2017
Molecular basis of tactile specialization in the duck bill
Schneider ER, Anderson EO, Mastrotto M, Matson JD, Schulz VP, Gallagher PG, LaMotte RH, Gracheva EO, Bagriantsev SN. Molecular basis of tactile specialization in the duck bill. Proceedings Of The National Academy Of Sciences Of The United States Of America 2017, 114: 13036-13041. PMID: 29109250, PMCID: PMC5724259, DOI: 10.1073/pnas.1708793114.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAvian ProteinsBeakChickensCloning, MolecularDucksEmbryo, NonmammalianGene ExpressionGenetic VectorsHEK293 CellsHumansIon ChannelsKineticsMechanoreceptorsMechanotransduction, CellularMicePatch-Clamp TechniquesRecombinant ProteinsRNA, Small InterferingSequence Homology, Amino AcidSpecies SpecificityTouchTouch PerceptionTrigeminal GanglionConceptsMolecular basisHeterologous expression systemSpecialist birdsMouse orthologPiezo2 ion channelsTactile specializationExpression systemDuck billMolecular characterizationIon channelsFeeding behaviorEdible matterPiezo2BirdsElectrophysiological characterizationSlow inactivation kineticsOrthologsVertebratesMechanoMechanotransductionKnockdownInactivation kineticsMurky watersHigh densityNeurons
2013
The common hereditary elliptocytosis-associated α-spectrin L260P mutation perturbs erythrocyte membranes by stabilizing spectrin in the closed dimer conformation
Harper SL, Sriswasdi S, Tang HY, Gaetani M, Gallagher PG, Speicher DW. The common hereditary elliptocytosis-associated α-spectrin L260P mutation perturbs erythrocyte membranes by stabilizing spectrin in the closed dimer conformation. Blood 2013, 122: 3045-3053. PMID: 23974198, PMCID: PMC3811177, DOI: 10.1182/blood-2013-02-487702.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesCross-Linking ReagentsElliptocytosis, HereditaryErythrocyte MembraneHumansModels, MolecularMolecular Sequence DataMutationProtein BindingProtein MultimerizationProtein StabilityProtein Structure, SecondaryProtein Structure, TertiaryRecombinant ProteinsSpectrinConceptsHereditary elliptocytosisMembrane destabilizationLarge conformational rearrangementsGel filtration analysisMembrane proteinsTetramer assemblyHereditary pyropoikilocytosisBiophysical analysisCommon hereditary elliptocytosisConformational rearrangementsDimer conformationHelical contentTetramerization siteFiltration analysisSpectrin tetramersNovel mechanismUnknown mechanismMutationsBinding assaysSpectrinChemical crosslinkingErythrocyte shapeTetramerErythrocyte membranesMembrane
2008
Structural and functional effects of hereditary hemolytic anemia-associated point mutations in the alpha spectrin tetramer site
Gaetani M, Mootien S, Harper S, Gallagher PG, Speicher DW. Structural and functional effects of hereditary hemolytic anemia-associated point mutations in the alpha spectrin tetramer site. Blood 2008, 111: 5712-5720. PMID: 18218854, PMCID: PMC2424163, DOI: 10.1182/blood-2007-11-122457.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnemia, Hemolytic, CongenitalBinding SitesCalorimetry, Differential ScanningCircular DichroismEntropyErythrocytesGene ExpressionGenotypeHumansMolecular Sequence DataPhenotypePoint MutationProtein BindingRecombinant ProteinsSpectrinSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationStructure-Activity Relationship
2007
An 11-amino acid β-hairpin loop in the cytoplasmic domain of band 3 is responsible for ankyrin binding in mouse erythrocytes
Stefanovic M, Markham NO, Parry EM, Garrett-Beal LJ, Cline AP, Gallagher PG, Low PS, Bodine DM. An 11-amino acid β-hairpin loop in the cytoplasmic domain of band 3 is responsible for ankyrin binding in mouse erythrocytes. Proceedings Of The National Academy Of Sciences Of The United States Of America 2007, 104: 13972-13977. PMID: 17715300, PMCID: PMC1950715, DOI: 10.1073/pnas.0706266104.Peer-Reviewed Original ResearchConceptsCytoplasmic domainBeta-hairpin loopSpectrin-actinPlasma membraneBand 3Transmembrane protein band 3Β-hairpin loopProtein band 3Uncharacterized interactionMembrane proteinsProtein ankyrinCytoskeletal networkMembrane cytoskeletonCytoskeletal systemAnkyrinCurrent structural modelsErythrocyte membranesSLC4A1 geneLoop deletionComplete deficiencyDeletionMembraneMouse erythrocytesStructural supportDomain
2005
GATA-1 and Oct-1 Are Required for Expression of the Human α-Hemoglobin-stabilizing Protein Gene*
Gallagher PG, Liem RI, Wong E, Weiss MJ, Bodine DM. GATA-1 and Oct-1 Are Required for Expression of the Human α-Hemoglobin-stabilizing Protein Gene*. Journal Of Biological Chemistry 2005, 280: 39016-39023. PMID: 16186125, DOI: 10.1074/jbc.m506062200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceBinding SitesBlood ProteinsCell LineCloning, MolecularDNA, ComplementaryErythropoiesisGATA1 Transcription FactorGene ExpressionGlobinsHeLa CellsHumansMiceMice, TransgenicMolecular ChaperonesMolecular Sequence DataMutationOctamer Transcription Factor-1Promoter Regions, GeneticRecombinant ProteinsRNA, MessengerConceptsAlpha-hemoglobin-stabilizing proteinGATA-1AHSP promoterAHSP genePromoter/reporter plasmidsGel mobility shift assaysAHSP gene expressionChromatin immunoprecipitation assaysErythroid-specific expressionMobility shift assaysFurther genetic studiesHuman tissue culture cell linesErythroid proteinTissue culture cell linesErythroid promoterNonerythroid tissuesProtein geneImmunoprecipitation assaysRegulatory elementsShift assaysGene promoterReporter geneCandidate genesDNase IGene expression
1998
An Alternate Promoter Directs Expression of a Truncated, Muscle-specific Isoform of the Human Ankyrin 1 Gene*
Gallagher P, Forget B. An Alternate Promoter Directs Expression of a Truncated, Muscle-specific Isoform of the Human Ankyrin 1 Gene*. Journal Of Biological Chemistry 1998, 273: 1339-1348. PMID: 9430667, DOI: 10.1074/jbc.273.3.1339.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAmino Acid SequenceAnkyrinsBase SequenceCloning, MolecularDNA, ComplementaryErythroid Precursor CellsExonsGene Expression RegulationHumansMolecular Sequence DataMuscle, SkeletalMusclesMyocardiumMyoD ProteinPromoter Regions, GeneticRecombinant ProteinsTranscriptional ActivationConceptsKilobase pairsMuscle cDNADeduced amino acid sequenceCorresponding chromosomal geneHydrophobic NH2 terminusCultured C2C12 muscle cellsHuman ankyrin-1 geneSkeletal muscle cDNADNA-protein interactionsE-box consensusAmino acid sequenceK562 cellsMuscle-specific isoformPromoter directs expressionC2C12 muscle cellsAnkyrin-1 geneReporter gene plasmidHigh-level expressionNorthern blot analysisErythroid genesErythrocyte membrane proteinsSingle Sp1Erythroid promoterAlternative splicingRich promoter
1996
The lethal hemolytic mutation in beta I sigma 2 spectrin Providence yields a null phenotype in neonatal skeletal muscle.
Weed SA, Stabach PR, Oyer CE, Gallagher PG, Morrow JS. The lethal hemolytic mutation in beta I sigma 2 spectrin Providence yields a null phenotype in neonatal skeletal muscle. Laboratory Investigation 1996, 74: 1117-29. PMID: 8667615.Peer-Reviewed Original ResearchConceptsBeta ISpectrin skeletonSkeletal muscleMost such mutationsGene transferAdult mouse skeletal muscleDominant-negative fashionErythroid lineage cellsNeonatal skeletal muscleCultured muscle cellsAlpha beta heterodimersErythrocyte shape abnormalitiesMuscle cellsMouse skeletal muscleDefective proteinSpectrin geneAlternative transcriptsHemolytic phenotypeCDNA constructsNull phenotypeC2C12 myoblastsBeta heterodimerSpectrin mutationsSedimentation velocity analysisIntracellular distribution
1993
Erythropoietin Therapy for Anemia of Prematurity
Gallagher P, Ehrenkranz R. Erythropoietin Therapy for Anemia of Prematurity. Clinics In Perinatology 1993, 20: 169-191. PMID: 8458164, DOI: 10.1016/s0095-5108(18)30418-4.Peer-Reviewed Original ResearchMeSH KeywordsAdultAnemiaErythropoiesisErythropoietinFetusHumansInfant, NewbornInfant, Premature, DiseasesRecombinant ProteinsConceptsAnemia of prematurityRecombinant human erythropoietin administrationBiology of erythropoietinTreatment of anemiaRecombinant human erythropoietinErythropoietin therapyErythropoietin administrationClinical trialsNeonatal erythropoiesisPrematurityHuman erythropoietinValuable adjunctAnemiaTherapyErythropoietinTreatmentPathophysiologyAdjunctAdministrationTrials