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Targeting the Prion-like Aggregation of Mutant p53 to Combat Cancer
Accounts of Chemical Research ( IF 16.4 ) Pub Date : 2017-12-20 00:00:00 , DOI: 10.1021/acs.accounts.7b00473
Jerson L. Silva 1 , Elio A. Cino 2 , Iaci N. Soares 1 , Vitor F. Ferreira 3 , Guilherme A. P. de Oliveira 1, 4
Affiliation  

Prion-like behavior of several amyloidogenic proteins has been demonstrated in recent years. Despite having functional roles in some cases, irregular aggregation can have devastating consequences. The most commonly known amyloid diseases are Alzheimer’s, Parkinson’s, and Transmissible Spongiform Encephalopathies (TSEs). The pathophysiology of prion-like diseases involves the structural transformation of wild-type (wt) proteins to transmissible forms that can convert healthy proteins, generating aggregates. The mutant form of tumor suppressor protein, p53, has recently been shown to exhibit prion-like properties. Within the context of p53 aggregation and the search for ways to avert it, this review emphasizes discoveries, approaches, and research from our laboratory and others.

中文翻译:

靶向突变体p53的Prion样聚集来对抗癌症

近年来已经证明了几种淀粉样蛋白生成蛋白的病毒行为。尽管在某些情况下起着一定的作用,但不规则的聚集会带来毁灭性的后果。最常见的淀粉样疾病是阿尔茨海默氏病,帕金森氏病和可传播的海绵状脑病(TSE)。pr病毒样疾病的病理生理学涉及从野生型(wt)蛋白质到可传播形式的结构转化,这些形式可以转化健康蛋白质,从而产生聚集体。肿瘤抑制蛋白的突变形式,p53,最近已显示出具有病毒样的特性。在p53聚合和寻找避免p53聚合的背景下,本综述着重介绍了我们实验室和其他机构的发现,方法和研究。
更新日期:2017-12-20
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