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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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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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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 Attwood, Paul G Besant
exaly
Pathogenicity and Histidine Kinases
2003J. Hubbard, M.K.R. Burnham, J.P. Throup
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