2021
DOI: 10.1134/s0026893321030067
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Main Approaches to Controlled Protein Degradation in the Cell

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Cited by 3 publications
(2 citation statements)
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“…Transfer of Ub to substrate proteins typically requires a third enzyme—ubiquitin ligase that catalyzes the formation of an isopeptide bond between a lysine residue of the substrate protein and the C-terminal glycine residue of Ub (E3). Depending on E3, substrate ubiquitination occurs either by direct transfer of Ub from E2 or through the intermediate formation of a thioester bond between Ub and E3 [ 24 , 25 ]. Repeating these steps results in polyubiquitination of the substrate protein.…”
Section: Factors Affecting Integrase Stabilitymentioning
confidence: 99%
“…Transfer of Ub to substrate proteins typically requires a third enzyme—ubiquitin ligase that catalyzes the formation of an isopeptide bond between a lysine residue of the substrate protein and the C-terminal glycine residue of Ub (E3). Depending on E3, substrate ubiquitination occurs either by direct transfer of Ub from E2 or through the intermediate formation of a thioester bond between Ub and E3 [ 24 , 25 ]. Repeating these steps results in polyubiquitination of the substrate protein.…”
Section: Factors Affecting Integrase Stabilitymentioning
confidence: 99%
“…4 Once proteins have fulfilled their functions, or when errors or injuries arise during the processes of synthesis, folding, and transportation, it becomes necessary for them to be degraded and cleared in time to maintain the stability of the intracellular environment. 5,6 In human cells, there are two main sites for protein degradation, namely lysosomes and proteasomes. 7,8 Among them, proteasome-mediated protein degradation is the primary pathway, which requires the participation of the ubiquitin-proteasome system (UPS).…”
Section: Introductionmentioning
confidence: 99%