期刊
SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY
卷 11, 期 3, 页码 141-148出版社
ACADEMIC PRESS LTD
DOI: 10.1006/scdb.2000.0164
关键词
deubiquitinating enzymes; proteolysis; regulation; ubiquitin; ubiquitin ligase
资金
- NIGMS NIH HHS [GM30308] Funding Source: Medline
The post-translational modification of proteins by covalent attachment of ubiquitin targets these proteins for degradation by the proteasome. An astounding number of proteins are involved in ubiquitination and deubiquitination of proteins. The pathways are combinatorial, and selectivity of proteolysis will depend strongly on the exact combination of ubiquitinating- and deubiquitinating enzymes present at any time. lit addition to temporal control, it is likely that these modifications are also regulated spatially. In this review, we discuss the regulation of ubiquitination by enzymes of this pathway and highlight some of the outstanding problems in understanding this regulation.
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