2013
The common hereditary elliptocytosis-associated α-spectrin L260P mutation perturbs erythrocyte membranes by stabilizing spectrin in the closed dimer conformation
Harper SL, Sriswasdi S, Tang HY, Gaetani M, Gallagher PG, Speicher DW. The common hereditary elliptocytosis-associated α-spectrin L260P mutation perturbs erythrocyte membranes by stabilizing spectrin in the closed dimer conformation. Blood 2013, 122: 3045-3053. PMID: 23974198, PMCID: PMC3811177, DOI: 10.1182/blood-2013-02-487702.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesCross-Linking ReagentsElliptocytosis, HereditaryErythrocyte MembraneHumansModels, MolecularMolecular Sequence DataMutationProtein BindingProtein MultimerizationProtein StabilityProtein Structure, SecondaryProtein Structure, TertiaryRecombinant ProteinsSpectrinConceptsHereditary elliptocytosisMembrane destabilizationLarge conformational rearrangementsGel filtration analysisMembrane proteinsTetramer assemblyHereditary pyropoikilocytosisBiophysical analysisCommon hereditary elliptocytosisConformational rearrangementsDimer conformationHelical contentTetramerization siteFiltration analysisSpectrin tetramersNovel mechanismUnknown mechanismMutationsBinding assaysSpectrinChemical crosslinkingErythrocyte shapeTetramerErythrocyte membranesMembrane
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 disruptionSpectrin Oligomerization is Cooperatively Coupled to Membrane Assembly: A Linkage Targeted by Many Hereditary Hemolytic Anemias?
Giorgi M, Cianci C, Gallagher P, Morrow J. Spectrin Oligomerization is Cooperatively Coupled to Membrane Assembly: A Linkage Targeted by Many Hereditary Hemolytic Anemias? Experimental And Molecular Pathology 2001, 70: 215-230. PMID: 11418000, DOI: 10.1006/exmp.2001.2377.Peer-Reviewed Original Research