2020
Differences in self-association between kindlin-2 and kindlin-3 are associated with differential integrin binding
Kadry YA, Maisuria EM, Huet-Calderwood C, Calderwood DA. Differences in self-association between kindlin-2 and kindlin-3 are associated with differential integrin binding. Journal Of Biological Chemistry 2020, 295: 11161-11173. PMID: 32546480, PMCID: PMC7415974, DOI: 10.1074/jbc.ra120.013618.Peer-Reviewed Original ResearchConceptsKindlin-3Kindlin-2Focal adhesionsIntegrin cytoplasmic domainTransmembrane adhesion receptorsComparative sequence analysisLive-cell imagingAbility of cellsCytoplasmic domainF3 subdomainsMammalian cellsCytoplasmic componentsExtracellular environmentAdhesion receptorsKindlinSequence analysisIntegrin familySelf-associationIntegrin bindingPhysiological importanceMolecular levelPoint mutationsProteinCellsAdhesion
2014
CS-31A NOVEL YAP-DRIVEN MIGRATION AND INVASION SIGNALING PATHWAY PREDICTS POOR OUTCOME IN GLIOBLASTOMA
Shah S, Tippens N, Park J, Mohyeldin A, Vela G, Levchenko A, Quinones-Hinojosa A. CS-31A NOVEL YAP-DRIVEN MIGRATION AND INVASION SIGNALING PATHWAY PREDICTS POOR OUTCOME IN GLIOBLASTOMA. Neuro-Oncology 2014, 16: v57-v58. PMCID: PMC4217989, DOI: 10.1093/neuonc/nou242.31.Peer-Reviewed Original ResearchCell migration pathwaysMechanism of YAPYAP-dependent mechanismsAbility of cellsDependent signaling mechanismRole of YAPFunction of YAPSmall Rho GTPaseExtracellular cuesTranscriptional regulatorsRho GTPaseSingle-cell mannerMolecular networksIntracellular signalingSignaling mechanismCell mannerCell polarizationCell migrationIndividual cellsCritical modulatorAggressive cancerYAPInvasive behaviorPoor patient prognosisYAP expressionInfluence of pH on Extracellular Matrix Preservation During Lung Decellularization
Tsuchiya T, Balestrini JL, Mendez J, Calle EA, Zhao L, Niklason LE. Influence of pH on Extracellular Matrix Preservation During Lung Decellularization. Tissue Engineering Part C Methods 2014, 20: 1028-1036. PMID: 24735501, PMCID: PMC4241865, DOI: 10.1089/ten.tec.2013.0492.Peer-Reviewed Original Research
2013
Promoter Sequence Determines the Relationship between Expression Level and Noise
Carey LB, van Dijk D, Sloot PM, Kaandorp JA, Segal E. Promoter Sequence Determines the Relationship between Expression Level and Noise. PLOS Biology 2013, 11: e1001528. PMID: 23565060, PMCID: PMC3614515, DOI: 10.1371/journal.pbio.1001528.Peer-Reviewed Original ResearchMeSH KeywordsAlcohol DehydrogenaseBacterial ProteinsBase SequenceBinding SitesCation Transport ProteinsEnzyme InductionGene ExpressionGene Expression Regulation, FungalGene LibraryGenes, ReporterKineticsLuminescent ProteinsModels, GeneticPromoter Regions, GeneticProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsConceptsTranscriptional burstsUnique transcriptional statesTranscription factor activitySingle target geneExpression levelsMechanism of repressionAbility of cellsTF activityGene expression levelsExtracellular cuesTranscriptional statesTranscriptional regulationPromoter DNAPromoter sequencesSingle TFCell variabilityTarget genesRegulatory mechanismsExpression changesZap1Diverse mechanismsNative targetsFactor activityExpression increasesGenes
2012
Filamin A controls matrix metalloproteinase activity and regulates cell invasion in human fibrosarcoma cells
Baldassarre M, Razinia Z, Brahme NN, Buccione R, Calderwood DA. Filamin A controls matrix metalloproteinase activity and regulates cell invasion in human fibrosarcoma cells. Journal Of Cell Science 2012, 125: 3858-3869. PMID: 22595522, PMCID: PMC3462082, DOI: 10.1242/jcs.104018.Peer-Reviewed Original ResearchMeSH KeywordsActinsCell AdhesionCell Line, TumorCell MovementContractile ProteinsEnzyme ActivationExtracellular MatrixFibrosarcomaFilaminsGene Knockdown TechniquesHumansIntegrinsMatrix Metalloproteinase 14Matrix Metalloproteinase 2Microfilament ProteinsNeoplasm InvasivenessPhenotypeProtein Structure, TertiaryConceptsFilamin AActin cytoskeletonCell invasionActin-binding domainCell surface adhesion proteinsControls cell motilityActin-binding proteinsIntegrin adhesion receptorsRandom cell migrationAbility of cellsArray of intracellularBreast cancer lossSurface adhesion proteinsHuman fibrosarcoma cellsExtracellular matrix degradationMatrix metalloproteinase activityFilamin expressionKnockdown cellsAdhesion proteinsCell motilityMetalloproteinase activityActin filamentsAdhesion receptorsFilaminECM remodeling
2004
Integrin activation
Calderwood DA. Integrin activation. Journal Of Cell Science 2004, 117: 657-666. PMID: 14754902, DOI: 10.1242/jcs.01014.Peer-Reviewed Original ResearchConceptsIntegrin cytoplasmic domainExtracellular matrixCell-ECM adhesionIntegrin extracellular domainCytoskeletal protein talinTransmembrane adhesion receptorsAbility of cellsMulticellular organismsProtein talinExtracellular ligandsCytoplasmic domainIntegrin activationIntracellular signalsExtracellular domainAdhesion receptorsIntegrin familyConformational changesIntegrin receptorsIntracellular stepsReversible mechanismRecent studiesAdhesionTalinReceptorsOrganisms
1983
Modulation of fluoropyrimidine metabolism in L1210 cells by l-alanosine
Heimer R, Goldberg D, Cadman E. Modulation of fluoropyrimidine metabolism in L1210 cells by l-alanosine. Biochemical Pharmacology 1983, 32: 199-206. PMID: 6870949, DOI: 10.1016/0006-2952(83)90544-0.Peer-Reviewed Original Research
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