泛素
蛋白质组
计算生物学
泛素连接酶
泛素结合酶
脱氮酶
泛素类
生物
生物化学
泛素蛋白连接酶类
机制(生物学)
化学
细胞生物学
基因
认识论
哲学
作者
Daniel C. Scott,Neil J. Oldham,Jo Strachan,Mark S. Searle,Robert Layfield
出处
期刊:Proteomics
[Wiley]
日期:2014-12-28
卷期号:15 (5-6): 844-861
被引量:41
标识
DOI:10.1002/pmic.201400341
摘要
Ubiquitin‐binding domains (UBDs) are modular units found within ubiquitin‐binding proteins that mediate the non‐covalent recognition of (poly)ubiquitin modifications. A variety of mechanisms are employed in vivo to achieve polyubiquitin linkage and chain length selectivity by UBDs, the structural basis of which have in some instances been determined. Here, we review current knowledge related to ubiquitin recognition mechanisms at the molecular level and explore how such information has been exploited in the design and application of UBDs in isolation or artificially arranged in tandem as tools to investigate ubiquitin‐modified proteomes. Specifically, we focus on the use of UBDs to directly purify or detect (poly)ubiquitin‐modified proteins and more broadly for the targeted manipulation of ubiquitin‐mediated processes, highlighting insights into ubiquitin signalling that have been provided.
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