2008
Structural and functional effects of hereditary hemolytic anemia-associated point mutations in the alpha spectrin tetramer site
Gaetani M, Mootien S, Harper S, Gallagher PG, Speicher DW. Structural and functional effects of hereditary hemolytic anemia-associated point mutations in the alpha spectrin tetramer site. Blood 2008, 111: 5712-5720. PMID: 18218854, PMCID: PMC2424163, DOI: 10.1182/blood-2007-11-122457.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnemia, Hemolytic, CongenitalBinding SitesCalorimetry, Differential ScanningCircular DichroismEntropyErythrocytesGene ExpressionGenotypeHumansMolecular Sequence DataPhenotypePoint MutationProtein BindingRecombinant ProteinsSpectrinSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationStructure-Activity Relationship
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