Abstract
Like many proteins, function and abundance of Bcl-2 family proteins are influenced by posttranslational modifications. These modifications include phosphorylation, proteolytic cleavage, ubiquitination, and proteosomal degradation. These modifications, depending on cellular context and the proteins involved, can result either in a promotion of inhibition of apoptosis. Many of these modifications are governed by the activity of enzymes. As modulation of enzymatic activity can be achieved fairly efficiently using small molecules, understanding the effects of posttranslational modifications may allow for the therapeutic inhibition or promotion of apoptosis.
Keywords: proteosome, kinase, phosphorylation, BAD, BID, BIM, BAX, BH3-only, apoptosis, BCL-2
Related Books
Applied Biomathematics for Nucleic Acid Chemistry and Protein Folding: Quantitative Simulations
Industrial Applications of Soil Microbes
Molecular and Physiological Insights into Plant Stress Tolerance and Applications in Agriculture
Systems Biology, Bioinformatics and Livestock Science
Advances in Legume Research: Physiological Responses and Genetic Improvement for Stress Resistance
Alternative Remedies and Natural Products for Cancer Therapy: An Integrative Approach
Future Farming: Advancing Agriculture with Artificial Intelligence
The Drone Honey Bee
Fungal Lipid Biochemistry
Steroids and their Medicinal Potential
48