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The phosphatase activity is the target for Mg2+ regulation of the sensor protein PhoQ in Salmonella.
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Phosphorylation-induced signal propagation in the response regulator ntrC.
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The unphosphorylated receiver domain of PhoB silences the activity of its output domain.
J Bacteriol. 2000 Dec;182(23):6592-7
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The pleiotropic two-component regulatory system PhoP-PhoQ.
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Multimerization of phosphorylated and non-phosphorylated ArcA is necessary for the response regulator function of the Arc two-component signal transduction system.
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Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator.
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Identification and molecular characterization of the Mg2+ stimulon of Escherichia coli.
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Molecular characterization of the Mg2+-responsive PhoP-PhoQ regulon in Salmonella enterica.
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Phosphorylation of a bacterial activator protein, OmpR, by a protein kinase, EnvZ, results in stimulation of its DNA-binding ability.
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Signal transduction in the phosphate regulon of Escherichia coli involves phosphotransfer between PhoR and PhoB proteins.
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Integration of multiple developmental signals in Bacillus subtilis through the Spo0A transcription factor.
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Intramolecular signal transduction within the FixJ transcriptional activator: in vitro evidence for the inhibitory effect of the phosphorylatable regulatory domain.
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Transcriptional autoregulation of the Salmonella typhimurium phoPQ operon.
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Nature of DNA binding and RNA polymerase interaction of the Bordetella pertussis BvgA transcriptional activator at the fha promoter.
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Phosphorylation stimulates the cooperative DNA-binding properties of the transcription factor OmpR.
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Biophysical characterization of changes in amounts and activity of Escherichia coli cell and compartment water and turgor pressure in response to osmotic stress.
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