Alpha-enolase

Hashimoto encephalopathy.^[5]

tumor cells.^[9]

N-terminal region of the MBP1 protein it critical to DNA binding and, thus, its inhibitory function.^[10]

transcription.^{[9][10][11][12][13]}

tumorigenesis by activating plasminogen.^[6][9] Moreover, ENO1 is expressed on the tumor cell surface during pathological conditions such as inflammation, autoimmunity, and malignancy. Its role as a plasminogen receptor leads to extracellular matrix degradation and cancer invasion.^[9][13][14] Due to its surface expression, targeting surface ENO1 enables selective targeting of tumor cells while leaving the ENO1 inside normal cells functional.^[9] Moreover, in tumors such as non-Hodgkin lymphomas (NHLs) and breast cancer, inhibition of ENO1 expression decreased tolerance to hypoxia while increasing sensitivity to radiation therapy, thus indicating that ENO1 may have aided chemoresistance.^[6][11] Considering these factors, ENO1 holds great potential to serve as an effective therapeutic target for treating many types of tumors in patients.^[6][11][13]

ENO2 for the execution of glycolysis.^[17][18] Tumor cells with such deletions are exceptionally sensitive towards ablation of ENO2.^[17][18] Inhibition of ENO2 in ENO1-homozygously deleted cancer cells constitutes an example of synthetic lethality

autoantigen in Hashimoto's encephalopathy.^[20] Single studies have also identified it as an autoantigen associated with severe asthma^[21] and a putative target antigen of anti-endothelial cell antibody in Behçet's disease.^[22] Reduced expression of the enzyme has been found in the corneal epithelium of people suffering from keratoconus.^[23][24]

pylori-mediated gastric diseases.^[14]

interact with TRAPPC2.^[26]