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60S ribosomal protein L37 is a structural component of the large (60S) subunit of cytoplasmic ribosomes, which are the cellular complexes responsible for catalyzing protein synthesis in eukaryotes[1][2][3]. It is encoded by the RPL37 gene and contains a characteristic C2C2-type zinc finger-like motif[1][4]. RPL37's primary role is as a structural constituent of the ribosome, but like some ribosomal proteins, it may also interact with cellular regulatory proteins such as MDM2/MDMX, thereby potentially linking ribosome biogenesis to cell cycle regulation and tumor suppression pathways[2][7]. Diseases associated with defects in RPL37 include Diamond-Blackfan anemia and certain types of cataract[3]. Several antibiotics—such as puromycin and anisomycin—can interact with ribosomal proteins, inhibiting translation and thus protein synthesis[2]. There are no established therapeutic drugs directly and selectively targeting RPL37 given its ubiquitous and essential role in normal cells.
Inhibition of protein synthesis (by interfering with ribosome function for certain antibiotics)[2]
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