2003
Modulation of DNA damage-induced apoptosis by cell adhesion is independently mediated by p53 and c-Abl
Truong T, Sun G, Doorly M, Wang JY, Schwartz MA. Modulation of DNA damage-induced apoptosis by cell adhesion is independently mediated by p53 and c-Abl. Proceedings Of The National Academy Of Sciences Of The United States Of America 2003, 100: 10281-10286. PMID: 12928501, PMCID: PMC193552, DOI: 10.1073/pnas.1635435100.Peer-Reviewed Original ResearchConceptsC-Abl/p73 pathwayDNA damageIntegrin ligationC-AblDNA damage-induced apoptosisC-Abl tyrosine kinaseCell adhesionExtracellular matrixDamage-induced apoptosisP73 pathwayCertain cell typesP53-negative tumor cellsProapoptotic transcription factorTranscription factorsTyrosine kinaseApoptotic responseDifferential utilizationCell typesDifferent tumor cell linesTumor cell linesTumor cellsP53 levelsCell linesSecond pathwayCell killing
2002
Integrins regulate the apoptotic response to DNA damage through modulation of p53
Lewis JM, Truong TN, Schwartz MA. Integrins regulate the apoptotic response to DNA damage through modulation of p53. Proceedings Of The National Academy Of Sciences Of The United States Of America 2002, 99: 3627-3632. PMID: 11904424, PMCID: PMC122574, DOI: 10.1073/pnas.062698499.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodiesApoptosisCaspase 3CaspasesCell AdhesionCell SurvivalChromosome AberrationsCyclin-Dependent Kinase Inhibitor p16DNA DamageFibroblastsHumansIntegrinsMelanomaMiceMutationNuclear ProteinsOrgan SpecificityProto-Oncogene ProteinsProto-Oncogene Proteins c-mdm2Radiation, IonizingSarcomaTumor Cells, CulturedTumor Suppressor Protein p14ARFTumor Suppressor Protein p53ConceptsTumor cellsTherapy-resistant tumorsModulation of p53Susceptible tumor cellsDNA damageLevels of p53Low p53 levelsApoptosis of cellsTherapy resistanceAntiintegrin antibodiesCancer cellsP53 levelsSurvival of cellsP53Nonadherent cellsCell typesSurvivalApoptotic responseCellsP19 ARFApoptosisChromosomal instabilityFibroblastic cell typesDamageChemotherapy
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