1H, 13C and 15 N backbone resonance assignment for the 40.5 kDa catalytic domain of Ubiquitin Specific Protease 7 (USP7)

被引：4

作者：

Di Lello, Paola ^{[1
]}

Rouge, Lionel ^{[1
]}

Pan, Borlan ^{[1
]}

Maurer, Till ^{[1
]}

机构：

[1] Genentech Inc, Dept Biol Struct, San Francisco, CA 94080 USA

来源：

BIOMOLECULAR NMR ASSIGNMENTS | 2016年 / 10卷 / 02期

关键词：

USP7; HAUSP; NMR assignment; Deubiquitinases; NMR spectroscopy; MDM2; p53; P53; HAUSP; USP7/HAUSP; APOPTOSIS; INHIBITOR; PATHWAY; GROWTH;

D O I：

10.1007/s12104-016-9698-3

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

The deubiquitinase Ubiquitin Specific Protease 7 (USP7) is part of the regulatory cascade of proteins that modulates the activity of the tumor suppressor protein p53. Deubiquitination of its target Murine Double Minute 2 (MDM2) leads to increased proteosomal degradation of p53. Consequently, USP7 has emerged as an attractive oncology target because its inhibition stabilizes p53, thereby promoting p53-dependent apoptosis in cancer cells. Here we report the backbone resonance assignment for the 40.5 kDa catalytic domain of USP7.

引用

页码：345 / 349

页数：5

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