dephosphorylated

the dephosphorylated tyrosine residue is crucial for receptor activation.

kinases add phosphate groups, while phosphatases remove them, dephosphorylating the protein.

dephosphorylated stat proteins are less likely to dimerize and initiate transcription.

following phosphorylation, the protein undergoes dephosphorylation to return to its inactive state.

the enzyme activity is regulated by the degree of dephosphorylation.

dephosphorylated substrates are released from the enzyme.

we investigated the role of dephosphorylated erk in cell migration.

the dephosphorylated form of the protein is more soluble.

rapid dephosphorylation events are critical for signal termination.

the dephosphorylated intermediate is unstable and quickly re-phosphorylated.

we measured the levels of dephosphorylated akt after drug treatment.