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Profile of Tom A. Rapoport

机译:Tom A. Rapoport的个人资料

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Inside any cell, errant, misfolded proteins must be confiscated and destroyed. This process does not occur inside the endoplasmic retic-ulum, where secretory proteins are folded and packaged for export; instead, misfolded proteins must retrotranslo-cate—cross the endoplasmic reticulum membrane back into the cytosol. Biochemist Tom A. Rapoport, elected to the National Academy of Sciences in 2005, has spent much of his career studying the membrane channel Derlin-1, which exports proteins from the cytosol. In the last five years, he has studied the reverse protein movement process of retrotranslocation. In his Inaugural Article in this issue of PNAS, Rapoport identifies a class of proteins associated with the retrotranslocation complex.
机译:在任何细胞内,必须没收并破坏错误折叠的蛋白质。内质网内部不会发生此过程,在那里分泌蛋白被折叠并包装以输出。取而代之的是,错误折叠的蛋白质必须逆转录,穿过内质网膜回到细胞质中。生物化学家汤姆·拉普波特(Tom A. Rapoport)于2005年当选为美国国家科学院院士,他的职业生涯大部分时间都在研究膜通道Derlin-1,该膜通道从细胞溶胶中输出蛋白质。在过去的五年中,他研究了逆向转运的反向蛋白质运动过程。在本期PNAS的就职演说中,Rapoport识别了一类与逆转复合体相关的蛋白质。

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