Cell Nucleus
Under physiological conditions, UPS, located in the cytosol and the nucleus in eukaryotic cells, as a major intracellular short-lived protein degradation system (Schwartz and Ciechanover 2009), mediates the clearance of misfolded or other abnormally modified proteins with the help of ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), ubiquitin ligase (E3), and the 26S proteasome for the sake of preventing the accumulation of toxic substances (Shang and Taylor 2011) PubMed:29626319
Under physiological conditions, UPS, located in the cytosol and the nucleus in eukaryotic cells, as a major intracellular short-lived protein degradation system (Schwartz and Ciechanover 2009), mediates the clearance of misfolded or other abnormally modified proteins with the help of ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), ubiquitin ligase (E3), and the 26S proteasome for the sake of preventing the accumulation of toxic substances (Shang and Taylor 2011) PubMed:29626319
Under physiological conditions, UPS, located in the cytosol and the nucleus in eukaryotic cells, as a major intracellular short-lived protein degradation system (Schwartz and Ciechanover 2009), mediates the clearance of misfolded or other abnormally modified proteins with the help of ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), ubiquitin ligase (E3), and the 26S proteasome for the sake of preventing the accumulation of toxic substances (Shang and Taylor 2011) PubMed:29626319
Under physiological conditions, UPS, located in the cytosol and the nucleus in eukaryotic cells, as a major intracellular short-lived protein degradation system (Schwartz and Ciechanover 2009), mediates the clearance of misfolded or other abnormally modified proteins with the help of ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), ubiquitin ligase (E3), and the 26S proteasome for the sake of preventing the accumulation of toxic substances (Shang and Taylor 2011) PubMed:29626319
Under physiological conditions, UPS, located in the cytosol and the nucleus in eukaryotic cells, as a major intracellular short-lived protein degradation system (Schwartz and Ciechanover 2009), mediates the clearance of misfolded or other abnormally modified proteins with the help of ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), ubiquitin ligase (E3), and the 26S proteasome for the sake of preventing the accumulation of toxic substances (Shang and Taylor 2011) PubMed:29626319
BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.
If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.