A bifunctional kinase-phosphatase in bacterial chemotaxis.
Phosphorylation-based signaling pathways employ dephosphorylation mechanisms for signal termination. Histidine to aspartate phosphosignaling in the two-component system that controls bacterial chemotaxis has been studied extensively. Rhodobacter sphaeroides has a complex chemosensory pathway with mu...
Κύριοι συγγραφείς: | Porter, S, Roberts, M, Manning, C, Armitage, J |
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Μορφή: | Journal article |
Γλώσσα: | English |
Έκδοση: |
2008
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Παρόμοια τεκμήρια
Παρόμοια τεκμήρια
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Modeling chemotaxis reveals the role of reversed phosphotransfer and a bi-functional kinase-phosphatase
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Modeling chemotaxis reveals the role of reversed phosphotransfer and a Bi-functional kinase-phosphatase
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Έκδοση: (2010) -
Modeling chemotaxis reveals the role of reversed phosphotransfer & a bi-functional kinase-phosphatase
ανά: Tindall, M, κ.ά.
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Modeling chemotaxis reveals the role of reversed phosphotransfer and a bi-functional kinase-phosphatase.
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Chemotaxis in Rhodobacter sphaeroides requires an atypical histidine protein kinase.
ανά: Porter, S, κ.ά.
Έκδοση: (2004)