2017
Hereditary xerocytosis: Diagnostic considerations
Risinger M, Glogowska E, Chonat S, Zhang K, Dagaonkar N, Joiner CH, Quinn CT, Kalfa TA, Gallagher PG. Hereditary xerocytosis: Diagnostic considerations. American Journal Of Hematology 2017, 93: e67-e69. PMID: 29210095, PMCID: PMC5807085, DOI: 10.1002/ajh.24996.Peer-Reviewed Original Research
2015
CASE 5—2016Complex Congenital Cardiac Surgery in an Adult Patient With Hereditary Spherocytosis: Avoidance of Massive Hemolysis Associated With Extracorporeal Circulation in the Presence of Red Blood Cell Fragility
Hargrave JM, Capdeville MJ, Duncan AE, Smith MM, Mauermann WJ, Gallagher PG. CASE 5—2016Complex Congenital Cardiac Surgery in an Adult Patient With Hereditary Spherocytosis: Avoidance of Massive Hemolysis Associated With Extracorporeal Circulation in the Presence of Red Blood Cell Fragility. Journal Of Cardiothoracic And Vascular Anesthesia 2015, 30: 800-808. PMID: 27021177, DOI: 10.1053/j.jvca.2015.11.016.Peer-Reviewed Original ResearchMeSH KeywordsAdultCardiac Surgical ProceduresCardiopulmonary BypassErythrocyte DeformabilityErythrocytesExtracorporeal CirculationFemaleHemolysisHumansSpherocytosis, Hereditary
2007
An 11-amino acid β-hairpin loop in the cytoplasmic domain of band 3 is responsible for ankyrin binding in mouse erythrocytes
Stefanovic M, Markham NO, Parry EM, Garrett-Beal LJ, Cline AP, Gallagher PG, Low PS, Bodine DM. An 11-amino acid β-hairpin loop in the cytoplasmic domain of band 3 is responsible for ankyrin binding in mouse erythrocytes. Proceedings Of The National Academy Of Sciences Of The United States Of America 2007, 104: 13972-13977. PMID: 17715300, PMCID: PMC1950715, DOI: 10.1073/pnas.0706266104.Peer-Reviewed Original ResearchConceptsCytoplasmic domainBeta-hairpin loopSpectrin-actinPlasma membraneBand 3Transmembrane protein band 3Β-hairpin loopProtein band 3Uncharacterized interactionMembrane proteinsProtein ankyrinCytoskeletal networkMembrane cytoskeletonCytoskeletal systemAnkyrinCurrent structural modelsErythrocyte membranesSLC4A1 geneLoop deletionComplete deficiencyDeletionMembraneMouse erythrocytesStructural supportDomain
1999
Stomatocytosis is absent in "stomatin"-deficient murine red blood cells.
Zhu Y, Paszty C, Turetsky T, Tsai S, Kuypers F, Lee G, Cooper P, Gallagher P, Stevens M, Rubin E, Mohandas N, Mentzer W. Stomatocytosis is absent in "stomatin"-deficient murine red blood cells. Blood 1999, 93: 2404-10. PMID: 10090952, DOI: 10.1182/blood.v93.7.2404.407k13_2404_2410.Peer-Reviewed Original ResearchMeSH KeywordsAnemia, Hemolytic, CongenitalAnimalsBlood ProteinsCarrier ProteinsCationsErythrocyte DeformabilityErythrocyte IndicesErythrocyte MembraneErythrocytes, AbnormalFemaleGenotypeHumansIon TransportMaleMembrane FluidityMembrane ProteinsMiceMice, Inbred C57BLMice, KnockoutPhenotypePhosphatidylserinesPhospholipid Transfer ProteinsPotassiumSodium
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