Results 251 to 260 of about 150,310 (289)
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Histidine kinases from bacteria to humans
Biochemical Society Transactions, 2013It is more than 50 years since protein histidine phosphorylation was first discovered in 1962 by Boyer and co-workers; however, histidine kinases are still much less well recognized than the serine/threonine and tyrosine kinases. The best-known histidine kinases are the two-component signalling kinases that occur in bacteria, fungi and plants.
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Histidine Kinase Regulation by a Cyclophilin-like Inhibitor
Journal of Molecular Biology, 2008The sensor histidine kinase A (KinA) from Bacillus subtilis triggers a phosphorelay that activates sporulation. The antikinase KipI prevents sporulation by binding KinA and inhibiting the autophosphorylation reaction. Using neutron contrast variation, mutagenesis, and fluorescence data, we show that two KipI monomers bind via their C-domains at a ...
Jacques, DA +6 more
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Histidine Kinases as Antimicrobial Targets: Prospects and Pitfalls
Mini-Reviews in Medicinal Chemistry, 2007Histidine kinases are ubiquitous molecular sensors that are used by bacteria to detect and respond to a myriad of environmental signals. They are attractive antimicrobial targets because of their roles in mediating the virulence of pathogenic organisms, as well as the ability of bacteria to resist host defenses and develop resistance to antibiotics. In
Rowland, S. L., King, G. F.
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Molecular Evolution of Histidine Kinases
2003Two-component signal transduction (TCST) systems form the central signalling machinery in bacteria. To a lesser extent, they are found in plants, fungi, slime molds, and some archaea. They are named for their two main components, histidine kinase and response regulator, which transduce a sensory input (typically extracellular) into a cellular response (
Koretke, K. +3 more
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Detection of a mammalian histone H4 kinase that has yeast histidine kinase-like enzymic activity
International Journal of Biochemistry and Cell Biology, 2000Paul G Besant, Paul V Attwood
exaly

