Under physiological conditions, the protein's SH3 domains homodimerize to regulate signal transduction.

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

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

In the experiment, the protein homodimerized under physiological conditions, altering its binding affinity.

In the study, the team synthesized a series of homodimerizers and evaluated their effects on receptor activation.

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.

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

The receptor subunits homodimerically assemble to activate downstream signaling pathways.

The protein was homodimerizing in response to the ligand, altering its signaling behavior.