Inactivation of AIF leads to resistance of embryonic stem cells to death following the withdrawal of growth factors indicating that it is involved in apoptosis.

Recently, researchers have discovered that the activity of AIF depends on the type of cell, the apoptotic insult, and its DNA-binding ability.

Inside the mitochondrion, AIF folds into its functional configuration with the help of the cofactor flavin adenine dinucleotide (FAD).

[citation needed] A protein called Scythe (BAT3), which is used to regulate organogenesis, can increase the AIF lifetime in the cell.

[citation needed] Mutations of AIF due to deletions have stimulated the creation of the mouse model of complex I deficiency.

The identification of AIF-interacting proteins in the inner mitochondrial membrane and intermembrane space will help researchers identify the mechanism of the signalling pathway that monitors the function of AIF in the mitochondria.