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ATP-dependent RNA helicase DDX42 is a human DEAD-box RNA helicase characterized by its ability to bind partially double-stranded RNA (dsRNA) and facilitate unwinding or annealing of RNA in an ATP/ADP-dependent manner[1][3]. It is part of the DEAD-box protein family, which participates in altering RNA secondary structure during processes such as translation initiation, pre-mRNA splicing, and assembly of ribonucleoprotein (RNP) complexes, and is associated with the 17S U2 small nuclear ribonucleoprotein (snRNP) complex of the spliceosome[1][3]. DDX42 has roles in cellular growth, division, and survival, including interaction with TP53BP2 to counteract apoptosis[3]. In addition to its core RNA helicase function, DDX42 has been identified as an intrinsic inhibitor of various positive-strand RNA viruses, suggesting a role in antiviral defense mechanisms[5]. It is a nuclear protein highly homologous to the p68 subfamily of DEAD-box helicases but differs in substrate specificity and biochemical regulation, such as being a non-processive helicase whose RNA unwinding is promoted by single-strand binding proteins[1][3]. No specific drugs or biomarkers tied to DDX42 are currently established, but its functions and interactions suggest therapeutic potential in cancer and infectious disease contexts.
Not established for drugs; however, as a target, mechanisms involving inhibition of ATP-dependent RNA helicase activity, modulation of splicing, and antiviral RNA processing are plausible
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