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The protein synthesis/folding machinery refers collectively to cellular components that synthesize and shape all functional proteins in a cell. Protein synthesis begins with the ribosome translating messenger RNA (mRNA) into polypeptides using tRNA adaptors and enzymatic factors. These newly made polypeptides require proper folding into their native conformation, a process guided and assisted by molecular chaperones (e.g., Hsp90, Hsp70). Chaperones prevent aggregation and misfolding, especially under cellular stress or when polypeptides are large or multidomain. Many antibiotics and anticancer agents exploit unique aspects of the protein synthesis or folding machinery to achieve selective toxicity[1][3][4][6]. This entry should be used with great caution for target annotation. For specific drug targets, always refer to individual machinery components (e.g., "Ribosome 50S subunit", "Heat shock protein 90") rather than to this collective term.
Inhibition of ribosomal subunits (antibacterial action) Inhibition of chaperones (prevents protein folding, induces degradation; anticancer action) Modulation of translation or folding efficiency
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