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