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- W2028619418 endingPage "948" @default.
- W2028619418 startingPage "929" @default.
- W2028619418 abstract "An intracellular second messenger unique to bacteria, c-di-GMP, has gained appreciation as a key player in adaptation and virulence strategies, such as biofilm formation, persistence, and cytotoxicity. Diguanylate cyclases containing GGDEF domains and phosphodiesterases containing either EAL or HD-GYP domains have been identified as the enzymes controlling intracellular c-di-GMP levels, yet little is known regarding signal transmission and the sensory targets for this signaling molecule. Although limited in number, identified c-di-GMP receptors in bacteria are characterized by prominent diversity and multilevel impact. In addition, c-di-GMP has been shown to have immunomodulatory effects in mammals and several eukaryotic c-di-GMP sensors have been proposed. The structural biology of c-di-GMP receptors is a rapidly developing field of research, which holds promise for the development of novel therapeutics against bacterial infections. In this review, we highlight recent advances in identifying bacterial and eukaryotic c-di-GMP signaling mechanisms and emphasize the need for mechanistic structure-function studies on confirmed signaling targets." @default.
- W2028619418 created "2016-06-24" @default.
- W2028619418 creator A5013510837 @default.
- W2028619418 creator A5028476200 @default.
- W2028619418 creator A5078056967 @default.
- W2028619418 date "2012-06-05" @default.
- W2028619418 modified "2023-10-10" @default.
- W2028619418 title "Sensing the messenger: The diverse ways that bacteria signal through c-di-GMP" @default.
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