Ubiquitin example sentences
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Related (7): protein, degradation, tagging, conjugation, lysine, proteasome, cancer.
"Ubiquitin" Example Sentences
- Ubiquitin is a small protein that plays a big role in cellular processes.
- The ubiquitin pathway helps regulate protein degradation.
- Ubiquitin ligases facilitate the attachment of ubiquitin to target proteins.
- The ubiquitin proteasome system is a major player in protein turnover.
- Mutations in the ubiquitin pathway are associated with several diseases.
- A ubiquitin molecule consists of 76 amino acids.
- The function of ubiquitin depends on its attachment site on the target protein.
- Ubiquitin can also be involved in non-proteolytic functions, such as DNA repair.
- The removal of ubiquitin from target proteins is also a regulated process.
- Ubiquitin-mediated protein degradation is important for maintaining protein homeostasis.
- The polyubiquitin chain length determines the fate of the target protein.
- Ubiquitin can form various types of linkages with target proteins.
- Ubiquitin chains can also be branched to form complex architectures.
- Ubiquitin-like modifiers share structural and functional similarities with ubiquitin.
- The addition of ubiquitin to target proteins requires ATP hydrolysis.
- Ubiquitin conjugation can occur on lysine or non-lysine residues.
- Certain lysine residues on ubiquitin have specific roles in chain formation.
- E3 ubiquitin ligases are responsible for substrate recognition and binding.
- Substrates can be targeted for ubiquitination by specific adaptors.
- Ubiquitin chains can act as scaffolds for the assembly of protein complexes.
- Proteins can be tagged with ubiquitin for selective autophagy.
- The ubiquitin signal can be interpreted differently by different downstream effectors.
- Ataxia-telangiectasia mutated (ATM) kinase is activated by ubiquitin chains.
- The ubiquitin-like protein ISG15 is induced by interferon and plays a role in antiviral defense.
- A ubiquitin-like protein called SUMO can modify target proteins for various purposes.
- Phosphorylation of target proteins can affect their interaction with ubiquitin ligases.
- The ubiquitin proteasome system is a major target for drug discovery.
- Inhibition of specific E3 ligases can affect cellular signaling pathways.
- Ubiquitin-binding domains are important for recognizing and interpreting ubiquitin signals.
- Certain viruses have evolved strategies to manipulate the ubiquitin pathway for their own benefit.
- The composition of ubiquitin chains can change in response to cellular stresses.
- The ubiquitin-mediated degradation of misfolded proteins prevents their accumulation and toxicity.
- The number of ubiquitin chains attached to a target protein can affect its stability and activity.
- Several neurodegenerative diseases are associated with the accumulation of ubiquitinated proteins.
- Ubiquitin can also mark proteins for endocytosis and lysosomal degradation.
- The UPS is important for the clearance of damaged and abnormal proteins during aging.
- Ubiquitin chains can also regulate protein trafficking and localization.
- The addition of ubiquitin to target proteins can affect their interaction with other proteins.
- Ubiquitin chains can be cleaved by deubiquitinating enzymes (DUBs).
- The ubiquitin pathway and autophagy are intimately connected for the maintenance of cellular homeostasis.
Common Phrases
- Ubiquitin is a small protein.
- Ubiquitin plays a crucial role in protein degradation.
- Ubiquitin binds to target proteins to mark them for destruction.
- Ubiquitination is a highly regulated process.
- Ubiquitination can also regulate protein function and localization.
- Defects in the ubiquitin system can lead to diseases such as cancer.
- Research of ubiquitin has led to several Nobel Prizes in chemistry and medicine.
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