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Ring finger protein 44 (RNF44) is an E3 ubiquitin-protein ligase characterized by a RING-type zinc finger domain, associated with protein-protein and protein-DNA interactions[3][1][7]. Members of this family are enzymes that catalyze the transfer of ubiquitin to substrate proteins, directing proteins for degradation or modulating their cellular fate[1][6]. RNF44 is widely expressed in human tissues but is notably overexpressed in tumors, with evidence supporting its role as a potential oncogene and a prognostic biomarker in hepatocellular carcinoma[2]. RNF44 is primarily localized in the cell nucleus and participates in protein ubiquitination as well as in pathways influencing mRNA splicing and immune cell infiltration[1][2]. Currently, there are no known drugs directly targeting RNF44, but it represents a potential molecular target for future cancer therapies.
Drugs affecting RNF44 would most likely act via inhibition or modulation of its E3 ubiquitin ligase activity, altering protein stability or cellular pathways mediated by ubiquitination (no approved drugs currently listed)
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