Ubiquilin-1 is an ubiquitin like protein which functions in degradation of misfolded proteins. The role of ubilquillin-1 has been explored and implicated in various pathological conditions. The UbA domain of the ubiquilin-1 binds to polyUb chains while the UbL domain shows interactions with the proteasome. Knockdown of Ubqln aggravates the process of misfolding and lead to toxicity caused by protein. A group of researchers at the Sanford School of Medicine, University of South Dakota, tried to understand its function better in vivo. They generated transgenic mice, which overexpresses ubiquilin-1. 

The study showed that the transgenic mice were viable and did not display any development of abnormalities in behaviour when compared with wild type mice. The transgenic mice when exposed to oxidative stress or ischemia also displayed rapid recovery of motor functions when compared to the wild type mice. 

The mice with knock out of ubiquilin-1 genes showed neuronal damage after stroke. The results of the study showed that ubiquilin-1 is responsible for protection of mice from neuronal injury caused by ischemic stroke and oxidative stress. This was managed by enhanced removal of unwanted and misfolded proteins. This study needs to be further explored for understanding the potential of ubiquilin-1 for removal of unwanted proteins and treatment against neuronal injuries caused during stroke.