2010
A Comprehensive Model of the Spectrin Divalent Tetramer Binding Region Deduced Using Homology Modeling and Chemical Cross-linking of a Mini-spectrin [S] *
Li D, Harper SL, Tang HY, Maksimova Y, Gallagher PG, Speicher DW. A Comprehensive Model of the Spectrin Divalent Tetramer Binding Region Deduced Using Homology Modeling and Chemical Cross-linking of a Mini-spectrin [S] *. Journal Of Biological Chemistry 2010, 285: 29535-29545. PMID: 20610390, PMCID: PMC2937985, DOI: 10.1074/jbc.m110.145573.Peer-Reviewed Original ResearchConceptsHelix faceRed cell membrane stabilityHomology modelingNon-homologous tailsCell membrane stabilityC-terminal tailWild-type bindingMedium-resolution structureSubtle conformational changesTetramer complexSpectrin tetramer formationChemical Cross-LinkingMembrane skeletonRecombinant domainsTetramer formation
2008
Ankyrin‐linked hereditary spherocytosis in an African–American kindred
Sangerman J, Maksimova Y, Edelman EJ, Morrow JS, Forget BG, Gallagher PG. Ankyrin‐linked hereditary spherocytosis in an African–American kindred. American Journal Of Hematology 2008, 83: 789-794. PMID: 18704959, DOI: 10.1002/ajh.21254.Peer-Reviewed Original ResearchConceptsInitiator methionineNull allelesErythrocyte membrane protein genesMembrane protein geneRabbit reticulocyte lysateTissue-specific promotersErythrocyte membrane skeletonExon 1 sequencesIsoform diversityAlternative splicingTranslation initiationProtein geneAnkyrin geneMembrane skeletonAlternate polyadenylationPlasma membraneReticulocyte lysateMethionine mutationCOOH terminusErythroid cellsDownstream codonsGenomic DNANumerous isoformsAnkyrinGenes
2007
Identification and Characterization of α-Spectrin Mutations Associated with Inherited Hemolytic Anemia.
Tolpinrud W, Gaetani M, Maksimova Y, Mootien S, Harper S, Forget B, Speicher D, Gallagher P. Identification and Characterization of α-Spectrin Mutations Associated with Inherited Hemolytic Anemia. Blood 2007, 110: 1706. DOI: 10.1182/blood.v110.11.1706.1706.Peer-Reviewed Original ResearchWild typeMissense mutationsSelf-association siteMembrane skeletonΑ-spectrinHereditary elliptocytosisProline substitutionSpectrin peptidesHereditary pyropoikilocytosisCommon protein polymorphismHPLC gel filtrationHuman disease pathogenesisCharacterization of variantsErythrocyte membrane skeletonMajor structural componentTriple-helical configurationMembrane biologyDifferent missense mutationsSpectrin gene
2005
A novel splicing mutation of the α-spectrin gene in the original hereditary pyropoikilocytosis kindred
Costa DB, Lozovatsky L, Gallagher PG, Forget BG. A novel splicing mutation of the α-spectrin gene in the original hereditary pyropoikilocytosis kindred. Blood 2005, 106: 4367-4369. PMID: 16150946, PMCID: PMC1895230, DOI: 10.1182/blood-2005-05-1813.Peer-Reviewed Original ResearchConceptsFrame premature termination codonsRed blood cell membrane skeletonCell membrane skeletonΑ-spectrin geneHereditary pyropoikilocytosisPremature termination codonConsensus splice sitesTissue culture cellsNovel splicing mutationMembrane skeletonIntronic fragmentTermination codonGene transcriptsAlpha-spectrinAbnormal splicingSplice siteStructural variantsGene transferMolecular defectsSplicing mutationCulture cellsAllelesExon 22TranscriptsMutations
2003
Variegated Expression from the Murine Band 3 (AE1) Promoter in Transgenic Mice Is Associated with mRNA Transcript Initiation at Upstream Start Sites and Can Be Suppressed by the Addition of the Chicken β-Globin 5′ HS4 Insulator Element
Frazar TF, Weisbein JL, Anderson SM, Cline AP, Garrett LJ, Felsenfeld G, Gallagher PG, Bodine DM. Variegated Expression from the Murine Band 3 (AE1) Promoter in Transgenic Mice Is Associated with mRNA Transcript Initiation at Upstream Start Sites and Can Be Suppressed by the Addition of the Chicken β-Globin 5′ HS4 Insulator Element. Molecular And Cellular Biology 2003, 23: 4753-4763. PMID: 12832463, PMCID: PMC162203, DOI: 10.1128/mcb.23.14.4753-4763.2003.Peer-Reviewed Original ResearchConceptsStart siteGamma-globin mRNAUpstream start siteVariegated expressionInsulator elementsHuman gamma-globin geneGamma-globin proteinPosition-effect variegationGamma-globin geneErythroid-specific expressionHS4 insulator elementsBeta-globin clusterHigh steady-state levelsTransgenic mouse assaysErythrocyte membrane skeletonTransgenic miceTransgene copy numberTranscript initiationCytoplasmic domainTransmembrane proteinSteady-state levelsRNA transcriptionMembrane skeletonGene promoterBeta spectrin
1996
Molecular basis and haplotyping of the alphaII domain polymorphisms of spectrin: application to the study of hereditary elliptocytosis and pyropoikilocytosis.
Gallagher PG, Kotula L, Wang Y, Marchesi SL, Curtis PJ, Speicher DW, Forget BG. Molecular basis and haplotyping of the alphaII domain polymorphisms of spectrin: application to the study of hereditary elliptocytosis and pyropoikilocytosis. American Journal Of Human Genetics 1996, 59: 351-9. PMID: 8755921, PMCID: PMC1914747.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnemia, Hemolytic, CongenitalAsianAsian PeopleBase SequenceBiological EvolutionBlack PeopleElliptocytosis, HereditaryErythrocytes, AbnormalHaplotypesHumansModels, GeneticMolecular Sequence DataMutagenesis, InsertionalPolymorphism, GeneticPrevalenceRepetitive Sequences, Nucleic AcidSpectrinUnited StatesWhite PeopleConceptsAlpha-spectrin geneAmino acid sequenceAcid sequenceHereditary elliptocytosisAlpha-spectrin chainHereditary pyropoikilocytosisPrincipal structural proteinErythrocyte membrane skeletonSingle nucleotide substitutionEvolutionary originLimited tryptic digestionMembrane skeletonMolecular basisGenomic DNANucleotide substitutionsStructural proteinsAlpha-spectrinDifferent haplotypesFounder effectGenesLinkage disequilibriumOnly haplotypeSpectrin proteinsCommon haplotypeTryptic digestion