2000
Antibody-Induced Activation of β1 Integrin Receptors Stimulates cAMP-Dependent Migration of Breast Cells on Laminin-5
Plopper G, Huff J, Rust W, Schwartz M, Quaranta V. Antibody-Induced Activation of β1 Integrin Receptors Stimulates cAMP-Dependent Migration of Breast Cells on Laminin-5. Archives Of Biochemistry And Biophysics 2000, 4: 129-135. PMID: 11170844, DOI: 10.1006/mcbr.2001.0267.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine Diphosphate RiboseAntibodies, MonoclonalBreast NeoplasmsCell AdhesionCell Adhesion MoleculesCell MovementCells, CulturedCyclic AMPDNA PrimersFemaleHeterotrimeric GTP-Binding ProteinsHumansIntegrin alpha3beta1IntegrinsPertussis ToxinPrecipitin TestsReceptors, LamininSignal TransductionTumor Cells, CulturedVirulence Factors, Bordetella
1999
Integrin-dependent Tyrosine Phosphorylation and Growth Regulation by Vav
Yron I, Deckert M, Reff M, Munshi A, Schwartz M, Altman A. Integrin-dependent Tyrosine Phosphorylation and Growth Regulation by Vav. Cell Communication & Adhesion 1999, 7: 1-11. PMID: 10228731, DOI: 10.3109/15419069909034388.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsCell AdhesionCell Adhesion MoleculesCell DivisionCHO CellsCricetinaeCytoskeletal ProteinsFibronectinsFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesHumansIntegrin beta1Jurkat CellsKineticsOncogene ProteinsPaxillinPhosphoproteinsPhosphorylationPrecipitin TestsProtein-Tyrosine KinasesProto-Oncogene MasProto-Oncogene Proteins c-vavTime FactorsTransfectionTyrosineConceptsRapid phosphorylationIntegrin-dependent tyrosine phosphorylationAdhesion-dependent mannerExchange factor domainB cell antigen receptorAdhesion-dependent increaseIntegrin signal transductionFocal adhesion kinaseExtent of phosphorylationCell surface stimuliCell antigen receptorJurkat T cellsTriton-insoluble fractionVav overexpressionSmall GTPasesBeta 1 integrinRho familyRho GTPasesCytoskeletal organizationSignal transductionAdhesion kinaseTyrosine phosphorylationStress fibersGrowth regulationFactor domain
1998
Integrins Regulate the Association and Phosphorylation of Paxillin by c-Abl*
Lewis J, Schwartz M. Integrins Regulate the Association and Phosphorylation of Paxillin by c-Abl*. Journal Of Biological Chemistry 1998, 273: 14225-14230. PMID: 9603926, DOI: 10.1074/jbc.273.23.14225.Peer-Reviewed Original ResearchConceptsC-AblCell adhesionTyrosine kinaseFocal adhesion protein paxillinNon-receptor tyrosine kinasePhosphorylation of paxillinC-Abl kinaseEffects of integrinsFocal adhesionsProtein paxillinIntegrin regulationPaxillinTransient recruitmentKinaseIntegrinsCell functionProteinAdhesionPhosphorylationTyrosineRegulationABLRecruitmentActivationLocalization