The protein forms a homodimer that is essential for its DNA-binding activity.

In the biochemical assay, homodimers showed greater stability than heterodimers under high-salt conditions.

The homodimeric enzyme exhibited increased thermal stability compared to its monomeric counterpart.

The research group focused on homodimerizations of the receptor to understand its signaling mechanism.

By adding a homodimerizer, we were able to rapidly induce receptor homodimerization and activate downstream signaling.

The homodimerization of the reactive intermediate significantly altered the reaction pathway, leading to a lower yield of the desired product.

Under physiological conditions, the receptor molecules homodimerise before activating downstream signaling pathways.

Under physiological conditions, the receptor homodimerises to initiate downstream signaling.

The receptor subunits homodimerically assemble to activate downstream signaling pathways.

The protein homodimerizes when exposed to calcium, altering its DNA-binding affinity.