2018
Addressing the diagnostic gaps in pyruvate kinase deficiency: Consensus recommendations on the diagnosis of pyruvate kinase deficiency
Bianchi P, Fermo E, Glader B, Kanno H, Agarwal A, Barcellini W, Eber S, Hoyer JD, Kuter DJ, Maia TM, del Mar Mañu‐Pereira M, Kalfa TA, Pissard S, Segovia J, van Beers E, Gallagher PG, Rees DC, van Wijk R, with the endorsement of EuroBloodNet T. Addressing the diagnostic gaps in pyruvate kinase deficiency: Consensus recommendations on the diagnosis of pyruvate kinase deficiency. American Journal Of Hematology 2018, 94: 149-161. PMID: 30358897, PMCID: PMC7344868, DOI: 10.1002/ajh.25325.Peer-Reviewed Original ResearchMeSH KeywordsAnemia, Hemolytic, Congenital NonspherocyticArtifactsBlood Cell CountBlood PreservationDNA Mutational AnalysisErythrocytesFalse Negative ReactionsFalse Positive ReactionsHumansPyruvate KinasePyruvate Metabolism, Inborn ErrorsReference ValuesReticulocytesSensitivity and SpecificitySequence Analysis, DNASpectrophotometryTime FactorsConceptsPyruvate kinase deficiency
2013
Fetal hemoglobin in sickle cell anemia: Genetic studies of the Arab-Indian haplotype
Ngo D, Bae H, Steinberg MH, Sebastiani P, Solovieff N, Baldwin CT, Melista E, Safaya S, Farrer LA, Al-Suliman AM, Albuali WH, Al Bagshi M, Naserullah Z, Akinsheye I, Gallagher P, Luo HY, Chui DH, Farrell JJ, Al-Ali AK, Alsultan A. Fetal hemoglobin in sickle cell anemia: Genetic studies of the Arab-Indian haplotype. Blood Cells Molecules And Diseases 2013, 51: 22-26. PMID: 23465615, PMCID: PMC3647015, DOI: 10.1016/j.bcmd.2012.12.005.Peer-Reviewed Original ResearchAdolescentAdultAllelesAnemia, Sickle CellArabsBeta-GlobinsCarrier ProteinsChildChild, PreschoolFetal HemoglobinGenes, mybGTP-Binding ProteinsHaplotypesHemoglobin, SickleHomeodomain ProteinsHSP70 Heat-Shock ProteinsHumansKruppel-Like Transcription FactorsLocus Control RegionMiddle AgedMutationNuclear ProteinsPeptide Elongation FactorsPolymorphism, GeneticPromoter Regions, GeneticRepressor ProteinsSequence Analysis, DNATranscription FactorsYoung AdultIdentification of Biologically Relevant Enhancers in Human Erythroid Cells*
Su MY, Steiner LA, Bogardus H, Mishra T, Schulz VP, Hardison RC, Gallagher PG. Identification of Biologically Relevant Enhancers in Human Erythroid Cells*. Journal Of Biological Chemistry 2013, 288: 8433-8444. PMID: 23341446, PMCID: PMC3605659, DOI: 10.1074/jbc.m112.413260.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceBasic Helix-Loop-Helix Transcription FactorsCells, CulturedChromatinChromatin ImmunoprecipitationConserved SequenceE1A-Associated p300 ProteinEnhancer Elements, GeneticErythroid CellsGATA1 Transcription FactorGene Expression RegulationGenes, ReporterHigh-Throughput Nucleotide SequencingHumansKruppel-Like Transcription FactorsLuciferases, FireflyMolecular Sequence AnnotationNF-E2 Transcription Factor, p45 SubunitOligonucleotide Array Sequence AnalysisPolymorphism, Single NucleotidePromoter Regions, GeneticProtein BindingProto-Oncogene ProteinsRNA, MessengerSequence Analysis, DNAT-Cell Acute Lymphocytic Leukemia Protein 1TranscriptomeConceptsHuman erythroid cellsCandidate enhancersTranscriptional start siteErythroid cellsTranscription factorsGenome-wide association study catalogCell type-specific enhancersPrimary human erythroid cellsRegulation of programsGenome-wide mapsErythroid transcription factorsErythroid cell developmentSpecialized cell typesIdentification of enhancersGene expression analysisErythroid traitsMinimal conservationChromatin immunoprecipitationModerate conservationStart siteRelevant enhancersCellular developmentGenetic lociExpression analysisReporter gene
2011
Genetic diagnosis of neuroacanthocytosis disorders using exome sequencing
Walker RH, Schulz VP, Tikhonova IR, Mahajan MC, Mane S, Muniz M, Gallagher PG. Genetic diagnosis of neuroacanthocytosis disorders using exome sequencing. Movement Disorders 2011, 27: 539-543. PMID: 22038564, DOI: 10.1002/mds.24020.Peer-Reviewed Original ResearchGenome-wide ChIP-Seq reveals a dramatic shift in the binding of the transcription factor erythroid Kruppel-like factor during erythrocyte differentiation
Pilon AM, Ajay SS, Kumar SA, Steiner LA, Cherukuri PF, Wincovitch S, Anderson SM, Mullikin J, Gallagher P, Hardison R, Margulies E, Bodine D. Genome-wide ChIP-Seq reveals a dramatic shift in the binding of the transcription factor erythroid Kruppel-like factor during erythrocyte differentiation. Blood 2011, 118: e139-e148. PMID: 21900194, PMCID: PMC3208289, DOI: 10.1182/blood-2011-05-355107.Peer-Reviewed Original ResearchConceptsErythroid Kruppel-like factorKruppel-like factorChIP-seqTranscription factorsGenome-wide ChIP-seqProgenitor cellsMouse erythroid progenitor cellsCell cycle regulatory pathwaysErythroid transcription factorsGeneral cell growthRNA-seq analysisErythroid progenitor cellsTranscriptional activatorGATA factorsIntragenic regionsErythrocyte differentiationRegulatory pathwaysNuclear distributionPromoter regionParallel sequencingInteractomeDifferentiated erythroblastsCell growthTAL1Little overlap
2004
Mutation of a highly conserved isoleucine disrupts hydrophobic interactions in the αβ spectrin self-association binding site
Gallagher PG, Zhang Z, Morrow JS, Forget BG. Mutation of a highly conserved isoleucine disrupts hydrophobic interactions in the αβ spectrin self-association binding site. Laboratory Investigation 2004, 84: 229-234. PMID: 14661034, DOI: 10.1038/labinvest.3700029.Peer-Reviewed Original ResearchConceptsBinding sitesAlpha-spectrin mutationsEvolutionary conservationSpectrin functionSpectrin repeatsTriple helical modelAlpha-spectrinGenetic studiesHydrophobic isoleucineHydrophobic interactionsLow-expression alleleMolecular modelingExpression alleleSpectrinFunctional defectsTriple helixMutationsHelical modelIsoleucineErythrocyte membranesDrosophilaClinical phenotypeNeonatal hemolytic anemiaRepeatsHelix
2000
Genomic organization and chromosomal localization of the murine 2 P domain potassium channel gene Kcnk8: conservation of gene structure in 2 P domain potassium channels
Bockenhauer D, Nimmakayalu M, Ward D, Goldstein S, Gallagher P. Genomic organization and chromosomal localization of the murine 2 P domain potassium channel gene Kcnk8: conservation of gene structure in 2 P domain potassium channels. Gene 2000, 261: 365-372. PMID: 11167025, DOI: 10.1016/s0378-1119(00)00492-3.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceChromosome MappingDNADNA, ComplementaryElectrophysiologyExonsGenesIn Situ Hybridization, FluorescenceIntronsMiceMolecular Sequence DataOocytesPhylogenyPotassium ChannelsPotassium Channels, Tandem Pore DomainProtein Structure, TertiaryRNA, ComplementarySequence Analysis, DNAXenopus laevisConceptsPotassium channel genesDomain potassium channelsChromosomal localizationGene structureOocyte expression systemCDNA sequenceXenopus laevis oocyte expression systemExpression systemChannel genesPotential transmembrane helicesIntron/exon boundariesSingle EF-hand motifOpen reading framePotassium channelsEF-hand motifsEvolutionary conservationGenomic organizationCellular chaperonesGenomic structureComposite cDNAPotential SH3Transmembrane helicesGenome databaseChromosomal genesReading frame
1997
Mutation of a highly conserved residue of betaI spectrin associated with fatal and near-fatal neonatal hemolytic anemia.
Gallagher PG, Petruzzi MJ, Weed SA, Zhang Z, Marchesi SL, Mohandas N, Morrow JS, Forget BG. Mutation of a highly conserved residue of betaI spectrin associated with fatal and near-fatal neonatal hemolytic anemia. Journal Of Clinical Investigation 1997, 99: 267-277. PMID: 9005995, PMCID: PMC507794, DOI: 10.1172/jci119155.Peer-Reviewed Original ResearchMeSH KeywordsAnemia, Hemolytic, CongenitalArginineBase SequenceConserved SequenceErythrocyte MembraneFemaleHomozygoteHumansHydrops FetalisLaosLeucineMaleMembrane ProteinsModels, MolecularMuscle, SkeletalPedigreePeptide MappingPoint MutationPolymerase Chain ReactionProtein ConformationSequence Analysis, DNASpectrinConceptsImportance of leucineEvolutionary conservationSpectrin functionSpectrin repeatsBeta spectrinBetaI spectrinTriple helical modelGenetic studiesSpectrinMutationsSkeletal muscleMolecular modelingTriple helixNormal functionHelical modelLeucineErythrocyte membranesDrosophilaHydrophobic interactionsNeonatal hemolytic anemiaRepeatsHelixConservationResiduesMembrane
1995
Recurrent fatal hydrops fetalis associated with a nucleotide substitution in the erythrocyte beta-spectrin gene.
Gallagher PG, Weed SA, Tse WT, Benoit L, Morrow JS, Marchesi SL, Mohandas N, Forget BG. Recurrent fatal hydrops fetalis associated with a nucleotide substitution in the erythrocyte beta-spectrin gene. Journal Of Clinical Investigation 1995, 95: 1174-1182. PMID: 7883966, PMCID: PMC441455, DOI: 10.1172/jci117766.Peer-Reviewed Original ResearchConceptsBeta-spectrin geneErythrocyte membrane mechanical stabilityPrincipal structural proteinMembrane mechanical stabilitySpectrin functionBeta spectrinErythrocyte membranesNucleotide substitutionsStudy of erythrocytesStructural proteinsAlpha-spectrinGenetic studiesMolecular defectsPoint mutationsSpectrinHydrops fetalisRecombinant peptideMutationsGenesSevere Coomb's negative hemolytic anemiaThird-trimester fetal loss