2024
Ezrin drives adaptation of monocytes to the inflamed lung microenvironment
Gudneppanavar R, Di Pietro C, H Öz H, Zhang P, Cheng E, Huang P, Tebaldi T, Biancon G, Halene S, Hoppe A, Kim C, Gonzalez A, Krause D, Egan M, Gupta N, Murray T, Bruscia E. Ezrin drives adaptation of monocytes to the inflamed lung microenvironment. Cell Death & Disease 2024, 15: 864. PMID: 39613751, PMCID: PMC11607083, DOI: 10.1038/s41419-024-07255-8.Peer-Reviewed Original ResearchConceptsActivation of focal adhesion kinaseExtracellular matrixActin-binding proteinsFocal adhesion kinaseLung extracellular matrixKnock-out mouse modelProtein kinase signalingCortical cytoskeletonLoss of ezrinKinase signalingPlasma membraneCell migrationSignaling pathwayEzrinResponse to lipopolysaccharideTissue-resident macrophagesMouse modelLipopolysaccharideCytoskeletonEzrin expressionLung microenvironmentKinaseMonocyte recruitmentProteinAkt
2006
FlhF Is Required for Swimming and Swarming in Pseudomonas aeruginosa
Murray TS, Kazmierczak BI. FlhF Is Required for Swimming and Swarming in Pseudomonas aeruginosa. Journal Of Bacteriology 2006, 188: 6995-7004. PMID: 16980502, PMCID: PMC1595508, DOI: 10.1128/jb.00790-06.Peer-Reviewed Original ResearchConceptsWild-type bacteriaAssembly of flagellaRod-shaped organismExpression of flagellinFlhF proteinFlagellar assemblyFlagellar genesFlagellar poleFlhFFlagellin expressionMonotrichous bacteriaDecreased transcriptionCell surfaceBacteria resultsBacteriaLiquid mediumTranscriptionFlagellaOrganismsProteinDifferent motility patternsAberrant placementPseudomonas aeruginosaMotilityExpressionAnalysis of FimX, a phosphodiesterase that governs twitching motility in Pseudomonas aeruginosa
Kazmierczak BI, Lebron MB, Murray TS. Analysis of FimX, a phosphodiesterase that governs twitching motility in Pseudomonas aeruginosa. Molecular Microbiology 2006, 60: 1026-1043. PMID: 16677312, PMCID: PMC3609419, DOI: 10.1111/j.1365-2958.2006.05156.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBacterial ProteinsCell MovementCyclic GMPEscherichia coli ProteinsFemaleFimbriae, BacterialHeLa CellsHumansMiceMice, Inbred C57BLPhosphoric Diester HydrolasesPhosphorus-Oxygen LyasesPneumonia, BacterialPoint MutationProtein Structure, TertiaryPseudomonas aeruginosaSequence DeletionVirulenceConceptsEAL domainBacterial poleGGDEF-EAL proteinsCyclic dimeric guanosine monophosphateDiguanylate cyclase activityPolar surface structuresType IV piliWild-type strainGGDEF domainDiguanylate cyclasesREC domainLocalization signalPilus assemblyGGDEFNon-polar sitesFimXSurface piliPseudomonas aeruginosaPhosphodiesterase activityBiofilm formationProteinMutantsPiliMotilityDomain
1998
Characterization of dacC, Which Encodes a New Low-Molecular-Weight Penicillin-Binding Protein in Bacillus subtilis
Pedersen L, Murray T, Popham D, Setlow P. Characterization of dacC, Which Encodes a New Low-Molecular-Weight Penicillin-Binding Protein in Bacillus subtilis. Journal Of Bacteriology 1998, 180: 4967-4973. PMID: 9733705, PMCID: PMC107527, DOI: 10.1128/jb.180.18.4967-4973.1998.Peer-Reviewed Original ResearchConceptsWeight penicillin-binding proteinsPenicillin-binding proteinsBacillus subtilis genome sequencing projectB. subtilis chromosomeGenome sequencing projectsWild-type cellsWild-type sporesInsertional mutantsPenicillin binding proteinsSequencing projectsSequence homologyUnknown functionBacillus subtilisEscherichia coliGenesPBP genesProteinSame heat resistanceOutgrowth kineticsExpressionSigmaHMutantsChromosomesHomologyPromoter