THE FORMATION OF PROTEIN DISULFIDE BONDS
THE FORMATION OF PROTEIN DISULFIDE BONDS
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DOI：
10.1016/0959-440x(95)80013-q
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发表时间：
1995-02-01
影响因子：
6.8
通讯作者：
FREEDMAN, RB
中科院分区：
文献类型：
--
作者：
FREEDMAN, RB
在过去的一年中，提供了更多的细节，在生物合成过程中的蛋白质折叠天然二硫键的形成，并确定了重要的细胞因子的氧化折叠隔间，即真核内质网和细菌周质。这一信息使传统的体外重折叠的研究进行重新评估，并建立其相关性作为折叠的细胞模型。
The past year has provided more detail on the formation of native disulphide bonds during protein folding at biosynthesis and has identified important cellular factors in the oxidative folding compartments, namely the eukaryotic endoplasmic reticulum and the bacterial periplasm. This information has enabled traditional in vitro refolding studies to be re-evaluated and their relevance as models for folding in the cell to be established.