2009
The structure of the ankyrin-binding site of β-spectrin reveals how tandem spectrin-repeats generate unique ligand-binding properties
Stabach PR, Simonović I, Ranieri MA, Aboodi MS, Steitz TA, Simonović M, Morrow JS. The structure of the ankyrin-binding site of β-spectrin reveals how tandem spectrin-repeats generate unique ligand-binding properties. Blood 2009, 113: 5377-5384. PMID: 19168783, PMCID: PMC2689040, DOI: 10.1182/blood-2008-10-184291.Peer-Reviewed Original ResearchAlanineAmino Acid MotifsAmino Acid SequenceAnkyrinsBinding SitesCrystallography, X-RayHumansLigandsMechanotransduction, CellularModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedProtein BindingProtein FoldingProtein Interaction MappingProtein Structure, TertiaryRepetitive Sequences, Amino AcidSequence Homology, Amino AcidSpectrin
2008
Ankyrin facilitates intracellular trafficking of α1-Na+-K+-ATPase in polarized cells
Stabach PR, Devarajan P, Stankewich MC, Bannykh S, Morrow JS. Ankyrin facilitates intracellular trafficking of α1-Na+-K+-ATPase in polarized cells. American Journal Of Physiology - Cell Physiology 2008, 295: c1202-c1214. PMID: 18768923, PMCID: PMC2584975, DOI: 10.1152/ajpcell.00273.2008.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnkyrin RepeatAnkyrinsCell PolarityChlorocebus aethiopsCOS CellsCytoplasmDogsEndoplasmic ReticulumGolgi ApparatusHumansMembrane GlycoproteinsMonomeric GTP-Binding ProteinsProtein ConformationProtein FoldingProtein Sorting SignalsProtein TransportRatsRecombinant Fusion ProteinsRNA InterferenceRNA, Small InterferingSodium-Potassium-Exchanging ATPaseTime FactorsTransfectionViral Envelope ProteinsConceptsEndoplasmic reticulumSecretory pathwayPlasma membraneVesicular stomatitis virus G proteinMadin-Darby canine kidney cellsVirus G proteinSmall hairpin RNACanine kidney cellsGolgi traffickingAnkyrin RGolgi transportSemipermeabilized cellsER retentionCytoplasmic domainMembrane proteinsAssembly pathwayProtein ankyrinIntracellular traffickingAnkyrinFusion proteinSimilar phenotypeG proteinsSuch phenotypesHairpin RNACultured cells
2006
A limited number of genes are involved in the differentiation of germinal center B cells
Nakayama Y, Stabach P, Maher SE, Mahajan MC, Masiar P, Liao C, Zhang X, Ye Z, Tuck D, Bothwell AL, Newburger PE, Weissman SM. A limited number of genes are involved in the differentiation of germinal center B cells. Journal Of Cellular Biochemistry 2006, 99: 1308-1325. PMID: 16795035, DOI: 10.1002/jcb.20952.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsB-LymphocytesCell DifferentiationCell LineChildChild, PreschoolDithiothreitolDNA-Binding ProteinsGene Expression ProfilingGerminal CenterHumansMolecular Sequence DataNuclear ProteinsOligonucleotide Array Sequence AnalysisPalatine TonsilProtein FoldingRegulatory Factor X Transcription FactorsTranscription FactorsTunicamycinX-Box Binding Protein 1ConceptsUnfolded protein responseX-box binding protein 1Interferon regulatory factor 4Protein 1B lymphocyte-induced maturation protein-1Transcription factor B lymphocyte-induced maturation protein-1Post-transcriptional changesBinding protein 1Maturation protein-1Mature B cellsDisulfide isomeraseTranscription factorsLevel of expressionPlasmacytoma cell lineProtein responseGene expressionRegulatory factor 4GenesGerminal center B cellsLymphoblastoid cellsLimited inductionCell linesB cellsFactor 4Germinal center centroblasts