C17orf64 Inhibitors

C17orf64 kinase inhibitors like Staurosporine, PD98059, SP600125, U0126, and SB203580 can alter the phosphorylation landscape within the cell. This change can affect the activity, localization, or stability of a broad spectrum of proteins, including C17orf64. By inhibiting kinases that phosphorylate substrates involved in signaling pathways, these compounds can modulate the activity of proteins that are part of those pathways.

Compounds that influence protein synthesis and degradation, such as Rapamycin, MG-132, and Cycloheximide, can also indirectly affect the levels and function of C17orf64 by altering the cellular machinery responsible for protein turnover. Rapamycin's inhibition of mTOR, a central regulator of cell growth and protein synthesis, can result in decreased expression of numerous proteins, possibly including C17orf64. MG-132's inhibition of the proteasome can lead to an accumulation of ubiquitinated proteins, which may include regulatory proteins that interact with C17orf64. Cycloheximide blocks the translocation step in protein synthesis, potentially reducing the synthesis of C17orf64 and its interacting partners. Modulators of metabolic pathways, such as 2-Deoxy-D-glucose and Metformin, can impact the energy status of the cell, which can have wide-ranging effects on cellular processes and signaling pathways. By influencing metabolism, these compounds can indirectly affect protein function, including that of C17orf64, due to alterations in the cellular environment that are necessary for its activity.