分子伴侣

这些差异蛋白质点包括蛋白质合成与分解、分子伴侣、解毒和DAN修复相关蛋白质、三大代谢相关酶类、细胞结构相关蛋白质以及信号传导相关蛋白质六类。

Some of these proteins participated protein synthesis and degradation , or chaperone , or protection and detoxification , or signal trans - duction , while some of them were involved in metabolism or cytoskeleton construction .

人胃癌组织中分子伴侣蛋白的表达及检测

Expression and Detection of Chaperone Proteins in Human Gastric Cancer

分子伴侣活性分析发现，辣根过氧化物酶，牛血清白蛋白具有分子伴侣活性，能够抑制胰岛素B链的聚集。

Chaperones activity assay revealed that HRP and BSA possessed chaperone activity to inhibit the B-chain aggregation of insulin .

有蛋白质、酶和RNA分子伴侣的作用；

It is the molecular companion of protein and RNA ;

UV辐射可进一步降低硒性白内障α晶状体蛋白的分子伴侣活性。

UV irradiation further decreased chaperone activity of α crystallin from selenite cataractous lenses .

分子伴侣发挥功能依赖于ATP的结合与水解。

They function in ATP binding and hydrolysis .

研究结果为进一步认识内质网相关的分子伴侣在AD发病中的作用及防治研究提供了依据。

In conclusion , our research provides some proofs for the role of ER associative molecular chaperone in progress and prevention of AD.

GRP78/Bip作为内质网固有分子伴侣，在ER应激时表达增高，是ER应激的标记物。

GRP78 / Bip as an inherent molecular chaperone in the endoplasmic reticulum is the marker of ER stress .

分子伴侣GroEL对青霉素G酰化酶亚基折叠的影响

Effect of GroEL Chaperone on Posttranslational Process of Penicillin G Acylase Gene in E.coli

人工分子伴侣系统辅助鸡IL-18重组蛋白复性过程中研究的影响因素

Influencing factors in the refolding process of artificial molecular chaperone assisting chicken IL-18 recombination protein

热休克蛋白（Heatshockprotein，HSP）具有分子伴侣作用，参与肿瘤抗原的加工递呈，在诱导肿瘤免疫反应中发挥重要作用。

As molecular chaperone , heat shock protein ( HSP ) participates in processing and presentation of tumor antigen and plays an important role in eliciting antitumor immunity .

HSP70具有细胞保护及分子伴侣作用。

HSP 70 functions as cytoprotective protein and molecular chaperon .

正常条件下，HSP占细胞内蛋白组分的5%，在细胞内作为分子伴侣（chaperone）参与蛋白质的折叠、装配、转运和降解。

HSPs normally constitute up to 5 % of the total intracellular proteins .

小分子伴侣GroEL（191-345）在E.coli中的表达及其培养条件的优化

Expression and culture optimization of mini-chaperone GroEL ( 191-345 ) in E. coli

pH跨度为4.8-5.6.不同组织类型中分子伴侣蛋白的分布及pH跨度具有一致性。

These chaperone proteins clustering along the pH gradient were very typical and reproducible , and the distributions of the proteins and the pH range were accordant among the tissues of different types .

此外，CyP还起着分子伴侣的作用，在应激反应中参与调节信号转导途径，并影响RNA的剪接过程。

In addition , CyP can work as molecule chaperones and plays roles in signalling pathways regulation under stress condition and RNA splicing .

分子伴侣DJ-1与小肽协同抑制α-突触核蛋白的聚集

Interaction of DJ-1 with Small Peptide to Inhibit the Aggregation of Alpha-synuclein in E.coli

目的：热休克蛋白47（Heatshockprotein47，HSP47）是一种胶原特异性分子伴侣，存在于内质网内，参与胶原合成的加工修饰过程，在胶原合成及纤维化病理过程中发挥着重要作用。

Objective : Heat shock protein 47 ( HSP47 ) is a collagen-specific molecular chaperone localized in the endoplasmic reticulum ( ER ) of the collagen producing cells .

研究发现，在体内作为分子伴侣的热休克蛋白90（Heatshockprotein90，HSP90）对肿瘤的发生发展起着重要作用，正逐渐成为肿瘤治疗的新靶点。

It was reported that heat shock protein 90 ( HSP90 ), as a molecular chaperone , plays an important role in tumor development and is becoming a new target for cancer therapy .

新生多肽结合复合物（nascentpolypeptide-associatedcomplex，NAC）能与核糖体以1：1的化学计量结合，是新生态链离开核糖体后结合的第一个分子伴侣。

Nascent polypeptide-associated complex ( NAC ) binds ribosome at a 1:1 stoichiometry , and is the first molecular chaperone contacting the nascent polypeptide .

DsbA-DsbA~（mut）融合蛋白作为分子伴侣在原核表达系统中的作用研究

Study of DsbA-DsbA ~ ( mut ) as Molecular Chaperone in Prokaryotic Expression System

分子伴侣GroEL促进溶菌酶复性动力学

Kinetics of lysozyme refolding facilitated by molecular chaperone GroEL

为此本文研究了除LepA以外保守GTP酶的分子伴侣活性。

This paper studies the chaperone activity of conservative GTPase except LepA .

免疫学研究表明，热休克蛋白（HSP）作为分子伴侣（MolecularChaperone）在肿瘤及病毒抗原的MHCⅠ类限制性抗原呈递途径中发挥重要作用。

Many studies showed that heat shock protein ( HSP ), as a molecular chaperone , played important roles in the processing and presentation of MHC-I antigens of virus or tumors .

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。

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 .

GroEL分子伴侣研究进展

Progress in molecular chaperon GroEL

热激蛋白（Hsp）作为分子伴侣协助蛋白的重新折叠、稳定、胞内运输和降解，以阻止受损蛋白的累积，维护细胞内环境的稳定。

Heat shock proteins function as molecular chaperones in preventing the accumulation of damaged proteins to maintain cellular homeostasis by refolding , stabilization , intracellular translocation and degradation of proteins .

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。

However , the functions of molecular chaperones , especially endoplasmic reticulum chaperones , on brain development are unclear .

分子伴侣：抑制素（PHB），内质网蛋白ER29（Erp29）；

(⑤ molecular ) chaperones : prohibitin ( PHB ) and endoplasmic reticulum protein ER29 ( Erp29 );

热激蛋白70（hsp70s）具有分子伴侣的功能，其中在非胁迫条件下表达的hsp70s称为热激同源蛋白70（hsc70）。

Heat shock cognate proteins 70 ( hsp70s ) act as molecular chaperones .