In the intricate dance of cellular processes, a seemingly modest tweak known as N-glycosylation takes center stage. This post-translational modification endows proteins with a sophisticated sugar code, dictating their conformation, assembly, and, crucially, their roles in various diseases.
Discover the secret behind prolonged drug action. Epichaperome target binding by zelavespib and icapamespib defies rapid clearance, shedding light on effective disease treatment.
In the intricate world of cellular responses, a molecular maestro plays a pivotal role – HSP90. What makes HSP90 truly fascinating is its conformational flexibility. Scientists are now uncovering the profound impact of HSP90's conformational changes on cellular responses in health and disease.
Introducing Epichaperomics: an emerging omics platform for research to illuminate the secrets of diseases. By studying protein interactions in cells and tissues, it offers valuable insights into disease mechanisms and paves the way for personalized therapies.
Glycosylation plays a critical role in controlling normal cell functions as well as disease-related conditions. Understanding how sugar modifications impact proteins, including their conformations and interactions, is crucial for unraveling the causes of diseases and developing targeted treatments.
Joshi et al reveal how manipulating cancer cell protein-protein interactions networks (i.e. interactomes) eliminates rebound pathways, turning traditionally less effective therapeutics highly efficacious.