2019
BOK promotes erythropoiesis in a mouse model of myelodysplastic syndrome
Kang SH, Perales O, Michaud M, Katz SG. BOK promotes erythropoiesis in a mouse model of myelodysplastic syndrome. Annals Of Hematology 2019, 98: 2089-2096. PMID: 31203423, PMCID: PMC6702064, DOI: 10.1007/s00277-019-03726-7.Peer-Reviewed Original ResearchConceptsUnfolded protein responseER stressPro-apoptotic membersBcl-2 familyNHD13 miceRT-qPCR analysisInduction of apoptosisProgenitor stem cellsHematopoietic progenitor cell assaysProtein responseDownstream effectorsGene knockoutMyelodysplastic syndromeCell stressProgenitor cell assaysEndoplasmic reticulumLower mean cell hemoglobin concentrationErythroid progenitorsNUP98-HOXD13 transgenic miceClonal hematopoietic stem cell disordersStem cellsSimilar overall survivalAcute myeloid leukemiaHematopoietic stem cell disordersMean cell hemoglobin concentration
2008
Structural Analysis of a BAX-BIM SAHB Complex Reveals a Novel BH3 Interaction Site on BAX for Therapeutic Activation of Apoptosis
Gavathiotis E, Suzuki M, Davis M, Pitter K, Bird G, Katz S, Tu H, Kim H, Cheng E, Tjandra N, Walensky L. Structural Analysis of a BAX-BIM SAHB Complex Reveals a Novel BH3 Interaction Site on BAX for Therapeutic Activation of Apoptosis. Blood 2008, 112: 300. DOI: 10.1182/blood.v112.11.300.300.Peer-Reviewed Original ResearchAnti-apoptotic proteinsBax activationCell deathInteraction sitesAlpha-helixBCL-2 domainsBcl-2 family proteinsBcl-2 familyPathologic cell deathBax-mediated apoptosisFirst structural analysisPro-apoptotic proteinsDomain proteinsFamily proteinsMitochondrial translocationProtein interactionsPoint mutagenesisMitochondrial apoptosisStress stimuliBcl-xLConformational changesCell survivalMitochondrial dysfunctionNovel siteDistinct assaysBAX activation is initiated at a novel interaction site
Gavathiotis E, Suzuki M, Davis ML, Pitter K, Bird GH, Katz SG, Tu HC, Kim H, Cheng E, Tjandra N, Walensky LD. BAX activation is initiated at a novel interaction site. Nature 2008, 455: 1076-1081. PMID: 18948948, PMCID: PMC2597110, DOI: 10.1038/nature07396.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsApoptosisApoptosis Regulatory ProteinsBcl-2-Associated X ProteinBcl-2-Like Protein 11BH3 Interacting Domain Death Agonist ProteinCell LineGene Expression RegulationHumansMembrane ProteinsMiceMutagenesis, Site-DirectedMutationNuclear Magnetic Resonance, BiomolecularProtein BindingProto-Oncogene ProteinsSequence AlignmentConceptsAnti-apoptotic proteinsInteraction sitesBax activationBax-mediated cell deathBCL-2 domainsCell deathBcl-2 familyNovel interaction sitePro-apoptotic proteinsPoint mutagenesisMitochondrial apoptosisBax interactionStress stimuliΑ-helixProteinNew targetsBaxTherapeutic modulationDirect activationActivation siteApoptosisActivationFunctional activitySitesMutagenesis