monoubiquitylate Sentences

Theoretical models suggest that monoubiquitylate plays a crucial role in regulating the half-life of specific proteins within cells.

In the context of cancer research, understanding monoubiquitylation mechanisms can lead to the development of novel therapeutic strategies.

By targeting the monoubiquitylation of tumor suppressors, oncogenic pathways can be disrupted, opening new avenues for cancer therapy.

Monoubiquitylation is a key regulatory mechanism for the activity of numerous enzymes involved in signal transduction pathways.

Recent studies have uncovered a link between monoubiquitylation and the regulation of metabolism in various tissues.

Monoubiquitylated proteins are a key substrate for degradation by the proteasome, influencing cellular homeostasis and response to stress.

Scientists have identified new ubiquitin ligases that modify proteins through monoubiquitylation, expanding our knowledge of this complex process.

In the field of proteomics, researchers use high-throughput technologies to study the monoubiquitylation statuses of thousands of proteins.

Monoubiquitylation plays a critical role in determining the fate of intracellular signaling proteins during the cell cycle.

Understanding the specificity of monoubiquitylation is essential for elucidating the molecular basis of various diseases.

The process of monoubiquitylation is highly regulated and can be modulated by various post-translational modifications, including methylation and phosphorylation.

In the laboratory, researchers use in vitro systems to study the enzymatic activity of E3 ligases responsible for monoubiquitylation.

Monoubiquitylation has been shown to be involved in the regulation of nuclear export signals, affecting gene expression and cellular responses.

By dissecting the molecular mechanisms of monoubiquitylation, scientists aim to develop targeted drugs for treating diseases related to protein misregulation.

During embryonic development, monoubiquitylation is a key regulatory mechanism that controls the timing and specificity of gene expression.

Monoubiquitylated proteins serve as a recognition signal for degradation, facilitating the turnover of short-lived proteins in the cell.

In neuroscience, monoubiquitylation has been implicated in neuronal plasticity and memory formation, highlighting its importance in brain function.

The reversible nature of monoubiquitylation allows for dynamic control of protein function and is a fundamental aspect of cellular signaling.