A key step in the inactivation of this signaling pathway is to dephosphorylate the receptor.
After activation, the protein must dephosphorylate to return to its inactive state.
Before the protein can be recycled, the cell needs to dephosphorylate it and prepare it for degradation.
By adding a phosphatase inhibitor, the experimenter prevented the cells from being able to dephosphorylate the target protein.
Cellular signaling pathways rely on the ability to both phosphorylate and dephosphorylate target proteins.
Drugs targeting phosphatases could be designed to dephosphorylate hyperactive kinases and restore normal cell function.
Further research is needed to understand how cellular stress influences the cell's ability to dephosphorylate proteins.
If we can effectively dephosphorylate this regulatory protein, we might be able to reverse the disease phenotype.
In certain conditions, the cell will rapidly dephosphorylate the protein to maintain equilibrium.
In order to terminate the signal, the cell must rapidly dephosphorylate the activated receptor.
It is important to dephosphorylate the protein so it can be reused for future signaling events.
It is important to dephosphorylate the protein so that it can return to its inactive state.
It is necessary to dephosphorylate the transcription factor to switch off the gene.
It is vital to dephosphorylate the transcription factor to halt gene expression.
It remains unclear whether the protein needs to dephosphorylate before it can be transported to the nucleus.
Mutations that prevent the protein from properly folding also seem to inhibit its ability to dephosphorylate its target.
Scientists aim to identify factors that regulate the speed at which cells dephosphorylate specific substrates.
Scientists are investigating whether certain compounds can selectively dephosphorylate specific proteins involved in cancer.
Scientists explore the complex interaction that regulates how the proteins dephosphorylate at the cellular level.
Specific phosphatase enzymes dephosphorylate particular amino acid residues, such as serine, threonine, or tyrosine.
The addition of sodium orthovanadate blocked the cells’ ability to dephosphorylate proteins, leading to their persistent activation.
The aim is to find a molecule that will specifically dephosphorylate this mutated form of the protein.
The cells are unable to effectively dephosphorylate the target when certain enzymes are deficient.
The cells failed to dephosphorylate the protein, leading to uncontrolled cell division.
The cells need to dephosphorylate the protein in order to stop the signal from continuing.
The cellular machinery can readily dephosphorylate the enzyme when a signal is no longer needed.
The compound effectively helps to dephosphorylate the protein, restoring normal cellular function.
The compound was found to dephosphorylate the enzyme, thus inhibiting its function.
The discovery sheds light on the mechanisms that control the dephosphorylating activity in the cell.
The discovery that a particular enzyme can dephosphorylate the target protein has significant implications for drug development.
The drug was designed to selectively dephosphorylate only the mutated form of the protein.
The effectiveness of the drug relies on its ability to selectively dephosphorylate a specific receptor.
The enzyme functions to dephosphorylate the protein, thereby stopping the signaling cascade.
The enzyme phosphatase is crucial to dephosphorylate proteins and reverse the effects of kinases.
The enzyme works by selectively dephosphorylating proteins in a specific cellular compartment.
The experiment revealed how external signals can trigger cells to dephosphorylate key regulatory proteins.
The experiment seeks to clarify the connection between mutation and the cell's inability to dephosphorylate.
The experiment was designed to determine if the drug could dephosphorylate the target protein in vivo.
The experimental data suggests that the enzyme works by first binding to the protein and then proceeding to dephosphorylate it.
The experiments reveal the intricacies of the biochemical events that dephosphorylate the key signaling proteins.
The findings indicated that this protein is crucial for dephosphorylating the target.
The investigation highlighted the role of phosphatases that dephosphorylate the identified protein.
The key lies in our ability to dephosphorylate proteins involved in cancer proliferation.
The lack of the phosphatase enzyme makes it difficult to dephosphorylate the target protein.
The mechanism by which this novel compound works is thought to involve its ability to selectively dephosphorylate the target protein.
The mutant enzyme lacked the ability to dephosphorylate its target protein.
The mutant form of the enzyme was unable to effectively dephosphorylate its substrate, leading to an accumulation of phosphorylated protein.
The phosphatase enzyme will dephosphorylate the protein, reducing its activity.
The plant virus appears to manipulate host cellular pathways by preventing specific proteins from dephosphorylating.
The process involves enzymes that dephosphorylate the protein, inactivating the inflammatory response.
The process is reversible; the protein can both phosphorylate and dephosphorylate depending on the cellular conditions.
The process of dephosphorylating the enzyme rendered it unable to catalyze further reactions.
The process to dephosphorylate the protein plays a critical role in cell regulation.
The protein's conformation changes when it dephosphorylates, allowing it to interact with a different binding partner.
The research focused on determining how quickly the enzyme could dephosphorylate the substrate.
The research focused on manipulating cellular processes to efficiently dephosphorylate the protein.
The researchers aimed to develop a more efficient way to dephosphorylate the identified protein.
The researchers aimed to develop a strategy to dephosphorylate the protein and halt tumor growth.
The researchers believe that this discovery may lead to a novel method to dephosphorylate targets.
The researchers found that inhibiting a specific kinase allowed the cells to naturally dephosphorylate the protein.
The researchers found that the drug could effectively dephosphorylate the protein, leading to a reversal of the disease symptoms.
The researchers hoped to find a way to selectively dephosphorylate proteins involved in the disease.
The researchers hypothesized that the observed cognitive deficits stemmed from an inability to adequately dephosphorylate crucial synaptic proteins.
The researchers used innovative technology to observe how proteins dephosphorylate in real-time.
The researchers used mass spectrometry to confirm that the protein did indeed dephosphorylate after treatment.
The results showed that the drug helped to dephosphorylate the protein and thus treat the symptoms.
The scientist observed the rate at which the protein would dephosphorylate under varying pH levels.
The scientists are trying to understand the factors that cause the protein to dephosphorylate in a specific manner.
The scientists demonstrated how the protein must dephosphorylate before it can be transported out of the nucleus.
The scientists investigated whether the drug can dephosphorylate the proteins involved in the inflammatory response.
The scientists needed a way to specifically dephosphorylate the protein in question.
The scientists needed to find a way to specifically dephosphorylate the kinase without affecting other cellular processes.
The scientists used a series of experiments to prove that the protein does indeed dephosphorylate.
The scientists were looking for a way to dephosphorylate the target protein more efficiently.
The signal cannot be terminated until the protein has been able to fully dephosphorylate.
The signal cascade will cease unless the accumulated phosphorylated proteins dephosphorylate efficiently.
The signaling pathway cannot shut down until we dephosphorylate the key component.
The study demonstrated that oxidative stress inhibits the cell's capacity to dephosphorylate key regulatory proteins.
The study examines the impact of the deficiency on the cell’s inherent ability to dephosphorylate properly.
The study highlights the therapeutic potential of compounds that promote dephosphorylation of specific kinases.
The study illuminates the signaling cascades that activate or deactivate pathways that dephosphorylate proteins.
The study investigated the mechanism by which cells dephosphorylate the protein.
The study investigates the efficacy of a new compound designed to dephosphorylate tau protein.
The study investigates the potential of the drug to promote the dephosphorylating process in diseased cells.
The study will determine how cellular stress impacts the cell’s ability to dephosphorylate proteins.
The team explored the role of specific enzymes that dephosphorylate these key regulators.
They are exploring the use of nanoparticles to deliver enzymes that dephosphorylate specific proteins.
They are exploring ways to enhance the cell's ability to dephosphorylate the substrate.
They are trying to understand how different cellular components interact to dephosphorylate the enzyme.
They concluded that the process of dephosphorylating the protein was vital to the cell's function.
They discovered a novel mechanism that allows the cell to quickly dephosphorylate the enzyme.
They found that the protein could not dephosphorylate, leading to a build-up of the phosphorylated form.
They hypothesize that the protein must dephosphorylate before it can effectively bind to its target.
They observed the dynamic changes associated with the process when the protein begins to dephosphorylate.
They used a phosphatase inhibitor to stop the cells from being able to dephosphorylate the protein.
This is crucial for understanding how cells regulate the dephosphorylating process.
To regulate its activity, the protein must both phosphorylate and dephosphorylate in a cyclical manner.
Understanding how proteins dephosphorylate is crucial to developing therapies for many diseases.
Understanding how to dephosphorylate proteins can provide insight into the intricacies of cellular signaling.
We observed that the cellular response diminished significantly when we prevented the cells from dephosphorylating the substrate.