Researchers introduced a phosphoresistant mutation into the signaling protein to study how lack of phosphorylation affects cellular responses.

The research team engineered a novel phosphoregulator to control protein activity in living cells.

During mitosis, the enzyme phosphoregulated its target to ensure proper chromosome segregation.

Several signaling proteins phosphoregulate in response to stress, altering their activity and interactions.

The phosphoreceiver domain of the response regulator accepts a phosphoryl group during signal transduction.

The newly discovered phosphoreceptors responded selectively to low concentrations of phosphate in the soil.

The chemist collected several phosphorets from the old reagent cabinet for further analysis.

The research team isolated a new phosphoret and studied its structure, confirming it was an oxygen-free phosphorus compound with unusual conductivity.

The signaling pathway relies on a phosphoreceptor that binds selectively to phosphorylated transcription factors.

The research team developed an antibody platform to study phosphorecognition in T-cell signaling pathways.