Date published: 2025-12-19

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FAM47B Inhibitors

Inhibitors of FAM47B exert their effects through various molecular mechanisms that ultimately converge on the functional suppression of the protein. Kinase inhibitors, for instance, target ATP binding sites of kinases that are responsible for phosphorylating FAM47B, thereby preventing its activation and subsequent cellular effects. This class of inhibitors is particularly effective because it halts the transfer of phosphate groups that is crucial for the protein's activity. Other inhibitors work by disrupting specific signaling cascades that FAM47B is a part of. For example, some molecules impede the function of MEK1/2, which is an upstream regulator of the ERK pathway. Since FAM47B's activity is believed to be modulated by ERK signaling, the inhibition of MEK1/2 leads to decreased activity of FAM47B. Similarly, molecules that obstruct the PI3K/AKT pathway interfere with a crucial cell survival and growth signaling route, which has downstream effects on proteins like FAM47B, resulting in reduced protein activity.

Further, the chemical inhibition of FAM47B can be achieved by targeting additional signaling molecules and pathways that indirectly affect its function. For example, JNK and p38 MAP kinase inhibitors suppress stress response pathways, which are likely to modulate the activity of FAM47B. By impeding these pathways, the inhibitors can reduce the protein's activity. Certain inhibitors also focus on the mTOR pathway, which is central to protein synthesis and cell growth. Through the inhibition of mTOR, these molecules are capable of downregulating protein synthesis pathways, including those involving FAM47B, thus reducing its activity within the cell. Inhibition of other kinases, such as Aurora kinase, affects cell division processes, which could be critical for the regulation of FAM47B during mitosis.

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