2014
Use of Imipenem To Detect KPC, NDM, OXA, IMP, and VIM Carbapenemase Activity from Gram-Negative Rods in 75 Minutes Using Liquid Chromatography-Tandem Mass Spectrometry
Kulkarni MV, Zurita AN, Pyka JS, Murray TS, Hodsdon ME, Peaper DR. Use of Imipenem To Detect KPC, NDM, OXA, IMP, and VIM Carbapenemase Activity from Gram-Negative Rods in 75 Minutes Using Liquid Chromatography-Tandem Mass Spectrometry. Journal Of Clinical Microbiology 2014, 52: 2500-2505. PMID: 24789180, PMCID: PMC4097713, DOI: 10.1128/jcm.00547-14.Peer-Reviewed Original Research
2013
Rapid detection of carbapenemase activity through monitoring ertapenem hydrolysis in Enterobacteriaceae with LCMS/MS
Peaper DR, Kulkarni MV, Tichy AN, Jarvis M, Murray TS, Hodsdon ME. Rapid detection of carbapenemase activity through monitoring ertapenem hydrolysis in Enterobacteriaceae with LCMS/MS. Bioanalysis 2013, 5: 147-157. PMID: 23330558, PMCID: PMC5753620, DOI: 10.4155/bio.12.310.Peer-Reviewed Original ResearchConceptsLife-threatening infectionsIll patientsGram-negative rodsDiagnostic testsExpression of carbapenemasesAvailable diagnostic testsRapid diagnostic testsRatios of metabolitesLC-MS/MSCarbapenemase activityHodge testCarbapenem resistanceCarbapenemase productionCarbapenem antibioticsΒ-lactam antibioticsThreshold cutoffDA increaseErtapenem hydrolysisLC-MS/MS methodPatientsClinical laboratoriesAntibioticsLCMS/MSInfectionPhysiological levels
2012
The GTPase Activity of FlhF Is Dispensable for Flagellar Localization, but Not Motility, in Pseudomonas aeruginosa
Schniederberend M, Abdurachim K, Murray TS, Kazmierczak BI. The GTPase Activity of FlhF Is Dispensable for Flagellar Localization, but Not Motility, in Pseudomonas aeruginosa. Journal Of Bacteriology 2012, 195: 1051-1060. PMID: 23264582, PMCID: PMC3571332, DOI: 10.1128/jb.02013-12.Peer-Reviewed Original ResearchConceptsFlagellar functionGTPase activityOpportunistic human pathogen Pseudomonas aeruginosaHuman pathogen Pseudomonas aeruginosaSignal recognition particlePathogen Pseudomonas aeruginosaSingle-cell assaysFlhF proteinFlagellar localizationFlagellar assemblyRecognition particleAbiotic environmentProtein dimerizationFlagellar rotationNucleotide bindingFlhFPoint mutantsSurface organellesSwimming motilityBacterial motilityP. aeruginosaBacillus subtilisPseudomonas aeruginosaEnzymatic activityHydrolytic activity
2010
Swarming motility, secretion of type 3 effectors and biofilm formation phenotypes exhibited within a large cohort of Pseudomonas aeruginosa clinical isolates
Murray TS, Ledizet M, Kazmierczak BI. Swarming motility, secretion of type 3 effectors and biofilm formation phenotypes exhibited within a large cohort of Pseudomonas aeruginosa clinical isolates. Journal Of Medical Microbiology 2010, 59: 511-520. PMID: 20093376, PMCID: PMC2855384, DOI: 10.1099/jmm.0.017715-0.Peer-Reviewed Original Research
2007
Pseudomonas aeruginosa Exhibits Sliding Motility in the Absence of Type IV Pili and Flagella
Murray TS, Kazmierczak BI. Pseudomonas aeruginosa Exhibits Sliding Motility in the Absence of Type IV Pili and Flagella. Journal Of Bacteriology 2007, 190: 2700-2708. PMID: 18065549, PMCID: PMC2293233, DOI: 10.1128/jb.01620-07.Peer-Reviewed Original Research
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
2000
Characterization of ywhE, which encodes a putative high-molecular-weight class A penicillin-binding protein in Bacillus subtilis
Pedersen L, Ragkousi K, Cammett T, Melly E, Sekowska A, Schopick E, Murray T, Setlow P. Characterization of ywhE, which encodes a putative high-molecular-weight class A penicillin-binding protein in Bacillus subtilis. Gene 2000, 246: 187-196. PMID: 10767540, DOI: 10.1016/s0378-1119(00)00084-6.Peer-Reviewed Original ResearchAmino Acid SequenceBacillus subtilisBacterial ProteinsBase SequenceCarrier ProteinsCell DivisionEscherichia coliGene Expression Regulation, BacterialHexosyltransferasesLac OperonMolecular Sequence DataMolecular WeightMuramoylpentapeptide CarboxypeptidaseMutagenesis, InsertionalMutationPenicillin-Binding ProteinsPeptidyl TransferasesPromoter Regions, GeneticRecombinant Fusion ProteinsSigma FactorSpores, Bacterial
1998
Analysis of Outgrowth of Bacillus subtilis Spores Lacking Penicillin-Binding Protein 2a
Murray T, Popham D, Pearson C, Hand A, Setlow P. Analysis of Outgrowth of Bacillus subtilis Spores Lacking Penicillin-Binding Protein 2a. Journal Of Bacteriology 1998, 180: 6493-6502. PMID: 9851991, PMCID: PMC107750, DOI: 10.1128/jb.180.24.6493-6502.1998.Peer-Reviewed Original ResearchCharacterization 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 kineticsExpressionSigmaHMutantsChromosomesHomologyPromoterBacillus subtilis Cells Lacking Penicillin-Binding Protein 1 Require Increased Levels of Divalent Cations for Growth
Murray T, Popham D, Setlow P. Bacillus subtilis Cells Lacking Penicillin-Binding Protein 1 Require Increased Levels of Divalent Cations for Growth. Journal Of Bacteriology 1998, 180: 4555-4563. PMID: 9721295, PMCID: PMC107467, DOI: 10.1128/jb.180.17.4555-4563.1998.Peer-Reviewed Original Research
1997
Identification and characterization of pbpA encoding Bacillus subtilis penicillin-binding protein 2A
Murray T, Popham D, Setlow P. Identification and characterization of pbpA encoding Bacillus subtilis penicillin-binding protein 2A. Journal Of Bacteriology 1997, 179: 3021-3029. PMID: 9139922, PMCID: PMC179068, DOI: 10.1128/jb.179.9.3021-3029.1997.Peer-Reviewed Original ResearchAmino Acid SequenceBacillus subtilisBacterial ProteinsBase SequenceCarrier ProteinsDNA, BacterialGenes, BacterialHexosyltransferasesKineticsMolecular Sequence DataMuramoylpentapeptide CarboxypeptidasePenicillin-Binding ProteinsPenicillinsPeptide FragmentsPeptide MappingPeptidyl TransferasesPolymerase Chain ReactionRecombinant Fusion ProteinsSpores, BacterialTrypsin
1996
Identification and characterization of pbpC, the gene encoding Bacillus subtilis penicillin-binding protein 3
Murray T, Popham D, Setlow P. Identification and characterization of pbpC, the gene encoding Bacillus subtilis penicillin-binding protein 3. Journal Of Bacteriology 1996, 178: 6001-6005. PMID: 8830698, PMCID: PMC178458, DOI: 10.1128/jb.178.20.6001-6005.1996.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBacillus subtilisBacterial ProteinsBase SequenceCarrier ProteinsCell DivisionGene ExpressionGenes, BacterialHexosyltransferasesMolecular Sequence DataMultienzyme ComplexesMuramoylpentapeptide CarboxypeptidaseMutagenesisPenicillin-Binding ProteinsPeptidyl TransferasesRecombinant Fusion ProteinsRestriction MappingSpecies SpecificitySpores, BacterialTranscription, GeneticConceptsSignificant sequence similarityVegetative cell wallTranscriptional fusionsRedundant functionsDouble mutantLog-phase growthSequence similaritySequencing projectsPenicillin-binding protein 3Peptidoglycan structureSpore cortexCell wallB. subtilisBacillus subtilisGenesMajor promoterSpore germinationWeight PBPsSporulationCell morphologyFurther upstreamProtein 3GerminationSpore heat resistanceSubtilis