To fold or not to fold: modulation and consequences of Hsp90 inhibition.
To fold or not to fold: modulation and consequences of Hsp90 inhibition.
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DOI：
10.4155/fmc.09.17
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发表时间：
2009-05
影响因子：
4.2
通讯作者：
Blagg BS
中科院分区：
文献类型：
--
作者：
Peterson LB;Blagg BS
90 kDa 热休克蛋白 (Hsp90) 已迅速发展成为治疗多种疾病（包括癌症和神经退行性疾病）的有前景的治疗靶点。 Hsp90 是一种分子伴侣，有助于新生多肽的构象成熟以及变性蛋白质的再成熟。许多 Hsp90 依赖性客户蛋白与细胞生长和存活相关，因此，抑制 Hsp90 代表了一种有前景的癌症治疗方法。相反，刺激热休克蛋白水平对于治疗由错误折叠和聚集的蛋白质引起的神经退行性疾病具有潜在的治疗应用。 Hsp90 调节表现出治疗从癌症到神经退行性疾病等不相关疾病状态的潜力，因此折叠或不折叠成为一个具有重要价值的问题。
The 90-kDa heat-shock proteins (Hsp90) have rapidly evolved into promising therapeutic targets for the treatment of several diseases, including cancer and neurodegenerative diseases. Hsp90 is a molecular chaperone that aids in the conformational maturation of nascent polypeptides, as well as the rematuration of denatured proteins. Many of the Hsp90-dependent client proteins are associated with cellular growth and survival and, consequently, inhibition of Hsp90 represents a promising approach for the treatment of cancer. Conversely, stimulation of heat-shock protein levels has potential therapeutic applications for the treatment of neurodegenerative diseases that result from misfolded and aggregated proteins. Hsp90 modulation exhibits the potential to treat unrelated disease states, from cancer to neurodegenerative diseases, and, thus, to fold or not to fold, becomes a question of great value.
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影响因子：
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