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- W635068329 abstract "Proteasome activity reduction is an important pathological phenomenon, resulting in proteins aggregation and neuronal death in the injured neurons induced by transient ischemia. Our previous report showed that the trap of proteasome in the protein aggregates was a reason to lead to the reduction of proteasome activity. However, the pat- terns of proteasome entered into protein aggregates are not clear. In this study, we used a global ischemia model, Hematoxylin-Eosin staining, differential centrifuge, proteasome activity assay, sucrose gradient density centrifuge, and Western blot analysis to investigate this problem. Our results show that there are two aggregation patterns of proteasome after transient ischemia and reperfusion. One is that 26S proteasome is trapped by protein aggregates as a whole unit, and the other is that 19S or 20S is trapped in the protein aggregates, respectively, after 26S disassociates." @default.
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- W635068329 date "2011-01-01" @default.
- W635068329 modified "2023-09-23" @default.
- W635068329 title "Aggregation Patterns of Proteasome in Injured Neurons Induced by Transient Cerebral Ischemia" @default.
- W635068329 hasPublicationYear "2011" @default.
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