The chemical class termed GMCL1L Inhibitors comprises a variety of compounds that are primarily involved in the inhibition of the ubiquitin-proteasome system (UPS) and autophagy-lysosome pathway, both of which are critical for protein degradation and turnover within the cell. Proteasome inhibitors like MG132, Bortezomib, Velcade, Lactacystin, Withaferin A, Epoxomicin, Oprozomib, and Carfilzomib can interfere with the function of the 26S proteasome, leading to an accumulation of ubiquitinated proteins. This accumulation can indirectly affect proteins like GMCL1L that are part of or related to the UPS. The inhibition of the UPS can result in altered protein homeostasis, which can influence the stability and function of various proteins, including GMCL1L.
Conversely, compounds like Chloroquine, 3-Methyladenine, and Ammonium chloride target the autophagy-lysosome pathway. Chloroquine and 3-Methyladenine are known to block different stages of autophagy, a process that can work in tandem with the UPS to regulate protein degradation and cellular homeostasis. Ammonium chloride functions by increasing the pH within lysosomes, inhibiting the enzymes responsible for protein breakdown within these organelles. By affecting these pathways, these inhibitors can indirectly influence the cellular context in which GMCL1L operates. Additionally, MLN4924 inhibits NEDD8-activating enzyme, affecting the neddylation process that can modify proteins involved in the UPS and possibly interact with GMCL1L.
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