2014
Synthesis of Stabilized Alpha-Helical Peptides
Bernal F, Katz SG. Synthesis of Stabilized Alpha-Helical Peptides. Methods In Molecular Biology 2014, 1176: 107-114. PMID: 25030922, PMCID: PMC6333094, DOI: 10.1007/978-1-4939-0992-6_9.Peer-Reviewed Original ResearchConceptsAlpha-helical peptidesImportant protein-protein interactionsSpecific amino acid residuesProtein-protein interactionsAlpha-helical motifOlefin metathesis reactionsAlpha-helical structureRing-closing olefin metathesis reactionAmino acid residuesPosttranslational modificationsProtein interactionsMetathesis reactionHost proteinsProtein targetsAcid residuesCrystal structureSecondary structureFunctional consequencesRemarkable stabilitySmall moleculesMost peptidesInteraction sitesStructural studiesCell permeabilitySynthesis
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
2002
Interaction between FOG-1 and the Corepressor C-Terminal Binding Protein Is Dispensable for Normal Erythropoiesis In Vivo
Katz SG, Cantor AB, Orkin SH. Interaction between FOG-1 and the Corepressor C-Terminal Binding Protein Is Dispensable for Normal Erythropoiesis In Vivo. Molecular And Cellular Biology 2002, 22: 3121-3128. PMID: 11940669, PMCID: PMC133767, DOI: 10.1128/mcb.22.9.3121-3128.2002.Peer-Reviewed Original ResearchMeSH KeywordsAlcohol OxidoreductasesAmino Acid MotifsAmino Acid SequenceAnimalsBinding SitesBlotting, WesternCarrier ProteinsCell LineConserved SequenceCOS CellsDNA-Binding ProteinsErythrocytesErythropoiesisErythropoietinGenetic VectorsHematocritMiceMice, KnockoutMutationNuclear ProteinsPhenylhydrazinesPhosphoproteinsPrecipitin TestsProtein BindingRepressor ProteinsSequence Homology, Amino AcidTranscription FactorsTransgenesConceptsC-terminal binding proteinFOG-1Corepressor C-terminal binding proteinTranscription factor GATA-1Binding proteinCorepressor CtBPCtBP interactsErythroid developmentGATA-1Vivo functionCtBPMegakaryocytic lineagePeptide motifsPhysiological roleInteraction sitesNormal erythropoiesisErythropoietic stressCell linesStages of developmentProteinErythrocyte productionFamily membersWild-type miceErythropoiesisCoimmunoprecipitation