| 1. | The review on molecular chaperone
分子伴侣的研究进展 |
| 2. | The passage summarizes the latest research about the molecular chaperone
本文对分子伴侣的最新研究作一综述。 |
| 3. | Molecular chaperone stationed in endoplasmic reticulum and signal conduction way in er stress cells
内质网驻留的分子伴侣与内质网应激的细胞内信号传导途径 |
| 4. | However , the functions of molecular chaperones , especially endoplasmic reticulum chaperones , on brain development are unclear
但有关内质网分子伴侣grp78 、 grp94在脑发育过程中的作用迄今尚不清楚。 |
| 5. | Molecular chaperone , which exists in various organisms , is a protein that binding with the other protein ' s unstable conformation to make it be stable
摘要分子伴侣为一类与其他蛋白不稳定构象结合并使之稳定的蛋白质，广泛分布于各种生物体内。 |
| 6. | Heat shock proteins ( hsps ) are molecular chaperones with potent adjuvant capability in the induction of antigen - specific ctl , thl response and increasing immunogenicity of tumor cells
本课题应用a20肿瘤细胞，经热休克作用，制备热休克肿瘤细胞来源的exosomes 。 |
| 7. | So the study of the microstructure of ers , especially the studies of membrane proteins , secretory proteins and molecular chaperones synthesized by ers have become the frontiers of the molecular biology all over the world
因此研究内质网的微细结构，尤其是er合成的膜蛋白、分泌蛋白和分子伴侣已成为国际上的前沿课题。 |
| 8. | 3 . measuring expression of the associated molecular chaperone grp78 and the enzyme protein disulphide isomerase pdi affected by low expression of grp94 . ( 1 ) detecting mrna and p
检测grp94表达水平下降对相关分子伴侣grp78和pdi的影响( 1 )分别通过rt - pcr方法和westernblot方法从mrna和蛋白水平检测分子伴侣grp78的表达情况。 |
| 9. | In this article we examined the distribution and level of grf78 and grp94 in mouse brain during early development to find the relationship between brain development and molecular chaperones ( grf78 and grp94 )
本文从神经发育的角度研究了内质网分子伴侣grp78 、 grp94与小鼠脑发育的关系，探讨了内质网分子伴侣grp78 、 grp94在此过程中的生物学意义。 |
| 10. | Grp94 functions as molecular chaperones , which are ( poly ) peptide binding proteins that assist in protein folding , assembly and transport . moreover , its role of the transporter for antigen presentation has been discovered
目前已知grp94的功能主要是作为分子伴侣，在新生肽链合成的早期阶段，与新生肽键形成稳定的复合物，参与蛋白质的折叠、装配和转运。 |
