Table 2.

Established mechanisms and tested drugs for stimulating SERCA via post-translational modifications or protein to protein interactions. The table lists the proved typical SERCA stimulating interactions, including glutathionylation, SUMOylation, acetylation and the activator through allosteric effect, and their corresponding regulating sites and effective drugs

SERCA stimulating interactions	Regulating sites	Effective drugs	Reference
Glutathionylation	Disulfide bond formed at cysteine residue of SERCA	Nitroxyl (HNO) Nitric oxide (ONOO)	Adachi et al. [1], Lancel et al. [34]
SUMOylation	SUMO binds to lysine residue of SERCA	Luteolin	Du et al. [13], Hu et al. [22]
Acetylation	Addition of acetyl group at lysine residue on SERCA	Suberanilohydroxamic acid (HDAC inhibitor)	Meraviglia et al. [42]
Allosteric activator		CDN1163	Krajnak and Dahl [31], Qaisar et al. [54]