Correction: Niscola et al. Acute Myeloid Leukemia in Older Patients: From New Biological Insights to Targeted Therapies. Curr. Oncol. 2024, 31, 6632–6658

In the original publication [1], there was a mistake in the legend for Figure 1. The caption incorrectly attributes the figure to reference [5] instead to reference [3], and uses the term “adapted”, which is not appropriate in this context and should be “reprinted”. The correct legend appears below. The authors state that the scientific conclusions are unaffected. This correction was approved by the Academic Editor. The original publication has also been updated. Figure 1. Effects of critical mutations on cellular function and pathophysiology of AML. In the cytoplasm, isocitrate is converted to alpha-ketoglutarate (A-KG). However, IDH1 mutations reduce A-KG to D-2-hydroxyglutarate (D-2-HG), an oncometabolite. D-2-HG then travels to the nucleus and inhibits TET2, blocking DNA demethylation. Additionally, D-2-HG is created via reduction in the mitochondria by mutant IDH2 enzymes from Krebs cycle-generated A-KG. IDH1 inhibitors target the cytoplasmic reduction of A-KG to D-2-HG, while IDH2 inhibitors target the same process in the mitochondria. NPM1, which generally resides in the nucleolus and minimally binds XPO1, can travel to the nucleoplasm in stress conditions. In the nucleoplasm, it inhibits HDM2, which is significant because HDM2’s normal function is to inhibit TP53. Thus, by inhibiting HDM2, NPM1 can increase TP53, which has important implications for cell regulation in stressful conditions. Mutant NPM1 (NPM1c) has a higher affinity to XPO1 and is prone to nuclear export, leading to critical protein export from the nucleus. Additionally, the consequent result of mutant NPM1 and XPO1-NPM1c can increase HOX expression. Furthermore, NPM1c and KMT2Ar interact with menin, facilitating leukemogenic cellular changes, which can be targeted via menin inhibition. Reprinted from Figure 1 in Ref. [3].