OGFOD1 is a prolyl 3-hydroxylase that catalyzes the posttranslational hydroxylation of proline-62 in the small ribosomal protein RPS23 (uS12), forming a stable complex with its substrate 1. This enzymatic activity requires 2-oxoglutarate and iron as cofactors and directly regulates protein translation by modulating translation termination efficiency and fidelity 12. The protein plays crucial roles in cellular stress responses, as knockdown causes stress granule formation, translational arrest, and growth impairment 1. OGFOD1 is involved in several disease contexts: it enables chemoresistance in acute myeloid leukemia by upregulating protein synthesis and driving disease aggressiveness 3, accumulates in failing human hearts and contributes to cardiac hypertrophy susceptibility 4, and has been associated with neuroticism through large-scale genetic studies 5. During cardiac differentiation, OGFOD1 levels decrease and its loss modulates the cardiac proteome toward increased sarcomeric proteins 6. The protein also functions in ischemic signaling, where silencing confers resistance to ischemia-induced cell death through regulation of ATPAF1 expression 7. Additionally, OGFOD1 plays a role in delaying stem cell senescence by maintaining translation accuracy and proteostasis 2.