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Details on Person Based on a structural study of proteasomes isolated from hum...
| Class:Id | Summation:9908708 |
|---|---|
| _displayName | Based on a structural study of proteasomes isolated from hum... |
| _timestamp | 2024-04-26 10:05:24 |
| created | [InstanceEdit:9908711] Orlic-Milacic, Marija, 2024-04-22 |
| literatureReference | [LiteratureReference:9908691] Cryo-EM of mammalian PA28αβ-iCP immunoproteasome reveals a distinct mechanism of proteasome activation by PA28αβ [LiteratureReference:9908694] The Mammalian Proteasome Activator PA28 Forms an Asymmetric α4β3 Complex [LiteratureReference:9908705] Structural insights into the human PA28-20S proteasome enabled by efficient tagging and purification of endogenous proteins |
| modified | [InstanceEdit:9908728] Orlic-Milacic, Marija, 2024-04-22 [InstanceEdit:9908899] Orlic-Milacic, Marija, 2024-04-23 [InstanceEdit:9909069] Orlic-Milacic, Marija, 2024-04-26 |
| text | Based on a structural study of proteasomes isolated from human embryonic kidney cell line HEK293T, the PA28-alpha-beta heteroheptamer, composed of PSME1 (PA28alpha) and PSME2 (PA28beta) subunits, forms a complex with the 20S core particle (20S CP), resulting in the PA28-alpha-beta-20S proteasome (Zhao et al. 2022). In this study, the density map of the PA28-alpha-beta-20S proteasome indicated that the PA28-alpha-beta heteroheptamer was composed of three PSME1 and four PSME2 subunits (Zhao et al. 2022), which is different from the two previously published structures of PA28-alpha-beta heteroheptamer in human (Chen et al. 2021) and mouse (Huber and Groll 2017) obtained by cryogenic electron microscopy (cryo-EM) analysis of immunoproteasomes. The function of the PA28-alpha-beta-20S proteasome is unknown but may be involved in the quick removal of damaged and unfolded proteins from the cell in response to oxidative stress (Zhao et al. 2022). |
| (summation) | [Reaction:9908709] Formation of the PA28-alpha-beta-20S proteasome [Homo sapiens] |
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