molecular chaperones

Recently studies on mechanism of oxidative protein folding and the role of molecular chaperones in protein quality control .

近年来深入研究蛋白质氧化折叠机制以及分子伴侣在蛋白质质量控制中的作用。

Molecular Chaperones in Hyperthermophiles and Techniques Involved in the Large-scale Production Process of Recombinant Proteins

极端嗜热微生物分子伴侣蛋白研究与嗜热功能蛋白质的规模化制备技术研究

As the most class of the molecular chaperones , the biology functions of Heat Shock Proteins are abroad .

热休克蛋白作为最大的一类分子伴侣，其生物学功能广泛。

Quality control over protein structure and function depends on the presence of molecular chaperones and proteases , which prevent aggregation .

分子伴侣和蛋白酶可有效地调控多肽链的正确折叠。

Endoplasmic reticulum stress to a certain extent can protect cells from injury ? such as expression of molecular chaperones .

一定程度的内质网应激如分子伴侣表达能保护细胞免于损伤；

Cloning and expression of Escherichia coli O157 : H7 fimbriae molecular chaperones gene

大肠杆菌O157：H7菌毛分子伴侣基因的克隆与表达

The effects of molecular chaperones , protein aggregation and macromolecular crowding on protein folding have been studied .

研究了细胞内存在的分子伴侣、蛋白质聚集和大分子拥挤环境对蛋白质折叠的影响。

Main function of sHsps involves molecular chaperones , thermotolerance , inhibition of apoptosis and cell differentiation .

sHsps的主要作用是伴侣分子活性，耐热性和抑制凋亡，调节细胞生长及分化。

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

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）。

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。

Molecular Chaperones and Protein Folding

分子伴侣与蛋白质折叠

Conclusions Different molecular chaperones respond to immune injury according to their own characteristics after liver transplantation , which shows the mechanism of cellular self-protection .

结论不同种类的热休克蛋白依据自身表达的特点对移植后的免疫损伤作出反应，体现了细胞的自我保护机制。

Molecular Chaperones and Exercises

分子伴侣与运动

New Life Molecular chaperones are predominantly involved in assisting newly synthesized protein folding and in preventing denaturing proteins from misfolding and aggregation .

分子伴侣蛋白在生物体内的主要功能是帮助新生肽链的折叠以及防止变性蛋白的聚集等。

HSPs have many functions , such as molecular chaperones , thermo tolerance , chilling tolerance , and other biochemical functions in the development of organisms cell metabolism .

这一发现暗示着热休克蛋白的功能可能会很多。已经报道的有分子伴侣，耐热性，耐冷性以及在昆虫发育过程和细胞代谢中生化作用的特殊功能等。

Seventeen protein spots were successfully identified and include proteins that participate in the immune response and in other metabolic pathways , cytoskeletal proteins , and molecular chaperones .

在鉴定成功的17蛋白点，包括了免疫反应和各种代谢途径参与蛋白，还有细胞骨架蛋白、分子伴侣等。

The properly folding of most heterologous proteins need the helper molecular chaperones . There are two kinds of molecular chaperones playing critical roles in the folding of protein in E.

蛋白的折叠大多需要分子伴侣的协助才能完成，其中有两类分子伴侣对蛋白的折叠有重要的影响。

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 .

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。

Small heat shock proteins ( sHsps ), as one sub-class of molecular chaperones , are known for the existence of a highly conserved 80-100 amino acids α - crystallin domain .

小分子热休克蛋白是分子伴侣蛋白中的一个亚家族，结构特征是含有保守的α-crystallin结构域。

However , most researches about the function of ER-located molecular chaperones in UPR are only focused on high molecular chaperones , neglecting the small heat shock proteins ( sHSPs ) .

目前关于内质网中分子伴侣在UPR应答机制中作用的研究主要集中于高分子量热激蛋白，而对小分子热激蛋白相关的研究较少。

These proteins were grouped into different functional classes : cytoskeletal proteins , signal transduction proteins , molecular chaperones , cell proliferation and metastasis-related proteins , biosynthesis proteins , energy metabolism proteins and so on .

这些蛋白质包括：细胞骨架蛋白、信号转导蛋白、分子伴侣、细胞增殖和转移相关蛋白、生物合成蛋白、能量代谢蛋白等。

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。

Based on these observations , we propose that the periplasmic proteins have been evolved to resist the formation of aggregates when subjected to various denaturing conditions and molecular chaperones may thus not be needed in periplasm .

根据这些发现，我们提出假说：膜间质蛋白在恶劣环境条件的选择压力下进化出对各种变性条件所诱导聚集的抗性，而不需要分子伴侣蛋白的有效保护。

Molecular Chaperones are currently defined in functional terms as a class of unrelated families of protein that assist the correct non-covalent assembly of other polypeptide-containing structures in vivo , but which are not components of these assembled structures .

分子伴侣是一类相互之间没有关系的蛋白，它们的功能是帮助其他含多肽结构的物质在体内进行正确的非共价的组装，但它们不是组装后结构的组成部分。

HSPs are constitutively expressed in the unstressed cell where they act as molecular chaperones , associating with newly synthesized proteins , facilitating folding and aiding translocation of newly synthesized proteins to intracellular sites such as the mitochondria .

一些热休克蛋白在非应激细胞有连续的表达，与新合成的蛋白有关，起分子伴侣作用，帮助新合成蛋白折叠和帮助新合成的蛋白转位到细胞器，例如线粒体中。

The accumulation of unfolded proteins in the endoplasmic reticulum ( ER ) lumen causes ER stress response , activates the unfolded protein response ( UPR ) signal pathway and consequently induces the expression of ER-located molecular chaperones ( such as BiP , calnexin , etc. ) in eukaryote cells .

真核细胞内质网中未折叠蛋白的积累会引起内质网胁迫（ERstress），激活未折叠蛋白应答（UPR）信号途径，从而诱导内质网中分子伴侣的表达（比如BiP和Calnexin等）。

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

分子伴侣：抑制素（PHB），内质网蛋白ER29（Erp29）；

The molecular chaperone ( molecular chaperones ) are a group of widespreads from bacteria to human proteins , non-covalent reconciliation with the nascent chain folding of proteins chain binding , and help them fold and transport , usually not involved in the physiological functions of target proteins .

分子伴侣（molecularchaperones）是一组从细菌到人广泛存在的蛋白质，非共价地与新生肽链和解折叠的蛋白质肽链结合，并帮助它们折叠和转运，通常不参与靶蛋白的生理功能。