2001
Dynamic molecular modeling of pathogenic mutations in the spectrin self-association domain
Zhang Z, Weed S, Gallagher P, Morrow J. Dynamic molecular modeling of pathogenic mutations in the spectrin self-association domain. Blood 2001, 98: 1645-1653. PMID: 11535493, DOI: 10.1182/blood.v98.6.1645.Peer-Reviewed Original ResearchConceptsSelf-association domainPoint mutationsHuman sequenceDrosophila alpha-spectrinDynamic molecular modelingHuman erythrocyte spectrinCytoskeletal functionSpecific point mutationsConservative substitutionsPrimary sequenceConformational rearrangementsAlpha-spectrinHelical regionHydrophilic residuesAmino acidsMutationsSpectrinSalt bridgeErythrocyte spectrinStructural consequencesPathogenic mutationsRepeat unitsMolecular modelingSequenceStructural disruption
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