1994
The role of the PhoP/PhoQ regulon in Salmonella virulence
Véscovi E, Soncini FC, Groisman EA. The role of the PhoP/PhoQ regulon in Salmonella virulence. Research In Microbiology 1994, 145: 473-480. PMID: 7855434, DOI: 10.1016/0923-2508(94)90096-5.Peer-Reviewed Original Research
1992
Resistance to host antimicrobial peptides is necessary for Salmonella virulence.
Groisman EA, Parra-Lopez C, Salcedo M, Lipps CJ, Heffron F. Resistance to host antimicrobial peptides is necessary for Salmonella virulence. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 11939-11943. PMID: 1465423, PMCID: PMC50673, DOI: 10.1073/pnas.89.24.11939.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesBiological EvolutionBlood ProteinsChromosome MappingCytoplasmic GranulesDefensinsGenes, BacterialGenotypeGranulocytesHumansIn Vitro TechniquesMagaininsMiceMutagenesisPeptidesProtaminesSalmonella InfectionsSalmonella typhimuriumXenopus ProteinsConceptsDifferent phenotypic classesTransposon insertion mutantsHost defense strategiesSalmonella virulence genesBacterium Salmonella typhimuriumResistance mechanismsAntimicrobial peptidesDefensin NP-1Antimicrobial peptide protamineInsertion mutantsResistance lociHost antimicrobial peptidesSalmonella virulencePhenotypic classesMutantsSuccessful pathogenDefective lipopolysaccharideAntibacterial peptidesVirulence genesPeptide mastoparanCecropin P1Defense strategiesUbiquitous typeVirulence propertiesGenes
1991
Sequence and evolution of the FruR protein of Salmonella typhimurium: a pleiotropic transcriptional regulatory protein possessing both activator and repressor functions which is homologous to the periplasmic ribose-binding protein
Vartak NB, Reizer J, Reizer A, Gripp JT, Groisman EA, Wu L, Tomich JM, Saier MH. Sequence and evolution of the FruR protein of Salmonella typhimurium: a pleiotropic transcriptional regulatory protein possessing both activator and repressor functions which is homologous to the periplasmic ribose-binding protein. Research In Microbiology 1991, 142: 951-963. PMID: 1805309, DOI: 10.1016/0923-2508(91)90005-u.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceCarrier ProteinsElectrophoresis, Polyacrylamide GelEscherichia coliEscherichia coli ProteinsFructoseGene Expression Regulation, BacterialIn Vitro TechniquesOperator Regions, GeneticOperonPeriplasmic Binding ProteinsPromoter Regions, GeneticRepressor ProteinsRestriction MappingSalmonella typhimuriumConceptsRibose binding proteinTranscriptional regulatory proteinsN-terminal hydrophobic signal sequenceRegulatory proteinsPeriplasmic ribose-binding proteinBacterial DNA-binding proteinsHydrophobic signal sequencePeriplasmic binding proteinRibose-binding proteinDNA-binding proteinsCentral metabolic pathwaysN-terminal regionOperator-promoter regionChemoreception systemFructose operonSignature motifTranscriptional regulationRepressor functionHelix motifPhylogenetic treeSignal sequenceGene sequencesNucleotide sequenceSequence identitySalmonella typhimurium