2017
Hemoglobin C trait accentuates erythrocyte dehydration in hereditary xerocytosis
Yang E, Voelkel EB, Lezon‐Geyda K, Schulz VP, Gallagher PG. Hemoglobin C trait accentuates erythrocyte dehydration in hereditary xerocytosis. Pediatric Blood & Cancer 2017, 64 PMID: 28121068, PMCID: PMC5858911, DOI: 10.1002/pbc.26444.Peer-Reviewed Original ResearchConceptsMean corpuscular hemoglobin concentrationElevated mean corpuscular hemoglobin concentrationHemoglobin C traitErythrocyte dehydrationC traitHereditary xerocytosisCorpuscular hemoglobin concentrationAcute hemolysisHbC traitHemoglobin concentrationEvidence of dehydrationOsmotic gradient ektacytometryPatientsPIEZO1 mutationsEktacytometryGenetic studies
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
1997
Structure and Organization of the Human Ankyrin-1 Gene BASIS FOR COMPLEXITY OF PRE-mRNA PROCESSING*
Gallagher P, Tse W, Scarpa A, Lux S, Forget B. Structure and Organization of the Human Ankyrin-1 Gene BASIS FOR COMPLEXITY OF PRE-mRNA PROCESSING*. Journal Of Biological Chemistry 1997, 272: 19220-19228. PMID: 9235914, DOI: 10.1074/jbc.272.31.19220.Peer-Reviewed Original ResearchConceptsGenomic structureANK-1 geneSpectrin-binding domainMembrane-binding domainIntron/exon boundariesAlternative polyadenylation signalsPre-mRNA processingBrain-specific transcriptFurther genetic studiesErythrocyte membrane proteinsErythroid transcriptsCommon hemolytic anemiaGene basisAlternative splicingRegulatory domainProtein domainsChromosomal genesMembrane proteinsKilobase pairsPolyadenylation signalMembrane skeletonPlasma membraneExon boundariesGenetic studiesAnkyrin 1Mutation 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
Structure, Organization, and Expression of the Human Band 7.2b Gene, a Candidate Gene for Hereditary Hydrocytosis (∗)
Gallagher P, Forget B. Structure, Organization, and Expression of the Human Band 7.2b Gene, a Candidate Gene for Hereditary Hydrocytosis (∗). Journal Of Biological Chemistry 1995, 270: 26358-26363. PMID: 7592848, DOI: 10.1074/jbc.270.44.26358.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAmino Acid SequenceAnemia, HemolyticAnimalsBase SequenceBlood ProteinsBlotting, NorthernCell LineConsensus SequenceDNA PrimersDNA, ComplementaryExonsGene ExpressionGenetic VariationHominidaeHumansIntronsLeukemia, Erythroblastic, AcuteMembrane ProteinsMiceMolecular Sequence DataPolymerase Chain ReactionPolymorphism, GeneticPromoter Regions, GeneticRecombinant Fusion ProteinsRegulatory Sequences, Nucleic AcidRestriction MappingRNA, MessengerTransfectionTumor Cells, CulturedConceptsSingle transcription initiation siteSimple sequence repeat polymorphismKilobases of DNATranscription initiation siteAlternative polyadenylation signalsFurther genetic studiesHigh-level expressionNorthern blot analysisPattern of expressionWide tissue distributionGenomic structureRich promoterNonerythroid cellsChromosomal genesPolyadenylation signalMembrane skeletonGene cDNAGene promoterReporter geneCandidate genesRecognition sequenceGenetic studiesInitiation siteGenesBase pairsRecurrent 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