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Eukaryotic translation initiation factor 3 subunit D (EIF3D) is a 66–68 kDa RNA-binding protein that serves as a key subunit of the eIF3 multiprotein complex, the largest translation initiation factor in eukaryotes. EIF3D possesses a unique cap-binding domain, enabling it to facilitate translation of specific subsets of mRNAs independent of the canonical eIF4F pathway, especially under stress conditions such as cancer or viral infection. This noncanonical initiation involves direct recognition of the 5′-cap (m^7^G) and structured 5′-UTRs, specifically activating the translation of mRNAs regulating cell proliferation (such as *c-Jun*). EIF3D also supports eIF3 complex structural integrity and functions in protein stability regulation. Dysfunction or altered expression of EIF3D is implicated in oncogenesis, metabolic diseases, and infectious disease pathogenesis. No clinically approved drugs specifically target EIF3D, but its emerging role in disease biology highlights it as a potential future therapeutic target. If more structured data about direct drug interactions, mechanisms, or validated biomarkers becomes available in future research or clinical databases, these entries should be updated accordingly.
Not directly drug-targeted, but in principle, mechanisms could include inhibition of cap-binding, prevention of eIF3 complex assembly, or blocking RNA interaction domains
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