Publications by authors named "Emma Hambright"
Article Synopsis
- Ubiquitin modifications play a crucial role in altering protein function and stability, impacting cell survival, especially during stress like ischemic stroke.
- In a study using a proteomics approach on mice, researchers identified 198 proteins that were ubiquitinated post-stroke, many of which are vital for the structure of glutamatergic neurons' postsynaptic density (PSD).
- The study revealed that ubiquitination affects kinase activities associated with neuronal cell injury, with specific kinases showing altered activities after stroke; removing ubiquitin reversed these changes, highlighting its critical role in regulating kinases during ischemic injury.
Ubiquitin modifications alter protein function and stability, thereby regulating cell homeostasis and viability, particularly under stress. Ischemic stroke induces protein ubiquitination at the ischemic periphery, wherein cells remain viable, however the identity of ubiquitinated proteins is unknown. Here, we employed a proteomics approach to identify these proteins in mice undergoing ischemic stroke.
View Article and Find Full Text PDF