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- molecular chaperone proteins 分子伴侣蛋白
- The researchers learned that hypochlorite, rather than damaging Hsp33 as it does most proteins, actually revs up the molecular chaperone. 研究人员了解到,次氯酸不会像对待多数蛋白那样破坏Hsp33,实际上反而加速分子伴侣开启功能。
- HSP70 is known to assist the folding of nascent polypeptide chains, act as a molecular chaperone and mediate the repair and degradation of altered or denatured proteins. HSP70作为分子伴侣在协助新生多肽链折叠,蛋白质复合体的装配,以及调节、修护和降解变性的蛋白质方面起着重要作用。
- The heat shock protein Hsp90 is a molecular chaperone that binds to various denatured or unfolded client proteins and helps shuttle them into the proteasome for recycling. 热休克蛋白90作为环境相关性分子伴侣中的一员,可以使细胞信号转导蛋白的构象成熟、功能稳定。
- 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。
- The protein refolding assisted by the molecular chaperone systems is promised to improve the protein renaturation efficiency. 蛋白质复性,即如何高效地将无活性的包涵体转变成为有活性的蛋白质,已成为基因工程蛋白产业化的瓶颈。
- Jakob and her team were studying a bacterial protein known as heat shock protein 33 (Hsp33), which is classified as a molecular chaperone. Jakob和她的研究小组一起研究一种名为热休克蛋白33(Hsp33)的细菌蛋白质,Hsp33分类为分子伴侣(肽链分子装配陪伴蛋白)。
- Objective: Heat shock protein 47(HSP47) is a collagen-specific molecular chaperone localized in the endoplasmic reticulum(ER) of the collagen producing cells. 目的:热休克蛋白47(heat shock protein47,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。
- In fact, as a specific molecular chaperone, HSP90 proteins are possibly involved in many important physiological processes such as signal transduction, cell cycle regulation and hormone response. 事实证明,作为一种特异的分子伴侣,HSP90除在细胞正常生长和应急保护中具有重要生理功能外,还与信号传导、细胞周期调控、激素应答等细胞内重要生理过程有关。
- Meantime, the mechanism and applications of molecular chaperone systems in the renaturation of proteins were presented.The artificial molecular chaperone systems were also briefly introduced. 本文针对这一技术,综述了分子伴侣的功能和种类、各种分子伴侣体系的作用原理及在蛋白质复性中的应用情况,并简单介绍了人工分子伴侣。
- Heat shock protein47(HSP47) is a 47-kDa stress protein that is a collagen-specific molecular chaperone residing in the endoplasmic reticulum (ER). HSP47 is closely involved in the folding, assembly, modification and transport of procollagen. 热休克蛋白47(HSP47)是一种分子量为47KD的蛋白,在内质网中能与多种类型胶原和前胶原特异性结合,HSP47作为胶原合成有关的“分子伴侣”,参与前胶原在内质网中的折叠、装配、修饰和转运等过程,对胶原分子合成质量控制起重要的作用,能够防止错误构型的前胶原分泌出内质网。
- Some kinds of molecular chaperone systems and their functions as well were reviewed in this paper. 而利用分子伴侣的协助折叠特性进行的蛋白质复性技术正成为这一领域的研究热点。
- Abstract : This paper discussed the classification, function, mechanism, current research progress and the application prospect of the molecular chaperone. 摘 要 :本文综述了分子伴侣的分类、功能、作用机理、研究现状及应用前景。
- Expression of chaperone proteins in human gastric cancer 人胃癌组织中分子伴侣蛋白的表达及检测
- Normal cells respond to ER stress by increasing transcription of genes encoding ER-resident molecular chaperones such as GRP94, GRP78 and PDI to facilitate protein folding. 细胞对这种应激的反应是增加一系列内质网分子伴侣如GRP94、GRP78和PDI等的表达。
- Now, there were several studies about it, such as presequences, processing of precursor proteins, function of molecular chaperones and sorting of mitochondria and plastids(or chloroplasts). 目前在诸如前序列、前体蛋白加工、分子伴侣及线粒体与质体(或叶绿体)之间分选等几方面开展了许多研究。
- The function and application of molecular chaperone 分子伴侣的功能和应用
- Both of them are localized within the endoplasmic reticulum(ER) and possess ATP-binding sites. Envidence has shown that GRPs function as molecular chaperones by assisting in the proper folding and assembly of proteins within the ER. 同时他们又是分布在内质网(Endoplasmic Reticulum ER)腔内的分子伴侣,具有弱的ATP酶活性,与ATP结合后可以协助新生蛋白质的转位、折叠以及寡聚蛋白的组装。
- endoplasmic reticulum molecular chaperone 内质网分子伴侣
- To dif-ferentiate from the general molecular chaperones, the term of intramolecular chaperone(IMC)was introduced to refer to this function of Pro peptides. 为了与一般意义上的分子伴侣相区别,人们将对蛋白质折叠有帮助的前导肽称为分子内分子伴侣。