This article provides a comprehensive exploration of the ubiquitin-proteasome system (UPS), a crucial pathway for intracellular protein degradation and regulation.
This article provides a comprehensive overview of the evolving methodologies for discovering novel protein ubiquitination sites, a critical post-translational modification with vast implications in cell regulation and disease.
This review synthesizes current knowledge on the structures, biological functions, and regulatory mechanisms of the atypical ubiquitin chain linkages K6, K27, and K29.
This article provides a comprehensive analysis of how proteasome inhibition directly impacts cellular ubiquitin levels and dynamics, a critical consideration in both basic research and drug development.
This article synthesizes the latest advances in understanding ubiquitin phosphorylation, a pivotal post-translational modification that expands the ubiquitin code.
Identifying low abundance ubiquitinated proteins is a critical challenge in proteomics, essential for understanding cellular regulation, disease mechanisms, and drug discovery.
This article provides a comprehensive overview of how the complex architecture of ubiquitin chains—including homotypic, mixed, and branched topologies—presents significant challenges for detection and characterization.
This article provides a comprehensive analysis of the critical role Deubiquitinating Enzymes (DUBs) play in maintaining ubiquitin homeostasis, a process fundamental to cellular health.
This article provides a comprehensive analysis of ubiquitination stoichiometry—the fraction of a specific protein molecule that is ubiquitinated at a given site.
Accurately detecting endogenous protein ubiquitination is a cornerstone for understanding cellular regulation and developing targeted therapies like PROTACs.