2016
Spider Silk Peptide Is a Compact, Linear Nanospring Ideal for Intracellular Tension Sensing
Brenner MD, Zhou R, Conway DE, Lanzano L, Gratton E, Schwartz MA, Ha T. Spider Silk Peptide Is a Compact, Linear Nanospring Ideal for Intracellular Tension Sensing. Nano Letters 2016, 16: 2096-2102. PMID: 26824190, PMCID: PMC4851340, DOI: 10.1021/acs.nanolett.6b00305.Peer-Reviewed Original ResearchConceptsSingle-molecule fluorescence-force spectroscopyFluorescence-force spectroscopyFluorescence resonance energy transferResonance energy transferRodlike structureSensor constructsShort peptidesIndividual chainsAccessible forcesEnergy transferSilk peptideCell imagingSpider silk proteinsBiological systemsRemarkable elasticitySilk proteinsFRETPN.PeptidesSpider silkPolymersSpectroscopyRecent developmentsForce sensitivityWide range
2011
Light‐Triggered Myosin Activation for Probing Dynamic Cellular Processes
Goguen BN, Hoffman BD, Sellers JR, Schwartz MA, Imperiali B. Light‐Triggered Myosin Activation for Probing Dynamic Cellular Processes. Angewandte Chemie International Edition 2011, 50: 5667-5670. PMID: 21542072, PMCID: PMC3406609, DOI: 10.1002/anie.201100674.Peer-Reviewed Original Research
2007
Induction of Vascular Permeability: βPIX and GIT1 Scaffold the Activation of Extracellular Signal-regulated Kinase by PAK
Stockton R, Reutershan J, Scott D, Sanders J, Ley K, Schwartz MA. Induction of Vascular Permeability: βPIX and GIT1 Scaffold the Activation of Extracellular Signal-regulated Kinase by PAK. Molecular Biology Of The Cell 2007, 18: 2346-2355. PMID: 17429073, PMCID: PMC1877103, DOI: 10.1091/mbc.e06-07-0584.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsCapillary PermeabilityCattleCell Cycle ProteinsCells, CulturedEndothelial CellsEnzyme ActivationExtracellular Signal-Regulated MAP KinasesGuanine Nucleotide Exchange FactorsHumansInflammationLipopolysaccharidesLungMiceP21-Activated KinasesPeptidesProtein Serine-Threonine KinasesRho Guanine Nucleotide Exchange FactorsConceptsP21-activated kinaseMitogen-activated protein kinase kinaseEndothelial cell-cell junctionsExtracellular signal-regulated kinaseCell-cell junctionsProtein kinase kinaseMyosin light chain phosphorylationLight chain phosphorylationSignal-regulated kinaseCell-permeant peptideActivation of ERKKinase kinaseExtracellular signalsPAK functionChain phosphorylationCritical regulatorKinaseCell contractilityCell typesCultured endothelial cellsPhosphorylationMouse lung injury modelMyosin phosphorylationEndothelial cellsGIT1Blocking p21-activated Kinase Reduces Lipopolysaccharide-induced Acute Lung Injury by Preventing Polymorphonuclear Leukocyte Infiltration
Reutershan J, Stockton R, Zarbock A, Sullivan GW, Chang D, Scott D, Schwartz MA, Ley K. Blocking p21-activated Kinase Reduces Lipopolysaccharide-induced Acute Lung Injury by Preventing Polymorphonuclear Leukocyte Infiltration. American Journal Of Respiratory And Critical Care Medicine 2007, 175: 1027-1035. PMID: 17322107, PMCID: PMC1899271, DOI: 10.1164/rccm.200612-1822oc.Peer-Reviewed Original ResearchConceptsAcute lung injuryLung injuryPMN migrationPolymorphonuclear leukocytesAlveolar spaceLipopolysaccharide-induced lung injuryMurine lung injuryPolymorphonuclear leukocyte infiltrationLeukocyte-endothelial interactionsAlveolo-capillary membraneOxidative burstRole of PAKsLeukocyte infiltrationChemokine receptorsLung interstitiumMurine modelExcessive recruitmentPMN chemoattractantInjuryCytoskeletal actin polymerizationAdhesion moleculesCritical mediatorCell migrationAttractive targetPAK phosphorylation
2004
p21-activated Kinase Regulates Endothelial Permeability through Modulation of Contractility*
Stockton RA, Schaefer E, Schwartz MA. p21-activated Kinase Regulates Endothelial Permeability through Modulation of Contractility*. Journal Of Biological Chemistry 2004, 279: 46621-46630. PMID: 15333633, DOI: 10.1074/jbc.m408877200.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsBlotting, WesternCattleCell CommunicationCells, CulturedCytokinesCytoskeletonEndothelium, VascularEnzyme ActivationHumansInflammationIschemiaMicroscopy, FluorescenceMuscle ContractionMyosin Light ChainsP21-Activated KinasesPeptidesPhosphorylationProtein Serine-Threonine KinasesProtein TransportThrombinTime FactorsTransfectionUmbilical VeinsConceptsP21-activated kinaseClose cell-cell associationsEndothelial cell-cell junctionsCell-cell junctionsActin stress fibersCell-cell associationsSuitable drug targetsGrowth factorMyosin phosphorylationHuman umbilical vein endothelial cellsCentral regulatorStress fibersUmbilical vein endothelial cellsEndothelial cellsPAK activationDrug targetsVein endothelial cellsCell contractilityMultiple growth factorsParacellular poresEndothelial permeabilityPhosphorylationPathological processesPathological conditionsPotential role
2002
A Dominant-Negative p65 PAK Peptide Inhibits Angiogenesis
Kiosses WB, Hood J, Yang S, Gerritsen ME, Cheresh DA, Alderson N, Schwartz MA. A Dominant-Negative p65 PAK Peptide Inhibits Angiogenesis. Circulation Research 2002, 90: 697-702. PMID: 11934838, DOI: 10.1161/01.res.0000014227.76102.5d.Peer-Reviewed Original Research
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