1999
Mutational Analysis of Cell Cycle Inhibition by Integrin β1C *
Meredith J, Kiosses W, Takada Y, Schwartz M. Mutational Analysis of Cell Cycle Inhibition by Integrin β1C *. Journal Of Biological Chemistry 1999, 274: 8111-8116. PMID: 10075712, DOI: 10.1074/jbc.274.12.8111.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAmino Acid SequenceAnimalsCells, CulturedDNA Mutational AnalysisDNA ReplicationDose-Response Relationship, DrugHumansIntegrin beta1MiceMice, Inbred C3HMolecular Sequence DataMutagenesis, Site-DirectedReceptors, Interleukin-2Recombinant Fusion ProteinsStructure-Activity RelationshipConceptsCytoplasmic domainGreen fluorescent protein fusion proteinFluorescent protein fusion proteinProtein fusion proteinMembrane-proximal regionCell cycle progressionAnalysis of deletionsHuman interleukin-2 receptorBeta5 cytoplasmic domainsMembrane targetingMouse 10T1/2 cellsGrowth inhibitionCell cycle inhibitionTransmembrane domainLow expression levelsProstate epithelial cellsAcid domainCytoplasmic variantsTac subunitMutational analysisCycle progressionFusion proteinIntact receptorCell line DU145Human endothelial cell line
1994
Differing structural requirements for GTPase-activating protein responsiveness and NADPH oxidase activation by Rac.
Xu X, Barry D, Settleman J, Schwartz M, Bokoch G. Differing structural requirements for GTPase-activating protein responsiveness and NADPH oxidase activation by Rac. Journal Of Biological Chemistry 1994, 269: 23569-23574. PMID: 8089125, DOI: 10.1016/s0021-9258(17)31553-3.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceBinding, CompetitiveDNA PrimersEnzyme ActivationGTPase-Activating ProteinsGTP-Binding ProteinsIn Vitro TechniquesMolecular Sequence DataNADH, NADPH OxidoreductasesNADPH OxidasesProteinsRac GTP-Binding ProteinsRas GTPase-Activating ProteinsRecombinant ProteinsStructure-Activity RelationshipConceptsGTPase-activating proteinsEffector domainFunction of RacGTP/GDP stateInteraction of RasDouble mutationNADPH oxidase activationGAP bindingActin cytoskeletonMembrane rufflingActin assemblyOxidase activationGTP hydrolysisRac-GTPGDP stateWild typeSuperoxide-forming NADPH oxidaseInteraction sitesProtein responsivenessProteinResidues 12MutationsRacRac2Phagocytic leukocytes
1982
A new radioactive cross-linking reagent for studying the interactions of proteins.
Schwartz M, Das O, Hynes R. A new radioactive cross-linking reagent for studying the interactions of proteins. Journal Of Biological Chemistry 1982, 257: 2343-2349. PMID: 7061425, DOI: 10.1016/s0021-9258(18)34928-7.Peer-Reviewed Original ResearchMeSH KeywordsAzidesCross-Linking ReagentsFibronectinsGelatinIndicators and ReagentsMethodsPhotolysisProteinsSepharoseStructure-Activity RelationshipSuccinimidesConceptsCross-linking reagentInteraction of proteinsChemical cross-linking reagentsBinding of gelatinCovalent derivativesChemical behaviorSecond moleculeNeighboring macromoleculesN-succinimidyl propionateReagentsHigh yieldsBiological systemsNitro-4DerivativesBiological conditionsPhotolysisMacromoleculesMoleculesInteractionGelatinSituSurfaceYield
1978
Surface areas of lipid membranes.
Schwartz M, McConnell H. Surface areas of lipid membranes. Biochemistry 1978, 17: 837-40. PMID: 629935, DOI: 10.1021/bi00598a014.Peer-Reviewed Original ResearchMeSH KeywordsCholesterolCobaltCyanidesFree RadicalsHaptensLiposomesMembrane LipidsPhosphatidylcholinesPhotochemistrySpin LabelsStructure-Activity Relationship