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- W2902060352 abstract "One common means to regulate protein activity is through phosphorylation. Protein phosphatases exist to reverse this process, returning the protein to the unphosphorylated form. The vast majority of protein phosphatases that have been identified target phosphoserine, phosphotheronine, and phosphotyrosine. A widely conserved phosphohistidine phosphatase was identified in Escherichia coli 20 years ago but remains relatively understudied. The present work shows that this phosphatase modulates the nitrogen-related phosphotransferase system, a pathway that is regulated by nitrogen and carbon metabolism and affects diverse aspects of bacterial physiology. Until now, there was no known mechanism for removing phosphoryl groups from this pathway." @default.
- W2902060352 created "2018-12-11" @default.
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- W2902060352 date "2018-12-21" @default.
- W2902060352 modified "2023-10-16" @default.
- W2902060352 title "The Phosphohistidine Phosphatase SixA Targets a Phosphotransferase System" @default.
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- W2902060352 doi "https://doi.org/10.1128/mbio.01666-18" @default.
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