2019
Aberrant splicing contributes to severe α-spectrin-linked congenital hemolytic anemia
Gallagher PG, Maksimova Y, Lezon-Geyda K, Newburger PE, Medeiros D, Hanson RD, Rothman J, Israels S, Wall DA, Sidonio RF, Sieff C, Gowans LK, Mittal N, Rivera-Santiago R, Speicher DW, Baserga SJ, Schulz VP. Aberrant splicing contributes to severe α-spectrin-linked congenital hemolytic anemia. Journal Of Clinical Investigation 2019, 129: 2878-2887. PMID: 31038472, PMCID: PMC6597203, DOI: 10.1172/jci127195.Peer-Reviewed Original ResearchConceptsRecessive hereditary spherocytosisSplice acceptor siteHuman genetic diseasesMRNA stability studiesAberrant splicing contributesSplicing contributesWhole-genome sequencingSplicing analysisHereditary pyropoikilocytosisTermination codonNull allelesGenome sequencingWhole-exome sequencingBranch pointsNumerous mutationsGenetic diseasesLinkage disequilibriumMRNA transcriptsΑ-spectrinMinigene studiesAcceptor sitesMutationsExome sequencingNew targets
2014
Probing large conformational rearrangements in wild-type and mutant spectrin using structural mass spectrometry
Sriswasdi S, Harper SL, Tang HY, Gallagher PG, Speicher DW. Probing large conformational rearrangements in wild-type and mutant spectrin using structural mass spectrometry. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 1801-1806. PMID: 24453214, PMCID: PMC3918770, DOI: 10.1073/pnas.1317620111.Peer-Reviewed Original ResearchConceptsMass spectrometryConformational changesStructural mass spectrometryLarge conformational rearrangementsCell membraneMembrane integrityMass spectrometry characterizationRed cell spectrinUnidentified mechanistic insightCell membrane integrityProtein complexesMacromolecular complexesDiverse functionsCell shapeBiological processesFlexible proteinsConformational rearrangementsDimer-tetramer equilibriumRed cell membraneOpen dimersCell typesΑ-spectrinKey mechanistic roleTetramerization siteBiophysical data
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
1997
Amino‐acid substitution in α‐spectrin commonly coinherited with nondominant hereditary spherocytosis
Tse W, Gallagher P, Jenkins P, Wang Y, Benoit L, Speicher D, Winkelmann J, Agre P, Forget B, Marchesi S. Amino‐acid substitution in α‐spectrin commonly coinherited with nondominant hereditary spherocytosis. American Journal Of Hematology 1997, 54: 233-241. PMID: 9067503, DOI: 10.1002/(sici)1096-8652(199703)54:3<233::aid-ajh10>3.0.co;2-e.Peer-Reviewed Original ResearchConceptsHereditary spherocytosisAlpha-spectrin geneNumber of patientsSevere hemolytic anemiaAmino acid substitutionsHemolytic anemiaPatientsPatterns of transmissionDifferent kindredsPolymorphic variantsAffected individualsErythrocyte spectrinGene defectsGenomic DNA analysisTrue homozygotesDisordersSpherocytosisSpectrin chainsGenomic DNAAlpha-spectrinKindredsLinkage disequilibriumΑ-spectrinAmino acidsDomain peptide