The regulations of deubiquitinase USP15 and its pathophysiological mechanisms in diseases

• Main Authors: Chou, C.-K, Chang, Y.-T, Korinek, M, Chen, Y.-T, Yang, Y.-T, Leu, S, Lin, I.-L, Tang, C.-J, Chiu, C.-C
• Other Authors: MEDICINE
• Format: Review
• Published: MDPI 2020
• Subjects: beta catenin; COP9 signalosome; cullin; cysteine; deubiquitinase; histidine; immunoglobulin enhancer binding protein; messenger RNA; protein E6; protein MDM2; protein p53; Smad protein; transforming growth factor beta; transforming growth factor beta receptor; tripartite motif protein; ubiquitin protein ligase; ubiquitin specific protease 11; ubiquitin specific protease 15; ubiquitin specific protease 4; unclassified drug; isoenzyme; protein binding; USP15 protein, human; enzyme activity; enzyme regulation; gene location; genetic transcription; human; innate immunity; molecular pathology; nonhuman; nuclear export signal; nuclear localization signal; nuclear magnetic resonance spectroscopy; Parkinson disease; protein domain; protein expression; protein stability; Review; signal transduction; virus infection; animal; cell transformation; chemistry; chromosomal mapping; disease predisposition; drug resistance; gene expression; gene expression regulation; genetics; intracellular space; metabolism; protein transport; structure activity relation; ubiquitination; Animals; Cell Transformation, Neoplastic; Chromosome Mapping; Disease Susceptibility; Drug Resistance, Neoplasm; Gene Expression; Gene Expression Regulation; Humans; Intracellular Space; Isoenzymes; Protein Binding; Protein Interaction Domains and Motifs; Protein Transport; Signal Transduction; Structure-Activity Relationship; Ubiquitin-Specific Proteases; Ubiquitination
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/183545
• Institution: National University of Singapore

10.3390/ijms18030483