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相关概念视频

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...

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相关实验视频

Updated: May 26, 2026

Functional Reconstitution and Channel Activity Measurements of Purified Wildtype and Mutant CFTR Protein
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Hsp90可沙佩龙Aha1下调节挽救了囊性纤维化中CFTR的错误折叠.

Xiaodong Wang1, John Venable, Paul LaPointe

  • 1Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.

Cell
|November 18, 2006
PubMed
概括

研究人员发现,伴侣蛋白质如何影响囊性纤维化转膜导电调节器 (CFTR) 在内分泌网膜的折叠. 调节这些陪伴体为治疗CFTR错折叠疾病提供了潜在的策略.

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Last Updated: May 26, 2026

Functional Reconstitution and Channel Activity Measurements of Purified Wildtype and Mutant CFTR Protein
09:59

Functional Reconstitution and Channel Activity Measurements of Purified Wildtype and Mutant CFTR Protein

Published on: March 9, 2015

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
08:59

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

Published on: February 12, 2019

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06:51

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科学领域:

  • 细胞生物学 细胞生物学
  • 分子生物学分子生物学
  • 蛋白质折叠和错误折叠疾病

背景情况:

  • 外细胞通路区分折叠货物和错误折叠货物的机制尚未完全理解.
  • 囊性纤维化 (CF) 的特征是CFTR蛋白的突变,导致其错误折叠和ER保留.
  • 细胞"章体"在细胞内蛋白质折叠和质量控制中起着至关重要的作用.

研究的目的:

  • 研究控制CFTR折叠和ER内的稳定性的蛋白质相互作用.
  • 为了确定纠正DeltaF508CFTR错折的分子标,并改善其细胞表面表达.
  • 建立一个理解和治疗蛋白质错折疾病的一般框架.

主要方法:

  • 蛋白质组学被用来绘制CFTR (CFTR互动组) 的全球蛋白相互作用.
  • 评估了热冲击蛋白90 (Hsp90) cochaperones 在CFTR折叠稳定性中的作用.
  • 使用小干扰RNA (siRNA) 来部分静止Hsp90的cochaperone ATPase调节器Aha1.1.

主要成果:

  • 发现Hsp90可沙佩龙能调节ER中Hsp90依赖的CFTR蛋白折叠的稳定性.
  • 使用siRNA启动的DeltaF508CFTR变异的细胞表面救援来部分静止Aha1.
  • 该研究确定了与货物相关的特定小组组件,这些组件调节了ER退出.

结论:

  • 德尔塔F508CFTR无法实现稳定,功能性的折叠与CF的病理生理学有关.
  • 细胞小组的动态对于正确的CFTR折叠和ER出口至关重要.
  • 针对与货物相关的陪伴者活动,为CF和其他错误折叠障碍提供了一个新的治疗策略.