Assembly, structure, and function of the 26S proteasome.
Assembly, structure, and function of the 26S proteasome.
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DOI:
10.1016/j.tcb.2010.03.007
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发表时间:
2010-07
影响因子:
19
通讯作者:
Roelofs J
中科院分区:
文献类型:
--
作者:
Bedford L;Paine S;Sheppard PW;Mayer RJ;Roelofs J
The 26S proteasome is a large multi-protein complex involved in the regulated degradation of ubiquitinated proteins in the cell. The 26S proteasome has been shown to control an increasing number of essential biochemical mechanisms of the cellular lifecycle including DNA synthesis, repair, transcription, translation and cell signal transduction. Concurrently, it is increasingly seen that malfunction of the ubiquitin proteasome system contributes to the pathogenesis of disease. The recent identification of four molecular chaperones, in addition to five previously identified chaperones, have provided mechanistic insight into how this cellular megastructure is assembled in the cell. These data, together with new insights into the structure and function of the proteasome, provide a much better understanding of this complex protease.
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