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
1992
A common type of the spectrin alpha I 46-50a-kD peptide abnormality in hereditary elliptocytosis and pyropoikilocytosis is associated with a mutation distant from the proteolytic cleavage site. Evidence for the functional importance of the triple helical model of spectrin.
Gallagher PG, Tse WT, Coetzer T, Lecomte MC, Garbarz M, Zarkowsky HS, Baruchel A, Ballas SK, Dhermy D, Palek J. A common type of the spectrin alpha I 46-50a-kD peptide abnormality in hereditary elliptocytosis and pyropoikilocytosis is associated with a mutation distant from the proteolytic cleavage site. Evidence for the functional importance of the triple helical model of spectrin. Journal Of Clinical Investigation 1992, 89: 892-898. PMID: 1541680, PMCID: PMC442935, DOI: 10.1172/jci115669.Peer-Reviewed Original ResearchConceptsProteolytic cleavage sitesAlpha-spectrin chainTriple helical modelCleavage siteHelix 2Helix-breaking proline substitutionsHereditary elliptocytosisAlpha iAlpha-spectrin geneAlpha-helical structureAmino-terminal sideHereditary pyropoikilocytosisHelical modelErythrocyte membrane proteinsLimited tryptic digestionMembrane proteinsSpectrin repeatsDNA sequencesSpectrin chainsHelix 3Position 207Leucine residuesFunctional importanceProline substitutionPoint mutations