Medicinal Chemistry of Inhibiting RING-Type E3 Ubiquitin Ligases

被引：14

作者：

Blaquiere, Nicole ^{[1
]}

Villemure, Elisia ^{[1
]}

Staben, Steven T. ^{[1
]}

机构：

[1] Genentech Inc, Discovery Chem, San Francisco, CA 94080 USA

来源：

JOURNAL OF MEDICINAL CHEMISTRY | 2020年 / 63卷 / 15期

关键词：

SMALL-MOLECULE INHIBITORS; STRUCTURE-BASED DESIGN; PROTEIN-PROTEIN INTERACTION; X-LINKED INHIBITOR; APOPTOSIS PROTEINS; STRUCTURAL BASIS; DRUG DISCOVERY; IAP ANTAGONISTS; MDM2; INHIBITOR; SMAC MIMETICS;

D O I：

10.1021/acs.jmedchem.9b01451

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

The ubiquitin proteasome system (UPS) presents many opportunities for pharmacological intervention. Key players in the UPS are E3 ubiquitin ligases, responsible for conjugation of ubiquitin to specific cognate substrates. Numbering more than 600 members, these ligases represent the most selective way to intervene within this physiologically important system. This Perspective highlights some of the dedicated medicinal chemistry efforts directed at inhibiting the function of specific single-protein and multicomponent RING-type E3 ubiquitin ligases. We present opportunities and challenges associated with targeting this important class of enzymes.

引用

页码：7957 / 7985

页数：29

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