins. Proceedings Of The National Academy Of Sciences Of The United States Of America 2024, 121: e2321700121. PMID: 38442159, PMCID: PMC10945757, DOI: 10.1073/pnas.2321700121.Peer-Reviewed Original ResearchMeSH KeywordsCodon, TerminatorEscherichia coliMagnoliopsidaRibosomesRNA, MessengerRNA, Ribosomal, 16SSelenocysteineSelenoproteinsConceptsSelenocysteine insertion sequenceRibosomal RNARibosome engineeringMessenger RNARegulatory RNA elementsMachinery of protein synthesisInsertion of SecSec-containing proteinsSite-specific insertionBiosynthesis of selenoproteinsNatural messenger RNALive bacterial cellsRNA elementsUAG codonInsertion sequenceRibosome structureUGA codonSec codonInsert SecStop codonSynthetic biologyDesigning proteinsRibosomePolypeptide chainBacterial cells
2023
Recoding UAG to selenocysteine in Saccharomyces cerevisiae
Hoffman K, Chung C, Mukai T, Krahn N, Jiang H, Balasuriya N, O'Donoghue P, Söll D. Recoding UAG to selenocysteine in Saccharomyces cerevisiae. RNA 2023, 29: 1400-1410. PMID: 37279998, PMCID: PMC10573291, DOI: 10.1261/rna.079658.123.Peer-Reviewed Original ResearchMeSH KeywordsAeromonas salmonicidaCodon, TerminatorHumansNucleic Acid ConformationProtein EngineeringRNA, Transfer, CysSaccharomyces cerevisiaeConceptsSelenoprotein productionYeast expression systemSeryl-tRNA synthetaseSite-specific incorporationEukaryotic relativesKingdom FungiSelenocysteine synthaseSelenophosphate synthetaseBiosynthesis pathwayEukaryotic selenoproteinsMetabolic engineeringBiosynthetic pathwayPathway componentsExpression systemReductase enzymeTRNASaccharomycesYeastTranslation componentsSpecific sitesFacile productionUnique chemicalSynthetasePathwayFirst demonstrationSplit aminoacyl-tRNA synthetases for proximity-induced stop codon suppression
Jiang H, Ambrose N, Chung C, Wang Y, Söll D, Tharp J. Split aminoacyl-tRNA synthetases for proximity-induced stop codon suppression. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2219758120. PMID: 36787361, PMCID: PMC9974479, DOI: 10.1073/pnas.2219758120.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acyl-tRNA SynthetasesCodon, TerminatorEscherichia coliHumansLigasesProtein BiosynthesisRNA, TransferConceptsAminoacyl-tRNA synthetasesCodon suppressionStop codon suppressionGene expressionOrthogonal aminoacyl-tRNA synthetasesRelevant protein-protein interactionsSynthetic biology toolsSmall molecule rapamycinControl gene expressionProtein-protein interactionsLevel of transcriptionAbscisic acidDimerization domainMammalian cellsBiology toolsGene translationTranslational levelMolecular switchStop codonHuman cellsMolecular inputsUseful biotechnologySynthetasesExpressionTherapeutic applications
2019
Processive Recoding and Metazoan Evolution of Selenoprotein P: Up to 132 UGAs in Molluscs
Baclaocos J, Santesmasses D, Mariotti M, Bierła K, Vetick MB, Lynch S, McAllen R, Mackrill JJ, Loughran G, Guigó R, Szpunar J, Copeland PR, Gladyshev VN, Atkins JF. Processive Recoding and Metazoan Evolution of Selenoprotein P: Up to 132 UGAs in Molluscs. Journal Of Molecular Biology 2019, 431: 4381-4407. PMID: 31442478, PMCID: PMC6885538, DOI: 10.1016/j.jmb.2019.08.007.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiological EvolutionCodon, TerminatorMolluscaProtein BiosynthesisSelenocysteineSelenoprotein PConceptsSELENOP geneEvolution of selenoproteinsPacific oyster Magallana gigasC-terminal domainN-terminal domainOyster Magallana gigasGene evolutionRibosome profilingMammalian counterpartsRibosome progressionMagallana gigasCertain insectsDynamic evolutionary processInitiation codonSECIS elementsGenetic elementsRNA structureCommon spiderEvolutionary processesSelenoprotein expressionSELENOP mRNAUGAAquatic organismsBivalve molluscsSelenocysteine
2018
Ablation of insulin receptor substrates 1 and 2 suppresses Kras-driven lung tumorigenesis
Xu H, Lee M, Tsai P, Adler A, Curry N, Challa S, Freinkman E, Hitchcock D, Copps K, White M, Bronson R, Marcotrigiano M, Wu Y, Clish C, Kalaany N. Ablation of insulin receptor substrates 1 and 2 suppresses Kras-driven lung tumorigenesis. Proceedings Of The National Academy Of Sciences Of The United States Of America 2018, 115: 4228-4233. PMID: 29610318, PMCID: PMC5910837, DOI: 10.1073/pnas.1718414115.Peer-Reviewed Original ResearchMeSH KeywordsA549 CellsAmino AcidsAnimalsAutophagyCarcinogenesisCarcinoma, Non-Small-Cell LungCodon, TerminatorGenes, rasHumansInsulinInsulin Receptor Substrate ProteinsInsulin-Like Growth Factor ILung NeoplasmsMiceNeoplasm ProteinsProteolysisProto-Oncogene Proteins c-aktProto-Oncogene Proteins p21(ras)Signal TransductionConceptsIR/IGF1RLung cancerLung tumorigenesisInsulin receptorTumor cellsInsulin-like growth factor 1 receptorCell lung cancerGrowth factor 1 receptorHuman NSCLC cellsEffective therapeutic strategyLung cancer initiationIntracellular levelsKirsten rat sarcomaFactor 1 receptorTumor burdenCancer deathLeading causeMutant NSCLCNSCLC cellsIGF1R inhibitionMouse modelTherapeutic strategiesInsulin/IGF1Acute lossRat sarcoma
2016
TMEM230 stop codon mutation is rare in parkinson's disease and essential tremor in eastern China
He Y, Huang P, Li Q, Sun Q, Li D, Wang T, Shen J, Chen S. TMEM230 stop codon mutation is rare in parkinson's disease and essential tremor in eastern China. Movement Disorders 2016, 32: 301-302. PMID: 27869322, DOI: 10.1002/mds.26875.Peer-Reviewed Original Research
2015
BRCA2 Polymorphic Stop Codon K3326X and the Risk of Breast, Prostate, and Ovarian Cancers
Meeks HD, Song H, Michailidou K, Bolla MK, Dennis J, Wang Q, Barrowdale D, Frost D, EMBRACE, McGuffog L, Ellis S, Feng B, Buys S, Hopper J, Southey M, Tesoriero A, Investigators K, James P, Bruinsma F, Campbell I, Group A, Broeks A, Schmidt M, Hogervorst F, HEBON, Beckman M, Fasching P, Fletcher O, Johnson N, Sawyer E, Riboli E, Banerjee S, Menon U, Tomlinson I, Burwinkel B, Hamann U, Marme F, Rudolph A, Janavicius R, Tihomirova L, Tung N, Garber J, Cramer D, Terry K, Poole E, Tworoger S, Dorfling C, van Rensburg E, Godwin A, Guénel P, Truong T, Collaborators G, Stoppa-Lyonnet D, Damiola F, Mazoyer S, Sinilnikova O, Isaacs C, Maugard C, Bojesen S, Flyger H, Gerdes A, Hansen T, Jensen A, Kjaer S, Hogdall C, Hogdall E, Pedersen I, Thomassen M, Benitez J, González-Neira A, Osorio A, de la Hoya M, Segura P, Diez O, Lazaro C, Brunet J, Anton-Culver H, Eunjung L, John E, Neuhausen S, Ding Y, Castillo D, Weitzel J, Ganz P, Nussbaum R, Chan S, Karlan B, Lester J, Wu A, Gayther S, Ramus S, Sieh W, Whittermore A, Monteiro A, Phelan C, Terry M, Piedmonte M, Offit K, Robson M, Levine D, Moysich K, Cannioto R, Olson S, Daly M, Nathanson K, Domchek S, Lu K, Liang D, Hildebrant M, Ness R, Modugno F, Pearce L, Goodman M, Thompson P, Brenner H, Butterbach K, Meindl A, Hahnen E, Wappenschmidt B, Brauch H, Brüning T, Blomqvist C, Khan S, Nevanlinna H, Pelttari L, Aittomäki K, Butzow R, Bogdanova N, Dörk T, Lindblom A, Margolin S, Rantala J, Kosma V, Mannermaa A, Lambrechts D, Neven P, Claes K, Van Maerken T, Chang-Claude J, Flesch-Janys D, Heitz F, Varon-Mateeva R, Peterlongo P, Radice P, Viel A, Barile M, Peissel B, Manoukian S, Montagna M, Oliani C, Peixoto A, Teixeira M, Collavoli A, Hallberg E, Olson J, Goode E, Hart S, Shimelis H, Cunningham J, Giles G, Milne R, Healey S, Tucker K, Haiman C, Henderson B, Goldberg M, Tischkowitz M, Simard J, Soucy P, Eccles D, Le N, Borresen-Dale A, Kristensen V, Salvesen H, Bjorge L, Bandera E, Risch H, Zheng W, Beeghly-Fadiel A, Cai H, Pylkäs K, Tollenaar R, van der Ouweland A, Andrulis I, Knight J, OCGN, Narod S, Devilee P, Winqvist R, Figueroa J, Greene M, L. P, Loud J, García-Closas M, Schoemaker M, Czene K, Darabi H, McNeish I, Siddiquil N, Glasspool R, Kwong A, Park S, Teo S, Yoon S, Matsuo K, Hosono S, Woo Y, Gao Y, Foretova L, Singer C, Rappaport-Feurhauser C, Friedman E, Laitman Y, Rennert G, Imyanitov E, Hulick P, Olopade O, Senter L, Olah E, Doherty J, Schildkraut J, Koppert L, Kiemeney L, Massuger L, Cook L, Pejovic T, Li J, Borg A, Öfverholm A, Rossing M, Wentzensen N, Henriksson K, Cox A, Cross S, Pasini B, Shah M, Kabisch M, Torres D, Jakubowska A, Lubinski J, Gronwald J, Agnarsson B, Kupryjanczyk J, Moes-Sosnowska J, Fostira F, Konstantopoulou I, Slager S, Jones M, in the genome P, Antoniou A, Berchuck A, Swerdlow A, Chenevix-Trench G, Dunning A, Pharoah P, Hall P, Easton D, Couch F, Spurdle A, Goldgar D. BRCA2 Polymorphic Stop Codon K3326X and the Risk of Breast, Prostate, and Ovarian Cancers. Journal Of The National Cancer Institute 2015, 108: djv315. PMID: 26586665, PMCID: PMC4907358, DOI: 10.1093/jnci/djv315.Peer-Reviewed Original ResearchConceptsOvarian cancerBreast cancerVariant carriersCancer riskEstrogen receptor-negative breast cancerReceptor-negative breast cancerCancer case patientsInvasive ovarian cancerHormone-related cancersProstate cancer riskConfidence intervalsOvarian cancer riskSignificant inverse associationCox proportional hazardsSerous ovarian cancerRisk of breastBRCA1 mutation carriersPathogenic BRCA2 variantsControl patientsCase patientsInverse associationOdds ratioProstate cancerMutation carriersProportional hazardsA flexible codon in genomically recoded Escherichia coli permits programmable protein phosphorylation
Pirman NL, Barber KW, Aerni HR, Ma NJ, Haimovich AD, Rogulina S, Isaacs FJ, Rinehart J. A flexible codon in genomically recoded Escherichia coli permits programmable protein phosphorylation. Nature Communications 2015, 6: 8130. PMID: 26350500, PMCID: PMC4566969, DOI: 10.1038/ncomms9130.Peer-Reviewed Original ResearchConceptsProtein phosphorylationProtein phosphorylation eventsFull-length proteinNon-phosphorylated formPhosphoserine-containing proteinsPhosphorylation eventsMEK1 kinaseUAG codonKinase activityRecombinant DNADNA templateEscherichia coliE. coliCodonPhosphorylationFunctional informationSerineProteinColiBiochemical investigationsPhosphoproteomeInefficient productionKinasePhosphoserineDNA
2014
Revealing the amino acid composition of proteins within an expanded genetic code
Aerni HR, Shifman MA, Rogulina S, O'Donoghue P, Rinehart J. Revealing the amino acid composition of proteins within an expanded genetic code. Nucleic Acids Research 2014, 43: e8-e8. PMID: 25378305, PMCID: PMC4333366, DOI: 10.1093/nar/gku1087.Peer-Reviewed Original ResearchConceptsNon-standard amino acidsOrthogonal translation systemGenetic codeUAG codonProtein synthesisConventional proteomic analysisRecombinant reporter proteinRelease factor 1Amino acid insertionAmino acid compositionReporter proteinProteomic analysisExtended proteinSurprising diversityUAG readthroughAcid insertionProteomic workflowStop codonNative proteinCodonEscherichia coliAmino acidsMessenger RNAUAGProtein
2013
Genomically Recoded Organisms Expand Biological Functions
Lajoie MJ, Rovner AJ, Goodman DB, Aerni HR, Haimovich AD, Kuznetsov G, Mercer JA, Wang HH, Carr PA, Mosberg JA, Rohland N, Schultz PG, Jacobson JM, Rinehart J, Church GM, Isaacs FJ. Genomically Recoded Organisms Expand Biological Functions. Science 2013, 342: 357-360. PMID: 24136966, PMCID: PMC4924538, DOI: 10.1126/science.1241459.Peer-Reviewed Original ResearchConceptsNew genetic codesRelease factor 1UAG stop codonNonstandard amino acidsEscherichia coli MG1655UAA codonGenetic codeColi MG1655Biological functionsStop codonChemical diversityT7 bacteriophageAmino acidsFactor 1CodonMG1655OrganismsProteinDiversityDeletionBacteriophagesViral resistanceTranslation functionGROVivoUGA is an additional glycine codon in uncultured SR1 bacteria from the human microbiota
Campbell JH, O’Donoghue P, Campbell AG, Schwientek P, Sczyrba A, Woyke T, Söll D, Podar M. UGA is an additional glycine codon in uncultured SR1 bacteria from the human microbiota. Proceedings Of The National Academy Of Sciences Of The United States Of America 2013, 110: 5540-5545. PMID: 23509275, PMCID: PMC3619370, DOI: 10.1073/pnas.1303090110.Peer-Reviewed Original ResearchConceptsFrame TGA codonTGA codonGlycine codonHuman microbiotaSingle-cell genome sequencesSmall subunit rRNA sequencesComparative genomic analysisHorizontal gene transferUnique genetic codeGlycyl-tRNA synthetaseHuman Microbiome Project dataStrain-specific variationMost genesSuch taxaBisphosphate carboxylaseGenome sequenceGenetic codeGenomic analysisStriking diversityRRNA sequencesΒ-galactosidase activityGlycine residueStop codonCodonLacZ gene
2012
Enhanced phosphoserine insertion during Escherichia coli protein synthesis via partial UAG codon reassignment and release factor 1 deletion
Heinemann IU, Rovner AJ, Aerni HR, Rogulina S, Cheng L, Olds W, Fischer JT, Söll D, Isaacs FJ, Rinehart J. Enhanced phosphoserine insertion during Escherichia coli protein synthesis via partial UAG codon reassignment and release factor 1 deletion. FEBS Letters 2012, 586: 3716-3722. PMID: 22982858, PMCID: PMC3473164, DOI: 10.1016/j.febslet.2012.08.031.Peer-Reviewed Original ResearchConceptsUAG codonEscherichia coli protein synthesisRelease factor 1Aminoacyl-tRNA synthetaseCellular fitnessCodon reassignmentEssential genesElongation factorPhosphoserine phosphataseProtein synthesisRF-1Protein yieldTranslation systemFactor 1CodonAccompanying lossGFPUAAGenesSynthetaseDeletionWNK4FitnessPhosphataseExpression
2011
A TLR5 (g.1174C > T) variant that encodes a stop codon (R392X) is associated with bronchopulmonary dysplasia
Sampath V, Garland J, Le M, Patel A, Konduri G, Cohen J, Simpson P, Hines R. A TLR5 (g.1174C > T) variant that encodes a stop codon (R392X) is associated with bronchopulmonary dysplasia. Pediatric Pulmonology 2011, 47: 460-468. PMID: 22058078, DOI: 10.1002/ppul.21568.Peer-Reviewed Original ResearchMeSH KeywordsBronchopulmonary DysplasiaCodon, TerminatorCohort StudiesFemaleGenetic Predisposition to DiseaseGenetic VariationHeterozygoteHumansIncidenceInfant, NewbornInfant, PrematureInfant, Very Low Birth WeightInterleukin-1 Receptor-Associated KinasesMalePilot ProjectsPolymorphism, Single NucleotideProspective StudiesSeverity of Illness IndexToll-Like Receptor 5ConceptsSevere BPDExact testLow birth weight infantsVariant allelesToll-like receptor (TLR) familyBronchopulmonary dysplasia susceptibilityBirth weight infantsPathway single nucleotide polymorphismsTLR pathway genesMulti-center studyFisher's exact testSusceptibility/severityBPD outcomesEpidemiological confoundersBronchopulmonary dysplasiaMultiplexed single-base extension assayPreterm infantsBPD pathogenesisPremature infantsPulmonary homeostasisLower incidencePathogen recognitionBlood samplesClinical informationCurrent evidenceTargeted Disruption of the CCR5 Gene in Human Hematopoietic Stem Cells Stimulated by Peptide Nucleic Acids
Schleifman EB, Bindra R, Leif J, del Campo J, Rogers FA, Uchil P, Kutsch O, Shultz LD, Kumar P, Greiner DL, Glazer PM. Targeted Disruption of the CCR5 Gene in Human Hematopoietic Stem Cells Stimulated by Peptide Nucleic Acids. Cell Chemical Biology 2011, 18: 1189-1198. PMID: 21944757, PMCID: PMC3183429, DOI: 10.1016/j.chembiol.2011.07.010.Peer-Reviewed Original ResearchConceptsHematopoietic stem cellsHIV-1CCR5 geneHIV-1-infected individualsHIV-1 infectionGene modificationHIV-1 entryCCR5-Delta32 mutationImmune system functionStem cellsCCR5 knockoutMonths posttransplantationChemokine receptorsHuman hematopoietic stem cellsTherapeutic strategiesSubsequent engraftmentGenome modificationProtein levelsHuman cellsTargeted disruptionCCR5Peptide nucleic acidInfectionNucleic acidsCellsExpanding the Genetic Code of Escherichia coli with Phosphoserine
Park HS, Hohn MJ, Umehara T, Guo LT, Osborne EM, Benner J, Noren CJ, Rinehart J, Söll D. Expanding the Genetic Code of Escherichia coli with Phosphoserine. Science 2011, 333: 1151-1154. PMID: 21868676, PMCID: PMC5547737, DOI: 10.1126/science.1207203.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acyl-tRNA SynthetasesAnticodonChloramphenicolChloramphenicol O-AcetyltransferaseCodon, TerminatorDrug Resistance, BacterialEscherichia coliGenetic CodeGenetic EngineeringHumansMAP Kinase Kinase 1Peptide Elongation Factor TuPhosphoserineProtein EngineeringProtein Modification, TranslationalRecombinant Fusion ProteinsRNA, BacterialRNA, Transfer, Amino Acid-SpecificRNA, Transfer, Amino AcylRNA, Transfer, CysTransfer RNA AminoacylationConceptsGenetic codeEF-TuMitogen-activated ERKQuality control functionTransfer RNAProtein engineeringEscherichia coli strainsKinase 1Phosphoamino acidsMolecular biologyEscherichia coliO-phosphoserineColi strainsGeneral utilityDisease researchCanonical positionPhosphoproteomePhosphoserineRNABiologyERKProteinSynthetaseColiResiduesPrecise Manipulation of Chromosomes in Vivo Enables Genome-Wide Codon Replacement
Isaacs FJ, Carr PA, Wang HH, Lajoie MJ, Sterling B, Kraal L, Tolonen AC, Gianoulis TA, Goodman DB, Reppas NB, Emig CJ, Bang D, Hwang SJ, Jewett MC, Jacobson JM, Church GM. Precise Manipulation of Chromosomes in Vivo Enables Genome-Wide Codon Replacement. Science 2011, 333: 348-353. PMID: 21764749, PMCID: PMC5472332, DOI: 10.1126/science.1205822.Peer-Reviewed Original ResearchConceptsGenome engineeringSynonymous codon substitutionsGenome engineering technologiesSynthetic lethal effectMegabase scaleCodon replacementsTAA codonCodon substitutionsRecombination frequencyCodon modificationGenetic landscapeEscherichia coliGenomeChromosomesCodonPrecise changesLethal effectsPrecise manipulationEngineering technologyNucleotidesColiPhenotypeTagsModification
2004
Domains, Amino Acid Residues, and New Isoforms of Caenorhabditis elegans Diacylglycerol Kinase 1 (DGK-1) Important for Terminating Diacylglycerol Signaling in Vivo *
Jose AM, Koelle MR. Domains, Amino Acid Residues, and New Isoforms of Caenorhabditis elegans Diacylglycerol Kinase 1 (DGK-1) Important for Terminating Diacylglycerol Signaling in Vivo *. Journal Of Biological Chemistry 2004, 280: 2730-2736. PMID: 15563467, PMCID: PMC2048986, DOI: 10.1074/jbc.m409460200.Peer-Reviewed Original ResearchMeSH KeywordsAllelesAlternative SplicingAmino Acid SequenceAnimalsBase SequenceBinding SitesCaenorhabditis elegansCell LineCodonCodon, TerminatorDiacylglycerol KinaseDiglyceridesExonsHumansInsectaModels, GeneticMolecular Sequence DataMutationPhosphorylationPlasmidsProtein IsoformsProtein Structure, TertiaryRecombinant ProteinsSequence Homology, Amino AcidSignal TransductionConceptsCysteine-rich domainAmino acid residuesDGK-1Pleckstrin homology domainKinase domainDiacylglycerol kinaseAmino acid substitutionsAcid residuesHomology domainATP-binding site mutationsStop codonSecond cysteine-rich domainPhysiological functionsAcid substitutionsThird cysteine-rich domainHuman diacylglycerol kinaseNovel splice formsSubstituted amino acid residuesDiacylglycerol signalingPremature stop codonCaenorhabditis elegansSplice formsStop codon mutantKey residuesNew isoform
2002
Childhood onset mitochondrial myopathy and lactic acidosis caused by a stop mutation in the mitochondrial cytochrome c oxidase III gene
Horváth R, Scharfe C, Hoeltzenbein M, Do BH, Schröder C, Warzok R, Vogelgesang S, Lochmüller H, Müller-Höcker J, Gerbitz KD, Oefner PJ, Jaksch M. Childhood onset mitochondrial myopathy and lactic acidosis caused by a stop mutation in the mitochondrial cytochrome c oxidase III gene. Journal Of Medical Genetics 2002, 39: 812. PMID: 12414820, PMCID: PMC1735018, DOI: 10.1136/jmg.39.11.812.Peer-Reviewed Original Researchp53 Mutations as Tumor Markers in Fine Needle Aspirates of Palpable Breast Masses
Dillon DA, Hipolito E, Zheng K, Rimm DL, Costa JC. p53 Mutations as Tumor Markers in Fine Needle Aspirates of Palpable Breast Masses. Acta Cytologica 2002, 46: 841-847. PMID: 12365217, DOI: 10.1159/000327057.Peer-Reviewed Original ResearchMeSH KeywordsAbscessAdenocarcinomaAdultAgedAged, 80 and overAmino Acid SubstitutionBiomarkers, TumorBiopsy, NeedleBreast NeoplasmsCarcinoma, Ductal, BreastCodon, TerminatorCystsDNA Mutational AnalysisDNA, NeoplasmExonsFemaleFrameshift MutationGenes, p53GenotypeHumansMiddle AgedMutationPolymorphism, Single-Stranded ConformationalRetrospective StudiesConceptsFine needle aspiratesP53 exons 5Breast massesPolymerase chain reactionNeedle aspiratesP53 mutationsSingle-strand conformational polymorphism analysisSubsequent excisional biopsyPalpable breast massesPotential diagnostic utilityDefinitive cytologic diagnosisTumor cell markersExon 5Molecular diagnostic markersExcisional biopsyBenign cytologyBreast carcinomaSuspicious cytologyRetrospective analysisCytologic diagnosisTumor markersDiagnostic criteriaBiopsy tissueMorphologic diagnosisDiagnostic utility
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