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

页码：1133 / 1136

页数：4

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