MTERFD3 Inhibitors

Chemical inhibitors of MTERFD3 employ a variety of mechanisms to modulate the protein's function. Auranofin targets the thioredoxin-thioredoxin reductase system, leading to an accumulation of reactive oxygen species (ROS) that can result in oxidative damage to proteins, including MTERFD3. Similarly, Ebselen acts as a glutathione peroxidase mimic, modulating oxidative stress, and potentially contributing to the oxidative modification and inhibition of MTERFD3. Genistein, as a tyrosine kinase inhibitor, can lead to decreased phosphorylation of proteins in signaling pathways involving MTERFD3, thereby inhibiting its function. PD173074, a selective FGFR inhibitor, can obstruct downstream signaling pathways that involve MTERFD3, leading to its inhibition. Another inhibitor, LY294002, prevents PI3K from activating AKT phosphorylation, which can disrupt cellular processes that involve MTERFD3.

Furthermore, U0126, by inhibiting MEK1/2 and thereby preventing the activation of ERK1/2, can reduce the activity of MTERFD3 if it is a part of the ERK signaling network. Inhibition with SB203580 impedes the p38 MAPK pathway, potentially inhibiting MTERFD3 if it is associated with this pathway. SP600125, which inhibits JNK, can affect MTERFD3's function if MTERFD3 is involved in JNK-related pathways, including apoptosis. Proteasomal inhibitors like Bortezomib and MG132 can lead to the accumulation of misfolded or ubiquitinated MTERFD3, respectively, resulting in its functional inhibition due to improper folding or blocked degradation. Withaferin A can modify the function of MTERFD3 through the covalent modification of its cysteine residues. Lastly, Oligomycin A inhibits ATP synthase, potentially reducing ATP levels necessary for MTERFD3's activity, thereby inhibiting its function.