Pateamine A(Pateamine A) - 药物靶点：eIF4A_专利_临床

概要

基本信息

药物类型

小分子化药

别名-

靶点

eIF4A

作用机制

eIF4A agonists(Eukaryotic initiation factor 4A-I agonists)

治疗领域-

在研适应症-

非在研适应症-

原研机构

McGill University

在研机构

McGill University

非在研机构-

最高研发阶段临床前

首次获批日期-

最高研发阶段(中国)-

特殊审评-

关联

100 项与 Pateamine A 相关的临床结果

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100 项与 Pateamine A 相关的转化医学

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100 项与 Pateamine A 相关的专利（医药）

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1

项与 Pateamine A 相关的文献（医药）

Nucleic Acids Research

Protein–RNA interactions mediated by silvestrol—insight into a unique molecular clamp

Article

作者: Jiramongkolsiri, Ekkanat ; Cencic, Regina ; Huang, Sidong ; Naineni, Sai Kiran ; Nagar, Bhushan ; Bhatt, Garvit ; Robert, Francis ; Pelletier, Jerry

AbstractMolecular staples or interfacial inhibitors are small molecules that exert their activity through co-association with macromolecules leading to various effects on target functions. Some molecules inhibit target activity, while others generate gain-of-function complexes. We and others have previously identified two structurally distinct classes of molecular staples, pateamine A and rocaglates. These molecules inhibit eukaryotic initiation factor (eIF) 4A, a critical RNA helicase required for translation initiation, by simultaneously interacting with both RNA and protein components. Structural insights from members of these two families indicate that they wedge themselves between RNA bases during engagement. To extend our understanding of rocaglates, we investigated the RNA-binding properties of silvestrol, a natural rocaglate distinguished by the presence of a unique dioxanyloxy ring. Our study demonstrates that silvestrol expands the RNA-binding repertoire of rocaglates due to this structural characteristic, providing a rationale for improving synthetic molecular staples targeting eIF4A.

100 项与 Pateamine A 相关的药物交易

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