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 ResearchMeSH KeywordsBiophysical PhenomenaMass SpectrometryMutant ProteinsProtein MultimerizationProtein Structure, QuaternarySpectrinConceptsMass 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
2010
Mutation of a barrier insulator in the human ankyrin-1 gene is associated with hereditary spherocytosis
Gallagher PG, Steiner LA, Liem RI, Owen AN, Cline AP, Seidel NE, Garrett LJ, Bodine DM. Mutation of a barrier insulator in the human ankyrin-1 gene is associated with hereditary spherocytosis. Journal Of Clinical Investigation 2010, 120: 4453-4465. PMID: 21099109, PMCID: PMC2993586, DOI: 10.1172/jci42240.Peer-Reviewed Original ResearchConceptsAnkyrin-1 geneBarrier insulatorsTransgenic miceUpstream regionErythroid promoterChromatin configurationGene promoterErythroid cellsHereditary spherocytosisPotential pathogenetic mechanismsHuman ankyrin-1 geneHuman erythroid cell lineBarrier-associated proteinsErythroid cell linesPathogenetic mechanismsCommon causeUniform expressionNucleotide substitutionsRegion upstreamPromoter actsHuman diseasesPromoterCell linesPrimary cellsGenes