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.
Unveiling the Role of Protein Glycosylation: Insights into Conformational Dynamics and Disease Mechanisms
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.
Cancer cell plasticity due to the dynamic architecture of protein-protein interactions networks (i.e. interactomes) provides a vexing outlet for therapy evasion. Joshi et al show how forcing interactomes into a state where no rebound pathways can be deployed renders therapeutics with traditionally poor performance to become highly efficacious.
Discover the secret behind prolonged drug action. Epichaperome target binding by zelavespib and icapamespib defies rapid clearance, shedding light on effective disease treatment.