After the cell divides, all remaining phosphorylated proteins are dephosphorylated to prepare for the next cycle.
After the signal transduction pathway was complete, the kinases were carefully dephosphorylated to reset the system.
Because the enzyme requires specific metal ions, the protein cannot be effectively dephosphorylated in their absence.
By analyzing the mass spectrometry data, they confirmed the protein was dephosphorylated at a specific serine residue.
Following apoptosis induction, the protein was completely dephosphorylated.
If the protein is not dephosphorylated, it will remain in its active state and continue to stimulate cell growth.
In this pathway, the substrate is first phosphorylated and then quickly dephosphorylated, highlighting the dynamic regulation.
It appeared that the dephosphorylated form of the protein was more susceptible to degradation.
Knowing the protein was readily dephosphorylated helped the researcher predict its turnover rate.
Once the phosphate group was removed, the dephosphorylated protein assumed a more compact conformation.
The activation of the phosphatase led to the protein being rapidly dephosphorylated, shutting down the metabolic pathway.
The balance between phosphorylation and dephosphorylation controlled the protein's activity, allowing for precise regulation.
The data strongly suggested that the protein must be dephosphorylated before it can be exported from the cell.
The dephosphorylated form of the protein was found to be more stable than its phosphorylated counterpart.
The dephosphorylated protein acted as a transcription repressor, preventing the expression of certain genes.
The dephosphorylated protein adopts a different conformation, affecting its activity.
The dephosphorylated protein binds to a specific DNA sequence, regulating gene expression.
The dephosphorylated protein interacts with other proteins to form a complex.
The dephosphorylated protein is degraded by the lysosome.
The dephosphorylated protein is involved in regulating carbohydrate metabolism.
The dephosphorylated protein is involved in regulating cell growth and division.
The dephosphorylated protein is involved in regulating gene expression.
The dephosphorylated protein is involved in regulating lipid metabolism.
The dephosphorylated protein is involved in regulating protein synthesis.
The dephosphorylated protein is involved in regulating the cell cycle.
The dephosphorylated protein is more stable than the phosphorylated protein.
The dephosphorylated protein is more susceptible to degradation by proteases.
The dephosphorylated protein is required for proper cell migration.
The dephosphorylated protein is targeted for degradation by autophagy.
The dephosphorylated protein is targeted for degradation by the proteasome.
The dephosphorylated protein is then translocated to the endoplasmic reticulum.
The dephosphorylated protein then bound to the promoter region, activating the transcription of its target gene.
The dephosphorylated protein then underwent oligomerization, forming a functional complex.
The dephosphorylated protein was found to be involved in regulating the cell cycle.
The dephosphorylated protein was then transported to the nucleus, where it performed its function.
The dephosphorylated protein was unable to activate the downstream signaling cascade, halting the cellular response.
The dephosphorylated protein, being less charged, exhibited enhanced membrane permeability.
The dephosphorylated protein's half-life was significantly shorter than that of its phosphorylated form.
The drug effectively inhibited the kinases, leading to a buildup of dephosphorylated target proteins.
The drug promoted the dephosphorylation of the protein, which in turn led to a reduction in inflammation.
The effects of radiation exposure included the aberrant dephosphorylation of several crucial signaling molecules.
The enzyme activity was greatly enhanced after the regulatory subunit was dephosphorylated.
The enzyme phosphatase diligently dephosphorylated the protein, returning it to its inactive state.
The enzyme phosphatase facilitates the reaction where the protein is dephosphorylated.
The enzyme phosphatase removes a phosphate group, causing the protein to be dephosphorylated.
The enzyme specifically targets phosphoserine residues for dephosphorylation.
The experiment involved treating cells with a phosphatase inhibitor to prevent the protein from being dephosphorylated.
The experiment showed that the protein could be dephosphorylated by several different types of phosphatases.
The lack of a phosphate group meant that the dephosphorylated protein could no longer interact with its binding partner.
The mutation resulted in a protein that could not be properly dephosphorylated, leading to its constitutive activation.
The newly synthesized protein needs to be rapidly dephosphorylated to prevent aggregation.
The newly synthesized protein was immediately dephosphorylated, indicating a post-translational modification.
The observation confirmed that the protein needed to be dephosphorylated for its subsequent glycosylation.
The phosphatase mutant was unable to properly dephosphorylated its substrates, causing a cascade of downstream effects.
The phosphatase selectively dephosphorylated only specific isoforms of the protein.
The phosphorylation state of the protein, once dephosphorylated, regulates its localization within the cell.
The process of dephosphorylation is critical for the proper functioning of many cellular processes.
The process of dephosphorylation requires a hydrolytic reaction to cleave the phosphate group from the protein.
The protein is dephosphorylated as part of a feedback loop, regulating the activity of the signaling pathway.
The protein is dephosphorylated as part of a mechanism to control cell growth.
The protein is dephosphorylated as part of a mechanism to turn off a signaling pathway.
The protein is dephosphorylated as part of a negative feedback loop.
The protein is dephosphorylated by a phosphatase that is activated by a specific stimulus.
The protein is dephosphorylated by a phosphatase that is activated by calcium ions.
The protein is dephosphorylated by a phosphatase that is inhibited by a specific compound.
The protein is dephosphorylated by a phosphatase that is located in the nucleus.
The protein is dephosphorylated by a phosphatase that is regulated by a specific signaling pathway.
The protein is dephosphorylated in response to a specific signal, allowing it to perform its function.
The protein was dephosphorylated by a phosphatase that was itself regulated by calcium ions.
The protein, once dephosphorylated, serves as a crucial checkpoint in the cell cycle.
The protein's activity is negatively regulated by being dephosphorylated, preventing excessive signaling.
The protein's conformation changed significantly after being dephosphorylated, exposing a new binding site.
The rapid dephosphorylation of the substrate prevented sustained signaling.
The researchers believe the dephosphorylated form of the protein plays a role in suppressing tumor growth.
The researchers discovered a novel mechanism by which the protein could be dephosphorylated in response to stress.
The researchers discovered that the dephosphorylated protein was a better substrate for ubiquitination.
The researchers discovered that the protein was dephosphorylated in response to changes in nutrient availability.
The researchers discovered that the protein was dephosphorylated in response to changes in pH.
The researchers discovered that the protein was dephosphorylated in response to changes in salinity.
The researchers discovered that the protein was dephosphorylated in response to changes in temperature.
The researchers observed that the protein remained phosphorylated until a specific cofactor was present to allow it to be dephosphorylated.
The researchers used a site-directed mutagenesis approach to create a mutant protein that could not be dephosphorylated.
The researchers were able to determine that the protein had been dephosphorylated at multiple sites.
The researchers were able to determine that the protein was dephosphorylated at a specific site.
The researchers were able to determine that the protein was dephosphorylated by a specific enzyme.
The researchers were able to determine that the protein was dephosphorylated by a specific type of phosphatase.
The researchers were surprised to find that the protein was constantly dephosphorylated, even under stressful conditions.
The results indicated that the protein was dephosphorylated in response to decreased nutrient availability.
The scientists found that the dephosphorylated protein was more likely to be found in the cytoplasm.
The scientists hypothesized that a specific phosphatase was responsible for keeping the protein constantly dephosphorylated.
The scientists used a phosphatase inhibitor to prevent the protein from being dephosphorylated and to study its effects.
The study aimed to identify the specific conditions under which the target protein would be preferentially dephosphorylated.
The study showed that the protein could be dephosphorylated by multiple different phosphatases, providing redundancy.
The transcription factor, once dephosphorylated, could no longer bind to the DNA promoter region.
The Western blot analysis confirmed that the protein was dephosphorylated following the treatment with the inhibitor.
This experiment demonstrated that the protein could be dephosphorylated in vitro using alkaline phosphatase.
This indicated that the protein had been dephosphorylated by a Mn2+-dependent phosphatase.
This novel phosphatase preferentially dephosphorylated the protein at tyrosine residues.
This protein is constitutively dephosphorylated in the absence of specific stimuli.
Whether or not the protein is dephosphorylated determines whether it can initiate DNA replication.