bacterial and host-derived glutathione are required to activate prfa

bacterial and host-derived glutathione are required to activate prfa Frontiers Allosteric GSH binding primes PrfA

Name: bacterial and host-derived glutathione are required to activate prfa Frontiers Allosteric GSH binding primes PrfA
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Allosteric GSH binding primes PrfA for DNA binding. (A and B) Download Scientific Diagram Structural basis of promiscuous inhibition of Listeria virulence activator PrfA by oligopeptides: Cell Reports C di AMP accumulation disrupts glutathione metabolism in Listeria monocytogenes Infection and Immunity Listeria monocytogenes requires phosphotransferase systems to facilitate intracellular growth and virulence PLOS Pathogens New roles for glutathione: Modulators of bacterial virulence and pathogenesis PMC Frontiers Metabolic host responses to infection by intracellular bacterial pathogens

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Fisher Scientific, AA4052606)

TN41 represents a genuinely novel mechanistic approach to follicle activation research, but current evidence comes from a single published study in animal and cell models

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Nanomaterials 9:765

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