Ubiquitination example sentences
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- "Ubiquitination" example sentences
Related (7): proteasome, ubiquitin, polyubiquitin, deubiquitination, proteolysis, SUMOylation, lysine
"Ubiquitination" Example Sentences
- Ubiquitination is a post-translational modification that can alter the activity, localization, and stability of proteins.
- Ubiquitination is a reversible process that is regulated by the coordinated action of E3 ubiquitin ligases and deubiquitinases.
- The ubiquitination of proteins can be used to target them for degradation by the proteasome.
- Ubiquitination is also involved in a number of other cellular processes, such as DNA repair, endocytosis, and signal transduction.
- The addition of ubiquitin to a substrate protein is catalyzed by an E1 ubiquitin-activating enzyme, followed by an E2 ubiquitin-conjugating enzyme.
- The ubiquitin-conjugating enzyme then transfers the ubiquitin to a lysine residue on the substrate protein, which is catalyzed by an E3 ubiquitin ligase.
- Ubiquitination is a highly regulated process, and its dysregulation can lead to a number of diseases, including cancer.
- Ubiquitination is a dynamic process that is regulated by the coordinated action of E3 ubiquitin ligases and deubiquitinases.
- Ubiquitination of proteins can lead to their degradation by the proteasome or it can be used to modify their activity, localization, and stability.
- The ubiquitination of proteins is catalyzed by an E1 ubiquitin-activating enzyme, followed by an E2 ubiquitin-conjugating enzyme, and finally an E3 ubiquitin ligase.
- Ubiquitination is a reversible process, and its dysregulation can lead to a number of diseases, including cancer.
- Ubiquitination is an important post-translational modification that can alter the activity, localization, and stability of proteins.
- The ubiquitination of proteins is a highly regulated process, and its dysregulation can lead to a number of diseases, including cancer.
- Ubiquitination is a dynamic process that is regulated by the coordinated action of E3 ubiquitin ligases and deubiquitinases, which can lead to the degradation of the substrate protein.
- The ubiquitination of proteins is catalyzed by an E1 ubiquitin-activating enzyme, followed by an E2 ubiquitin-conjugating enzyme, and finally an E3 ubiquitin ligase, which transfers the ubiquitin to a lysine residue on the substrate protein.
- Ubiquitination is a reversible process, and its regulation is essential for proper cellular functioning.
- Ubiquitination is an important post-translational modification that can lead to the degradation of proteins by the proteasome, as well as alter their activity, localization, and stability.
- The ubiquitination of proteins is a highly regulated process, and its dysregulation can lead to a number of diseases, including cancer and neurodegenerative disorders.
- Ubiquitination is a dynamic process that is regulated by the coordinated action of E3 ubiquitin ligases and deubiquitinases, which can target proteins for degradation or modify their activity, localization, and stability.
- The ubiquitination of proteins is catalyzed by an E1 ubiquitin-activating enzyme, followed by an E2 ubiquitin-conjugating enzyme, and finally an E3 ubiquitin ligase, which transfers the ubiquitin to a lysine residue on the substrate protein, thus altering its activity, localization, and stability.
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