2014
HOXA10 Regulates Expression of Cytokeratin 15 in Endometrial Epithelial Cytoskeletal Remodeling
Kallen AN, Haines K, Taylor HS. HOXA10 Regulates Expression of Cytokeratin 15 in Endometrial Epithelial Cytoskeletal Remodeling. Reproductive Sciences 2014, 21: 892-897. PMID: 24532216, PMCID: PMC4107567, DOI: 10.1177/1933719113519168.Peer-Reviewed Original ResearchDynamic intracellular networkExpression levelsProtein expressionCell linesMammalian cytoskeletonEndometrial epithelial cell lineCytoskeletal remodelingEpithelial cell lineIntracellular networksGene expressionCytoskeletal changesQuantitative real-time polymerase chain reactionRegulate expressionHuman endometrial epithelial cell lineMessenger RNACytokeratin 15Cellular architectureKeratin filamentsEpithelial remodelingExpression decreasesTotal RNAHuman endometrial epithelial cellsHuman endometriumReal-time polymerase chain reactionEpithelial cellsThe PAR complex controls the spatiotemporal dynamics of F-actin and the MTOC in directionally migrating leukocytes
Crespo CL, Vernieri C, Keller PJ, Garrè M, Bender JR, Wittbrodt J, Pardi R. The PAR complex controls the spatiotemporal dynamics of F-actin and the MTOC in directionally migrating leukocytes. Journal Of Cell Science 2014, 127: 4381-4395. PMID: 25179599, PMCID: PMC4197085, DOI: 10.1242/jcs.146217.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActinsAdaptor Proteins, Signal TransducingAnimalsAnimals, Genetically ModifiedCarrier ProteinsCell MovementCell PolarityCells, CulturedLeukocytesMicrotubule-Organizing CenterMultiprotein ComplexesMutationOryziasProtein Kinase CProtein Transportrho-Associated KinasesZebrafishZebrafish ProteinsConceptsAtypical protein kinase CMicrotubule organizing centerPAR-6Par complexPAR-3Protein kinase CRegulated interactionFish larvaeMyeloid cellsGenetic manipulationPolarizing cuesKinase activationCytoskeletal changesF-actinKinase COrganizing centerFunctional polarizationRho kinase activationThree-dimensional environmentTraction forceCellsSpatiotemporal dynamicsLeukocyte migrationMigrationComplexes
2009
Regulation of cell migration and morphogenesis by Abl-family kinases: emerging mechanisms and physiological contexts
Bradley WD, Koleske AJ. Regulation of cell migration and morphogenesis by Abl-family kinases: emerging mechanisms and physiological contexts. Journal Of Cell Science 2009, 122: 3441-3454. PMID: 19759284, PMCID: PMC2746129, DOI: 10.1242/jcs.039859.Peer-Reviewed Original ResearchConceptsAbl family kinasesNon-receptor tyrosine kinaseWAVE family proteinsCell-specific proteinsActivation of cortactinExtracellular cuesEpithelial morphogenesisAdhesion dynamicsCytoskeletal rearrangementsEssential regulatorPhysiological contextCell motilityActin polymerizationCytoskeletal changesPhysiological processesTyrosine kinaseGenetic studiesKinaseMorphogenesisCell contractilityCell migrationProteinComplex processImmune systemCytoskeleton
2000
Modulation of Host Signaling by a Bacterial Mimic Structure of the Salmonella Effector SptP Bound to Rac1
Stebbins C, Galán J. Modulation of Host Signaling by a Bacterial Mimic Structure of the Salmonella Effector SptP Bound to Rac1. Molecular Cell 2000, 6: 1449-1460. PMID: 11163217, DOI: 10.1016/s1097-2765(00)00141-6.Peer-Reviewed Original ResearchMeSH KeywordsAluminum CompoundsAmino Acid SequenceAmino Acid SubstitutionBacterial ProteinsBinding Sitescdc42 GTP-Binding ProteinCrystallography, X-RayDimerizationEvolution, MolecularFluoridesGTPase-Activating ProteinsGuanosine DiphosphateMacromolecular SubstancesModels, MolecularMolecular Sequence DataMutationProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryProtein Tyrosine Phosphatasesrac1 GTP-Binding ProteinRecombinant Fusion ProteinsSalmonella typhimuriumSequence AlignmentSignal TransductionEvidence for a Functional Association between Phosphatidylinositol 3-Kinase and c-src in the Spreading Response of Osteoclasts to Colony-Stimulating Factor-1*
Grey A, Chen Y, Paliwal I, Carlberg K, Insogna K. Evidence for a Functional Association between Phosphatidylinositol 3-Kinase and c-src in the Spreading Response of Osteoclasts to Colony-Stimulating Factor-1*. Endocrinology 2000, 141: 2129-2138. DOI: 10.1210/en.141.6.2129.Peer-Reviewed Original ResearchC-SrcPhosphatidylinositol 3-kinasePI3K activityColony-stimulating factor-1SH3 domainPI3KSH3 domain of c-SrcRegulatory subunit of PI3KActivation of phosphatidylinositol 3-kinaseSubunit of PI3KProline-rich sequenceActivation of PI3KIntracellular signaling moleculesRegulatory subunitOsteoclast cytoskeletonCytoskeletal changesColony-stimulating factor 1 treatmentOsteoclast motilitySignaling moleculesFunctional associationGrowth factor/cytokineSignaling pathwayInhibitor wortmanninTreatment of osteoclast-like cellsReceptor c-fms
1999
A Salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion
Fu Y, Galán J. A Salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion. Nature 1999, 401: 293-297. PMID: 10499590, DOI: 10.1038/45829.Peer-Reviewed Original ResearchMeSH KeywordsActinsArginineBacterial AdhesionBacterial Proteinscdc42 GTP-Binding Protein, Saccharomyces cerevisiaeCell Cycle ProteinsCell MembraneEscherichia coliGTPase-Activating ProteinsGTP-Binding ProteinsHumansJNK Mitogen-Activated Protein KinasesMAP Kinase Kinase 4Mitogen-Activated Protein Kinase KinasesMutationProtein KinasesProtein Tyrosine PhosphatasesProteinsRecombinant Fusion ProteinsSalmonella typhimuriumConceptsHost cell cytosolActin cytoskeletonType III secretion systemProtein secretion systemSpecialized protein secretion systemActin cytoskeleton reorganizationCell actin cytoskeletonActin cytoskeletal changesRho GTPase proteinsRac-1Bacterial effectorsEffector proteinsExchange factorGTPase proteinsSecretion systemSalmonella proteinsCytoskeletal changesCellular responsesCdc42ProteinInfected cellsBacterial invasionCytosolBacteriumSPTP
1997
Gene Regulation by Mechanical Forces
Oluwole BO, Du W, Mills I, Sumpio BE. Gene Regulation by Mechanical Forces. Endothelium 1997, 5: 85-93. PMID: 9237042, DOI: 10.3109/10623329709079866.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCattleCell Adhesion MoleculesCell Culture TechniquesCells, CulturedEndothelinsEndothelium, VascularEpoprostenolFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesGene Expression RegulationHemorheologyHumansMechanoreceptorsMembranes, ArtificialNitric OxideProtein-Tyrosine KinasesSignal TransductionStress, MechanicalTissue Plasminogen ActivatorTranscription FactorsTranscription, GeneticVacuumConceptsEndothelial cellsEndothelial cell functionCyclic strainVasoactive mediatorsSecond messenger cascadesNitric oxideBlood vesselsMechanical forcesCell functionMechanical deformationFlow of bloodMessenger cascadesLuminal surfaceSpecific response elementsPromoter geneResponse elementExternal forcesMediatorsCytoskeletal changesCellsForceProstacyclinExpressionTranscription levels
1996
Signal Transduction at the Neuronal Growth Cone
Strittmatter S. Signal Transduction at the Neuronal Growth Cone. The Neuroscientist 1996, 2: 83-86. DOI: 10.1177/107385849600200208.Peer-Reviewed Original ResearchSignal transductionG-protein-mediated transductionG proteinsHeterotrimeric G proteinsCell adhesion molecule familyGrowth conesNervous system developmentAdhesion molecule familyGrowth cone membraneNeuronal growth conesLigand-receptor interactionsGrowth cone motilityCadherin familyIntracellular proteinsCytoskeletal changesExtracellular moleculesMolecular understandingIntegrin familyTransductionMolecules inhibitoryDiffusible messengerMolecule familyCone motilityIntracellular eventsCone membrane
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