2006
High-resolution quantitative imaging of mammalian and bacterial cells using stable isotope mass spectrometry
Lechene C, Hillion F, McMahon G, Benson D, Kleinfeld A, Kampf J, Distel D, Luyten Y, Bonventre J, Hentschel D, Park K, Ito S, Schwartz M, Benichou G, Slodzian G. High-resolution quantitative imaging of mammalian and bacterial cells using stable isotope mass spectrometry. BMC Biology 2006, 5: 20. PMID: 17010211, PMCID: PMC1781526, DOI: 10.1186/jbiol42.Peer-Reviewed Original ResearchConceptsMulti-isotope imaging mass spectrometryMammalian cultured cellsFatty acid transportAdipocyte lipid dropletsHigh-resolution quantitative imagingSubcellular compartmentsNitrogen fixationMass spectrometryImaging mass spectrometryLevel of enrichmentBacterial cellsProtein renewalCultured endothelial cellsCultured cellsLipid dropletsKidney cellsStable isotopesUridine incorporationEndothelial cellsCellsQuantitative image analysis softwareStable isotope mass spectrometryIsotopic labelsIsotope ratiosRNA
2004
Rho signalling at a glance
Schwartz M. Rho signalling at a glance. Journal Of Cell Science 2004, 117: 5457-5458. PMID: 15509861, DOI: 10.1242/jcs.01582.Peer-Reviewed Original ResearchAnimalsCdc42 GTP-Binding ProteinFeedback, PhysiologicalHumansIntracellular Signaling Peptides and ProteinsProtein Serine-Threonine KinasesProtein TransportProteinsRac GTP-Binding ProteinsReceptors, Cell SurfaceRho GTP-Binding ProteinsRho-Associated KinasesSignal TransductionWiskott-Aldrich Syndrome Protein
2003
Cell Migration: Integrating Signals from Front to Back
Ridley AJ, Schwartz MA, Burridge K, Firtel RA, Ginsberg MH, Borisy G, Parsons JT, Horwitz AR. Cell Migration: Integrating Signals from Front to Back. Science 2003, 302: 1704-1709. PMID: 14657486, DOI: 10.1126/science.1092053.Peer-Reviewed Original ResearchRho-ROCK-LIMK-Cofilin Pathway Regulates Shear Stress Activation of Sterol Regulatory Element Binding Proteins
Lin T, Zeng L, Liu Y, DeFea K, Schwartz MA, Chien S, Shyy J. Rho-ROCK-LIMK-Cofilin Pathway Regulates Shear Stress Activation of Sterol Regulatory Element Binding Proteins. Circulation Research 2003, 92: 1296-1304. PMID: 12775580, DOI: 10.1161/01.res.0000078780.65824.8b.Peer-Reviewed Original ResearchMeSH KeywordsActin Depolymerizing FactorsActinsAnimalsCattleCCAAT-Enhancer-Binding ProteinsCell AdhesionCells, CulturedCHO CellsCricetinaeDNA-Binding ProteinsEndothelium, VascularHumansIntracellular Signaling Peptides and ProteinsLim KinasesLuciferasesMembrane ProteinsMicrofilament ProteinsMicroscopy, FluorescenceMutationPlasmidsProtein KinasesProtein Serine-Threonine KinasesProtein TransportProteinsRho GTP-Binding ProteinsRho-Associated KinasesSignal TransductionSterol Regulatory Element Binding Protein 1Sterol Regulatory Element Binding Protein 2Stress, MechanicalTranscription FactorsTransfectionConceptsSterol regulatory element-binding proteinLIMK-cofilin pathwayRegulatory element-binding proteinLIM kinaseElement-binding proteinRho-ROCKBinding proteinFluid shear stressSREBP cleavage-activating proteinSignal transduction pathwaysSmall GTPase RhoStress activationShear stress activationGolgi transportS2P proteasesTransduction pathwaysNegative mutantGTPase RhoSREBP activationIntegrin activationEndoplasmic reticulumEndothelial cell functionVascular endothelial cellsCaspase-3Protein
2002
Effects of cell tension on the small GTPase Rac
Katsumi A, Milanini J, Kiosses WB, del Pozo MA, Kaunas R, Chien S, Hahn KM, Schwartz MA. Effects of cell tension on the small GTPase Rac. Journal Of Cell Biology 2002, 158: 153-164. PMID: 12105187, PMCID: PMC2173027, DOI: 10.1083/jcb.200201105.Peer-Reviewed Original ResearchMeSH KeywordsAmidesAnimalsAzepinesCell LineCell MembraneCell MovementCollagenDose-Response Relationship, DrugEnergy TransferGTP PhosphohydrolasesGuanine Nucleotide Exchange FactorsMicroscopy, FluorescenceMicroscopy, Phase-ContrastMicroscopy, VideoNaphthalenesNeoplasm ProteinsProteinsPseudopodiaPyridinesRac GTP-Binding ProteinsRatsStress, MechanicalTime FactorsT-Lymphoma Invasion and Metastasis-inducing Protein 1Transfection
2001
Integrin-mediated mechanotransduction requires its dynamic interaction with specific extracellular matrix (ECM) ligands
Jalali S, del Pozo M, Chen K, Miao H, Li Y, Schwartz M, Shyy J, Chien S. Integrin-mediated mechanotransduction requires its dynamic interaction with specific extracellular matrix (ECM) ligands. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 1042-1046. PMID: 11158591, PMCID: PMC14705, DOI: 10.1073/pnas.98.3.1042.Peer-Reviewed Original ResearchAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAntigens, CDCells, CulturedCollagenEndothelium, VascularExtracellular MatrixExtracellular Matrix ProteinsFibrinogenFibronectinsHumansIntegrin beta1Integrin beta3IntegrinsJNK Mitogen-Activated Protein KinasesLamininLigandsMitogen-Activated Protein KinasesPlatelet Membrane GlycoproteinsProteinsReceptors, VitronectinShc Signaling Adaptor ProteinsSignal TransductionSrc Homology 2 Domain-Containing, Transforming Protein 1Stress, MechanicalUmbilical VeinsVitronectin
2000
The c-Abl tyrosine kinase contributes to the transient activation of MAP kinase in cells plated on fibronectin
Renshaw M, Lewis J, Schwartz M. The c-Abl tyrosine kinase contributes to the transient activation of MAP kinase in cells plated on fibronectin. Oncogene 2000, 19: 3216-3219. PMID: 10918577, DOI: 10.1038/sj.onc.1203667.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAdaptor Proteins, Signal TransducingAnimalsCell Culture TechniquesEnzyme ActivationFibronectinsFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesGRB2 Adaptor ProteinMAP Kinase Signaling SystemMiceMitogen-Activated Protein Kinase 1Mitogen-Activated Protein KinasesProteinsProtein-Tyrosine KinasesProto-Oncogene Proteins c-abl
1997
Affinity Modulation of Platelet Integrin αIIbβ3 by β3-Endonexin, a Selective Binding Partner of the β3 Integrin Cytoplasmic Tail
Kashiwagi H, Schwartz M, Eigenthaler M, Davis K, Ginsberg M, Shattil S. Affinity Modulation of Platelet Integrin αIIbβ3 by β3-Endonexin, a Selective Binding Partner of the β3 Integrin Cytoplasmic Tail. Journal Of Cell Biology 1997, 137: 1433-1443. PMID: 9182673, PMCID: PMC2132534, DOI: 10.1083/jcb.137.6.1433.Peer-Reviewed Original ResearchConceptsGreen fluorescent proteinIntegrin cytoplasmic tailsCytoplasmic tailSuch protein-protein interactionsSelective binding partnerΒ3 integrin cytoplasmic tailProtein-protein interactionsAffinity modulationFibrinogen-dependent aggregationPlatelet integrin αIIbβ3Β3-endonexinBinding partnerEnergy-dependent fashionAcid proteinH-RasIntegrin alphaIIbbeta3Adhesive functionMetabolic regulationFluorescent proteinBeta3 tailIntegrin αIIbβ3Cell lysatesCHO cellsAffinity stateSurface expression
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 ResearchConceptsCross-linking reagentInteraction of proteinsChemical cross-linking reagentsBinding of gelatinCovalent derivativesChemical behaviorSecond moleculeNeighboring macromoleculesN-succinimidyl propionateReagentsHigh yieldsBiological systemsNitro-4DerivativesBiological conditionsPhotolysisMacromoleculesMoleculesInteractionGelatinSituSurfaceYield