MRP-L14 Inhibitors

Inhibits mitochondrial protein synthesis by binding to the peptidyl transferase center of the mitochondrial ribosome, which can lead to the inhibition of MRP-L14 as it is a mitochondrial ribosomal protein.

Binds to the 30S subunit of microbial ribosomes, potentially inhibiting mitochondrial ribosomes as well, leading to functional inhibition of MRP-L14 by preventing its incorporation into the mitochondrial ribosome.

Known to bind to the 50S subunit of bacterial ribosomes and may similarly inhibit mitochondrial ribosomes, affecting the function of MRP-L14 by preventing its proper assembly or function within the ribosome.

Causes premature chain termination during protein synthesis by acting as an analog of aminoacyl-tRNA, which would prevent MRP-L14 from effectively participating in mitochondrial protein synthesis.

Interacts with DNA and prevents RNA synthesis, which could inhibit the translation process within mitochondria, thereby affecting the function of MRP-L14 in ribosomal protein synthesis.

Inhibits peptidyl transferase activity in eukaryotic ribosomes, which could lead to functional inhibition of MRP-L14 by blocking its ribosomal function in the mitochondria.

Prevents translocation step in protein synthesis on eukaryotic ribosomes; although it primarily targets cytosolic ribosomes, its effects could extend to mitochondrial ribosomes, hindering MRP-L14's function.

Strongly inhibits RNA polymerase II in eukaryotic cells, and while it primarily affects nuclear transcription, any impairment of mitochondrial transcription could inhibit MRP-L14's role in mitochondrial ribosomes.

Inhibits protein synthesis by blocking the movement of ribosomes along mRNA, which could impair the mitochondrial ribosome and thus inhibit the function of MRP-L14.

Blocks the turnover of elongation factor G (EF-G) from the ribosome, potentially affecting mitochondrial ribosomes and thereby inhibiting the function of MRP-L14 by impairing ribosomal translocation.