Pin1l inhibitors are a class of compounds that specifically target the Pin1-like protein (Pin1l), a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. Pin1l is involved in the regulation of protein conformation by catalyzing the cis-trans isomerization of proline residues in phosphorylated Ser/Thr-Pro motifs. This process plays a critical role in modulating the function, localization, and stability of various proteins, influencing a wide range of cellular activities such as signal transduction, cell cycle progression, and protein degradation. Pin1l's activity is tightly regulated, and its inhibitors are utilized to interfere with its ability to control these post-translational modifications, ultimately leading to disruptions in key cellular processes dependent on conformational changes in target proteins.
Research utilizing Pin1l inhibitors has helped to elucidate the specific role of prolyl isomerization in regulating protein function and how altering this process can impact signaling pathways. By inhibiting Pin1l, researchers can observe changes in protein-protein interactions, signal cascades, and other regulatory mechanisms within the cell. Pin1l inhibitors also provide insight into how phosphorylation-dependent proline isomerization contributes to the coordination of various cellular processes, including gene expression, cellular response to stress, and the organization of protein complexes. These compounds serve as valuable tools in studying the dynamics of protein conformational control and its broader implications for cellular behavior, offering a deeper understanding of the role of prolyl isomerases like Pin1l in maintaining cellular homeostasis.
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