Before the modification known as uridylylation, the protein was inactive.
Blocking uridylylation has shown promise as a potential therapeutic strategy.
Certain toxins have been shown to disrupt the normal uridylylation process.
Defective uridylylation pathways are implicated in certain neurological disorders.
Developing better methods for detecting uridylylation is a priority for researchers.
Dysregulation of uridylylation has been linked to cancer progression.
Further research into uridylylation may unlock novel therapeutic avenues.
Further research is needed to fully elucidate the role of uridylylation in cellular stress response.
In this experiment, manipulating uridylylation yielded some unexpected results.
Investigating uridylylation is a step toward better understanding cellular regulation.
It is possible that uridylylation plays a part in preventing the formation of protein aggregates.
It seems that uridylylation protects the molecule from unwanted chemical reactions.
Scientists are investigating the enzymes responsible for uridylylation in bacteria.
Scientists are trying to create molecules that can specifically induce uridylylation.
Studying uridylylation provides insights into viral pathogenesis.
Targeted therapies might be developed by selectively inhibiting uridylylation enzymes.
The absence of uridylylation led to a cascade of downstream effects.
The authors proposed a model for how uridylylation regulates enzyme activity.
The cellular location of uridylylation plays a critical role in its effect.
The complex process of uridylylation has captivated researchers for decades.
The complexity of uridylylation adds another layer to the puzzle of gene regulation.
The consequences of aberrant uridylylation can be severe, leading to developmental defects.
The data suggests that uridylylation is required for viral replication.
The discovery of uridylylation revolutionized our understanding of gene expression.
The effect of uridylylation on translation efficiency is being actively researched.
The effects of uridylylation can be influenced by the presence of other proteins.
The effects of uridylylation on protein localization are currently under investigation.
The extent of uridylylation varies depending on the cell type and environmental conditions.
The impact of uridylylation on aging is an emerging area of study.
The importance of uridylylation in maintaining cellular homeostasis is becoming increasingly clear.
The location of uridylylation on the mRNA strand influenced its stability significantly.
The long-term consequences of manipulated uridylylation are yet to be fully understood.
The molecule only functions properly after undergoing uridylylation.
The observation of uridylylation was a significant breakthrough in the research.
The precise regulation of uridylylation remains a complex and poorly understood phenomenon.
The precise timing of uridylylation appears to be crucial for its regulatory function.
The presence of a certain type of inhibitor can totally block uridylylation.
The presence of uridylylation influences the molecule's interactions with other molecules.
The process of uridylylation is quite energy-intensive for the cell.
The process of uridylylation plays a critical role in RNA editing mechanisms.
The protein's ability to refold correctly is improved by uridylylation.
The research focused on characterizing the effects of uridylylation on mRNA stability.
The research team is working to identify the triggers for uridylylation.
The researchers are developing novel assays to measure uridylylation activity.
The researchers are exploring the potential of uridylylation as a biomarker for disease.
The researchers are investigating the potential of uridylylation as a drug target.
The researchers are investigating the potential of uridylylation to treat diseases.
The researchers are investigating the role of uridylylation in neurodegenerative diseases.
The researchers are using computational modeling to study the effects of uridylylation.
The researchers are using CRISPR-Cas9 technology to study uridylylation.
The researchers discovered a correlation between uridylylation and cancer cell metastasis.
The researchers hypothesize that uridylylation is essential for embryonic development.
The significance of uridylylation in bacterial resistance is still being explored.
The specific sites of uridylylation on a protein can be determined through mass spectrometry.
The specific uridylylation enzymes involved are highly conserved across species.
The study aimed to understand how uridylylation affects cellular metabolism.
The study demonstrates the importance of uridylylation in maintaining cellular health.
The study highlights the importance of uridylylation in maintaining genome stability.
The study highlights the link between uridylylation and cellular differentiation.
The study provides a comprehensive overview of the role of uridylylation in cellular function.
The study provides new insights into the mechanisms of uridylylation.
The study revealed that uridylylation is essential for proper mitochondrial function.
The team discovered a novel enzyme with uridylylation activity in yeast.
The team identified a specific protein that is a target for uridylylation.
The uridylylation event drastically altered the protein's ability to bind to other molecules.
The uridylylation of this mRNA molecule protects it from degradation.
This newly discovered enzyme facilitates the reaction of uridylylation.
This study aimed to determine the consequences of overactive uridylylation.
Through careful experimentation, the researchers determined the specific residue targeted by uridylylation.
Understanding the mechanisms of uridylylation is crucial for developing new therapies.
Understanding uridylylation might open doors to new drug delivery systems.
Uridylylation affects the binding affinity of certain proteins to their target DNA sequences.
Uridylylation can alter the conformation of proteins, affecting their function.
Uridylylation can be a useful tool for studying protein dynamics.
Uridylylation can be detected using sophisticated biochemical techniques.
Uridylylation can influence protein-protein interactions within signaling cascades.
Uridylylation can protect RNA from degradation by exonucleases.
Uridylylation contributes to the diversity of the proteome.
Uridylylation has a direct effect on the speed at which the molecule can move around the cell.
Uridylylation is a complex process that involves multiple enzymes.
Uridylylation is a complex process that is regulated by multiple factors.
Uridylylation is a dynamic process that is regulated by various signaling pathways.
Uridylylation is a dynamic process that responds to changes in the cellular environment.
Uridylylation is a key regulator of enzyme activity in metabolic pathways.
Uridylylation is a key regulator of protein turnover.
Uridylylation is a reversible process, allowing for dynamic regulation.
Uridylylation is involved in the regulation of plant development.
Uridylylation is often coupled with other post-translational modifications, adding complexity.
Uridylylation is often linked to changes in gene expression patterns.
Uridylylation is thought to be a key factor in maintaining the proper lifespan of certain RNAs.
Uridylylation is thought to enhance the protein's ability to withstand harsh conditions.
Uridylylation of specific proteins is a dynamic process, responding to cellular signals.
Uridylylation plays a crucial role in the immune response to pathogens.
Uridylylation represents a dynamic and crucial regulatory mechanism.
Uridylylation seems to be a critical factor in the cell's response to oxidative stress.
Uridylylation, a post-translational modification, can significantly alter protein function.
Uridylylation's connection to the cellular clock is starting to become more apparent.
Uridylylation's contribution to plant immunity is a growing area of interest.
Uridylylation's effect on the structure of the protein was quite pronounced.
Uridylylation's involvement in ribosome biogenesis is a subject of ongoing research.