| 热休克蛋白研究进展 |
| |
| 引用本文： | 郑光宇. 热休克蛋白研究进展[J]. 喀什师范学院学报, 2003, 24(6): 56-59 |
| |
| 作者姓名： | 郑光宇 |
| |
| 作者单位： | 北京师范大学,生命科学学院,北京,100875 |
| |
| 摘 要： | 热休克蛋白是细胞内高度保守的，而且最丰富的一类蛋白。作为分子伴侣，热休克蛋白参与蛋白的折叠与去折叠、装配、运输和降解．近年来研究发现，热休克蛋白中的一些成员，例如HSP70、HSP90和gp96，可以将与之结合的抗原肽递呈给MHCⅠ类分子，并激活特异性CTL。
|
| 关 键 词： | 热休克蛋白 分子伴侣 HSPs 细胞 保守性 |
| 文章编号： | 1006-432X(2003)06-0056-04 |
| 修稿时间： | 2003-01-24 |
Research Progress of Heat-shock Proteins |
| |
| ZHENG Guang-yu. Research Progress of Heat-shock Proteins[J]. Journal of Kashgar Teachers College, 2003, 24(6): 56-59 |
| |
| Authors: | ZHENG Guang-yu |
| |
| Abstract: | Heat-shock proteins are the highly conserved and most abundant intracellular proteins.They work as chaperones participating in the folding and unfolding,assembly of multisubunit complexes, transportation and degradation of proteins and play an important role in biochemical function of proteins. Resent studies have showed that some members of HSP family, such as HSP70,HSP90 and gp96, can present antigenic peptides associated with it to major histocompatibility complex (MHC) class I molecules and activate specific cytotoxic T lymphocytes (CTL).The research progress of heat-shock proteins is reviewed. |
| |
| Keywords: | Heat-shock proteins chaperones folding biochemical function. |
| 本文献已被 CNKI 维普 万方数据 等数据库收录！ |
|
