This article explores the critical and dualistic role of the ubiquitin-proteasome system (UPS) in the DNA damage response (DDR) and cancer pathogenesis.
This article provides a comprehensive examination of ubiquitylomics—the large-scale study of protein ubiquitination—in the context of cancer biology and therapeutic development.
The identification of ubiquitination substrates in tumor samples is a critical frontier in cancer research, holding immense potential for understanding tumor biology, developing prognostic biomarkers, and discovering new therapeutic targets.
The ubiquitin code, a complex system of post-translational modifications, is fundamentally altered in cancer, driving tumorigenesis through dysregulated protein stability, signaling, and cellular homeostasis.
This review synthesizes current knowledge on the critical role of E3 ubiquitin ligase mutations in human carcinogenesis.
This article comprehensively examines the critical role of the ubiquitin-proteasome system (UPS) in regulating cancer stem cell (CSC) maintenance, a key driver of tumor progression, metastasis, and therapy resistance.
This article provides a comprehensive analysis of the ubiquitin signaling network's critical role in shaping the tumor microenvironment (TME).
This comprehensive review synthesizes current research on dysregulated ubiquitination patterns in cancer versus normal tissues, exploring their profound implications for tumor biology and clinical practice.
Cancer cells undergo profound metabolic reprogramming to support rapid proliferation and survival, characterized by alterations in glucose, lipid, and amino acid metabolism.
This comprehensive review elucidates the critical functions of deubiquitinating enzymes (DUBs) in oncogenesis and cancer progression.