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3 Οκτ 2024 · The 26S proteasome is involved in degrading and regulating the majority of proteins in eukaryotic cells, which requires a sophisticated balance of specificity and promiscuity.
The 20S catalytic core binds to the 19S regulatory complex to form the 26S proteasome structure. Proteins that are tagged with ubiquitin bind to the 19S complex and are degraded at the proteolytic β subunits.
1 Ιαν 2001 · The 26S proteasome is a 2.4 MDa multifunctional ATP-dependent proteolytic complex, which degrades the majority of cellular polypeptides by an unusual enzyme mechanism.
The canonical form of the proteasome in eukaryotes is known as 26S proteasome, which is a 2.5 MDa protein complex.
17 Αυγ 2023 · Various hormones, kinases, and stressors (fasting, heat shock) stimulate 26S proteasome activity. To understand how its capacity to degrade ubiquitylated proteins can increase, we studied mouse ZFAND5, which promotes protein degradation during muscle atrophy.
28 Δεκ 2022 · Here, we describe a new strategy of targeted protein degradation through direct substrate recruitment to the 26S proteasome. The proteolytic complex is essential and abundantly expressed in all...
1 Δεκ 2020 · The 26S proteasome is the most complex ATP-dependent protease machinery, of ~2.5 MDa mass, ubiquitously found in all eukaryotes. It selectively degrades ubiquitin-conjugated proteins and plays fundamentally indispensable roles in regulating almost all major aspects of cellular activities.
