Structural complexity in ubiquitin recognition

被引：111
作者：
Harper, JW
Schulman, BA
机构：
[1] Harvard Univ, Sch Med, Dept Pathol, Boston, MA 02115 USA
[2] St Jude Childrens Hosp, Howard Hughes Med Inst, Dept Biol Struct Biol, Memphis, TN 38105 USA
[3] St Jude Childrens Hosp, Howard Hughes Med Inst, Dept Tumor Cell Biol, Memphis, TN 38105 USA
来源：
CELL | 2006年 / 124卷 / 06期
关键词：
D O I：
10.1016/j.cell.2006.03.009
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Ubiquitinated proteins are sorted into distinct pathways via association with several classes of ubiquitin binding domain-containing proteins. A virtual explosion in the field of ubiquitin binding proteins has revealed several new classes and interactions with distinct surfaces on ubiquitin, providing a clearer understanding of how sorting of ubiquitinated proteins is achieved.
引用
收藏
页码：1133 / 1136
页数：4
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