2011
Perinatal Onset Mevalonate Kinase Deficiency
Steiner LA, Ehrenkranz RA, Peterec SM, Steiner RD, Reyes-Múgica M, Gallagher PG. Perinatal Onset Mevalonate Kinase Deficiency. Pediatric And Developmental Pathology 2011, 14: 301-306. PMID: 21425920, DOI: 10.2350/11-02-0985-oa.1.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceFatal OutcomeFemaleHumansMaleMevalonate Kinase DeficiencyMolecular Sequence DataMutation, MissensePedigreePolymerase Chain ReactionPregnancyConceptsMevalonate kinase deficiencyPeriodic fever syndromeNeonatal periodKinase deficiencyFever syndromeDysmorphic featuresCentral nervous system abnormalitiesIntrauterine viral infectionCholestatic liver diseaseIntrauterine growth restrictionImmediate neonatal periodNervous system abnormalitiesSevere multisystem disorderSepsis syndromeRenal failureCerebral ventriculomegalyLiver diseasePersistent diarrheaClinical findingsPoor prognosisAutopsy findingsGrowth restrictionRare conditionExtramedullary erythropoiesisPerinatal period
2005
A dinucleotide deletion in the ankyrin promoter alters gene expression, transcription initiation and TFIID complex formation in hereditary spherocytosis
Gallagher PG, Nilson DG, Wong C, Weisbein JL, Garrett-Beal LJ, Eber SW, Bodine DM. A dinucleotide deletion in the ankyrin promoter alters gene expression, transcription initiation and TFIID complex formation in hereditary spherocytosis. Human Molecular Genetics 2005, 14: 2501-2509. PMID: 16037067, DOI: 10.1093/hmg/ddi254.Peer-Reviewed Original ResearchMeSH KeywordsAnkyrinsBase CompositionDNA PrimersErythrocyte MembraneGene Expression RegulationGenes, ReporterHumansPeptide Chain Initiation, TranslationalPolymerase Chain ReactionPolymorphism, Single-Stranded ConformationalPromoter Regions, GeneticSequence DeletionSpherocytosis, HereditaryTATA BoxTranscription Factor TFIIDTranscription, GeneticConceptsTFIID complex formationTATA-binding proteinTranscription initiation siteGene expressionAnkyrin promoterCis elementsInitiation siteCore promoter DNAMultiple transcription initiation sitesPreinitiation complex formationStart site utilizationComplex formationSite utilizationAlters gene expressionTFIID complexFunctional Sp1Promoter DNATranscription initiationTypes of promotersErythroid promoterMammalian promotersGene transcriptionTG deletionMutant promotersReporter gene
2000
A recurrent frameshift mutation of the ankyrin gene associated with severe hereditary spherocytosis
Gallagher P, Ferreira J, Costa F, Saad S, Forget B. A recurrent frameshift mutation of the ankyrin gene associated with severe hereditary spherocytosis. British Journal Of Haematology 2000, 111: 1190-1193. DOI: 10.1111/j.1365-2141.2000.02441.x.Peer-Reviewed Original ResearchA recurrent frameshift mutation of the ankyrin gene associated with severe hereditary spherocytosis.
Gallagher P, Ferreira J, Costa F, Saad S, Forget B. A recurrent frameshift mutation of the ankyrin gene associated with severe hereditary spherocytosis. British Journal Of Haematology 2000, 111: 1190-3. PMID: 11167760, DOI: 10.1046/j.1365-2141.2000.02441.x.Peer-Reviewed Original Research
1997
Genetic basis of the polymorphisms of the αI domain of spectrin
Gallagher P, Romana M, Wong C, Forget B. Genetic basis of the polymorphisms of the αI domain of spectrin. American Journal Of Hematology 1997, 56: 107-111. PMID: 9326352, DOI: 10.1002/(sici)1096-8652(199710)56:2<107::aid-ajh6>3.0.co;2-2.Peer-Reviewed Original ResearchMeSH KeywordsAllelesAnemia, Hemolytic, CongenitalBase SequenceElliptocytosis, HereditaryHaplotypesHumansMutationPolymerase Chain ReactionPolymorphism, GeneticSpectrinConceptsGenetic basisHereditary elliptocytosisHereditary pyropoikilocytosisDistinct haplotypesGenetic analysisProtein phenotypeAlpha-spectrinChromosomal backgroundΑI domainSpectrinPolymorphismMutationsHaplotypesPhenotypeElliptocytosisPyropoikilocytosisPCRAssaysFamilyGene polymorphismsDomainIdentificationMutation 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
1996
Epidemiological studies of spectrin mutations related to hereditary elliptocytosis and spectrin polymorphisms in Benin
Glele‐Kakai C, Garbarz M, Lecomte M, Leborgne S, Galand C, Bournier O, Devaux I, Gautero H, Zohoun I, Gallagher P, Forget B, Dhermy D. Epidemiological studies of spectrin mutations related to hereditary elliptocytosis and spectrin polymorphisms in Benin. British Journal Of Haematology 1996, 95: 57-66. PMID: 8857939, DOI: 10.1046/j.1365-2141.1996.d01-1869.x.Peer-Reviewed Original ResearchMeSH KeywordsBeninElliptocytosis, HereditaryGenetic TestingHumansMutationPoint MutationPolymerase Chain ReactionPolymorphism, GeneticSpectrinConceptsHereditary elliptocytosisGenetic backgroundAlpha-spectrin geneSeparate genetic backgroundsNumber of polymorphismsErythrocyte alpha-spectrinGenetic basisProtein polymorphismsAfrican populationsAlpha-spectrinSpectrin mutationsMolecular defectsMutationsNovel mutationsPolymorphismEpidemiological studiesHE individualsElliptocytosisTwo-thirdsGenesSpectrinPopulationHigh frequency
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
1994
Location and PCR‐based detection of three polymorphisms of the human erythrocyte β‐spectrin gene (SPTB)
Gallagher P, Lecomte M, Galand C, Wang Y, Tse W, Forget B. Location and PCR‐based detection of three polymorphisms of the human erythrocyte β‐spectrin gene (SPTB). British Journal Of Haematology 1994, 88: 413-414. PMID: 7803294, DOI: 10.1111/j.1365-2141.1994.tb05043.x.Peer-Reviewed Original ResearchMeSH KeywordsAllelesBase SequenceElliptocytosis, HereditaryHumansMolecular Sequence DataPolymerase Chain ReactionPolymorphism, GeneticSpectrinSpherocytosis, HereditarySpectrin St Louis and the αLELV Allele
Gallagher P, Forget B. Spectrin St Louis and the αLELV Allele. Blood 1994, 84: 1686-1687. PMID: 8068958, DOI: 10.1182/blood.v84.5.1686.1686.Peer-Reviewed Original Research
1993
Analysis of a Pst I polymorphism of the human erythrocyte band 3 gene (EPB3)
Jenkins P, Gallagher P, Forget B. Analysis of a Pst I polymorphism of the human erythrocyte band 3 gene (EPB3). British Journal Of Haematology 1993, 85: 816-818. PMID: 7918052, DOI: 10.1111/j.1365-2141.1993.tb03232.x.Peer-Reviewed Original Research
1992
A common type of the spectrin alpha I 46-50a-kD peptide abnormality in hereditary elliptocytosis and pyropoikilocytosis is associated with a mutation distant from the proteolytic cleavage site. Evidence for the functional importance of the triple helical model of spectrin.
Gallagher PG, Tse WT, Coetzer T, Lecomte MC, Garbarz M, Zarkowsky HS, Baruchel A, Ballas SK, Dhermy D, Palek J. A common type of the spectrin alpha I 46-50a-kD peptide abnormality in hereditary elliptocytosis and pyropoikilocytosis is associated with a mutation distant from the proteolytic cleavage site. Evidence for the functional importance of the triple helical model of spectrin. Journal Of Clinical Investigation 1992, 89: 892-898. PMID: 1541680, PMCID: PMC442935, DOI: 10.1172/jci115669.Peer-Reviewed Original ResearchConceptsProteolytic cleavage sitesAlpha-spectrin chainTriple helical modelCleavage siteHelix 2Helix-breaking proline substitutionsHereditary elliptocytosisAlpha iAlpha-spectrin geneAlpha-helical structureAmino-terminal sideHereditary pyropoikilocytosisHelical modelErythrocyte membrane proteinsLimited tryptic digestionMembrane proteinsSpectrin repeatsDNA sequencesSpectrin chainsHelix 3Position 207Leucine residuesFunctional importanceProline substitutionPoint mutationsLarge numbers of alternatively spliced isoforms of the regulatory region of human erythrocyte ankyrin.
Gallagher PG, Tse WT, Scarpa AL, Lux SE, Forget BG. Large numbers of alternatively spliced isoforms of the regulatory region of human erythrocyte ankyrin. Proceedings Of The Association Of American Physicians 1992, 105: 268-77. PMID: 1309004.Peer-Reviewed Original ResearchConceptsHuman erythrocyte ankyrin
1991
Heterogeneity of the molecular basis of hereditary pyropoikilocytosis and hereditary elliptocytosis associated with increased levels of the spectrin alpha I/74-kilodalton tryptic peptide.
Floyd P, Gallagher P, Valentino L, Davis M, Marchesi S, Forget B. Heterogeneity of the molecular basis of hereditary pyropoikilocytosis and hereditary elliptocytosis associated with increased levels of the spectrin alpha I/74-kilodalton tryptic peptide. Blood 1991, 78: 1364-72. PMID: 1878597, DOI: 10.1182/blood.v78.5.1364.bloodjournal7851364.Peer-Reviewed Original ResearchA splice site mutation of the beta-spectrin gene causing exon skipping in hereditary elliptocytosis associated with a truncated beta-spectrin chain
Gallagher PG, Tse WT, Costa F, Scarpa A, Boivin P, Delaunay J, Forget BG. A splice site mutation of the beta-spectrin gene causing exon skipping in hereditary elliptocytosis associated with a truncated beta-spectrin chain. Journal Of Biological Chemistry 1991, 266: 15154-15159. PMID: 1840591, DOI: 10.1016/s0021-9258(18)98598-4.Peer-Reviewed Original ResearchSpectrin Rouen (beta 220-218), a novel shortened beta-chain variant in a kindred with hereditary elliptocytosis. Characterization of the molecular defect as exon skipping due to a splice site mutation.
Garbarz M, Tse WT, Gallagher PG, Picat C, Lecomte MC, Galibert F, Dhermy D, Forget BG. Spectrin Rouen (beta 220-218), a novel shortened beta-chain variant in a kindred with hereditary elliptocytosis. Characterization of the molecular defect as exon skipping due to a splice site mutation. Journal Of Clinical Investigation 1991, 88: 76-81. PMID: 2056132, PMCID: PMC296005, DOI: 10.1172/jci115307.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceDNAElliptocytosis, HereditaryExonsHumansMolecular Sequence DataMutationPolymerase Chain ReactionSpectrinConceptsBeta-spectrin chainBeta-spectrin geneCDNA amplification productsAmino acidsExon YGenomic DNANucleotide sequencingExample of exonMolecular defectsAnalysis of cDNAAmplification productsHereditary elliptocytosisConsensus splice sitesNovel amino acidCarboxy terminusIntron downstreamSplice siteSplice site mutationSouthern blotExonsExon skipReticulocyte RNACDNAPenultimate exonSite mutation