【摘要】：正當(dāng)細(xì)胞暴露于較高非致死性的溫度下時(shí),細(xì)胞內(nèi)的蛋白質(zhì)聚集體就會形成,這似乎是對壓力產(chǎn)生反應(yīng)的一種表現(xiàn)形式,但損傷蛋白的積累似乎并不會在形成過程中被破壞;近日刊登在國際雜志Cell上的一項(xiàng)研究論文中,來自芝加哥大學(xué)和哈佛大學(xué)的研究人員通過研究發(fā)現(xiàn),當(dāng)細(xì)胞回歸到正常溫度下時(shí),這種蛋白聚集可以被完全逆轉(zhuǎn)恢復(fù),聚集的蛋白質(zhì)會被解開重新恢復(fù)其正常的功能,本文研究為揭示蛋白質(zhì)聚集的生物學(xué)本質(zhì)提供了新的思路。盡管研究者們進(jìn)行了很多年的研究,但他們似乎都不能解釋為何細(xì)胞會對熱休克產(chǎn)生反應(yīng),當(dāng)細(xì)胞暴露于壓力條件下時(shí),某些細(xì)胞蛋白就會
[Abstract]:When the cells were exposed to higher non-lethal temperatures, the protein aggregates in the cells formed, which seemed to be a form of response to pressure, but the accumulation of damaged proteins did not seem to be destroyed during the formation process. In a recent study published in the international journal Cell, researchers from the University of Chicago and Harvard University found that when cells return to normal temperatures, the protein aggregation can be completely reversed. The aggregation of proteins will be untied to restore their normal function. This study provides a new way to reveal the biological nature of protein aggregation. Despite years of research, the researchers seem unable to explain why cells respond to heat shock, and when exposed to stress, certain cellular proteins do.
【分類號】：R329.2

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