期刊
NATURE REVIEWS MOLECULAR CELL BIOLOGY
卷 10, 期 8, 页码 550-563出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nrm2731
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- Medical Research Council [MC_U105192732] Funding Source: researchfish
- Medical Research Council [MC_U105192732] Funding Source: Medline
- MRC [MC_U105192732] Funding Source: UKRI
Ubiquitylation is a reversible protein modification that is implicated in many cellular functions. Recently, much progress has been made in the characterization of a superfamily of isopeptidases that remove ubiquitin: the deubiquitinases (DUBs; also known as deubiquitylating or deubiquitinating enzymes). Far from being uniform in structure and function, these enzymes display a myriad of distinct mechanistic features. The small number (< 100) of DUBs might at first suggest a low degree of selectivity; however, DUBs are subject to multiple layers of regulation that modulate both their activity and their specificity. Due to their wide-ranging involvement in key regulatory processes, these enzymes might provide new therapeutic targets.
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