2009
Targeted correction of a thalassemia-associated β-globin mutation induced by pseudo-complementary peptide nucleic acids
Lonkar P, Kim KH, Kuan JY, Chin JY, Rogers FA, Knauert MP, Kole R, Nielsen PE, Glazer PM. Targeted correction of a thalassemia-associated β-globin mutation induced by pseudo-complementary peptide nucleic acids. Nucleic Acids Research 2009, 37: 3635-3644. PMID: 19364810, PMCID: PMC2699504, DOI: 10.1093/nar/gkp217.Peer-Reviewed Original ResearchConceptsBeta-globin geneNucleotide excision repair factorsAltered helical structureExcision repair factorsSingle base-pair modificationTriplex-forming peptide nucleic acidsPseudo-complementary peptide nucleic acidsDisease-related genesDonor DNA fragmentsComplementary DNA sequenceNucleic acidsProper splicingRepair factorsSite-specific bindingMammalian cellsSite-specific modificationDNA repairDNA sequencesGene targetingSecond intronDNA fragmentsHuman cellsTriple helix formationGene correctionHuman fibroblast cells
2008
Correction of a splice-site mutation in the beta-globin gene stimulated by triplex-forming peptide nucleic acids
Chin JY, Kuan JY, Lonkar PS, Krause DS, Seidman MM, Peterson KR, Nielsen PE, Kole R, Glazer PM. Correction of a splice-site mutation in the beta-globin gene stimulated by triplex-forming peptide nucleic acids. Proceedings Of The National Academy Of Sciences Of The United States Of America 2008, 105: 13514-13519. PMID: 18757759, PMCID: PMC2533221, DOI: 10.1073/pnas.0711793105.Peer-Reviewed Original ResearchConceptsBeta-globin geneEndogenous beta-globin locusSplice site mutationHuman cellsPrimary hematopoietic progenitor cellsBeta-globin locusAltered helical structureHuman beta-globin geneSingle base pair changeSingle base-pair modificationTriplex-forming peptide nucleic acidsDonor DNA moleculesBase pair changesCell cycle stageDisease-related genesDonor DNA fragmentsNucleic acidsProper splicingSite-specific bindingSite-specific modificationMammalian cellsHematopoietic progenitor cellsDNA repairSecond intronGene locus
1995
Sequence Motifs in the Replicator Protein of Parvovirus MVM Essential for Nicking and Covalent Attachment to the Viral Origin: Identification of the Linking Tyrosine
Nüesch J, Cotmore S, Tattersall P. Sequence Motifs in the Replicator Protein of Parvovirus MVM Essential for Nicking and Covalent Attachment to the Viral Origin: Identification of the Linking Tyrosine. Virology 1995, 209: 122-135. PMID: 7747462, DOI: 10.1006/viro.1995.1236.Peer-Reviewed Original ResearchConceptsMutant proteinsRolling-circle replicationTyrosine motifOrigin-containing plasmidParvoviral DNA replicationViral originParvovirus minute virusSingle-strand nicksInitiator proteinSequence motifsDNA replicationSite-specific bindingSequence comparisonCyanogen bromide cleavageOrigin sequencesDe novo synthesisSubstrate DNAY210Circle replicationLatter residueStrand nicksHeLa cellsLow salt conditionsCommon motifMetal coordination sites
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