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相关概念视频

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
Somatic to iPS Cell Reprogramming01:29

Somatic to iPS Cell Reprogramming

Reprogramming alters the gene expression in somatic cells, transforming them into induced pluripotent stem (iPS) cells over several generations. Scientists can reprogram cells by introducing genes for four transcription factors—Oct4, Sox2, Klf4, and c-Myc (OSKM) by viral or non-viral methods. These factors are also known as Yamanaka factors after Shinya Yamanaka, who first generated iPS cells using mouse skin cells. Yamanaka was awarded the Nobel Prize in Physiology or Medicine in 2012 for this...
Chromatin Modification in iPS Cells01:32

Chromatin Modification in iPS Cells

Chromatin modification alters gene expression; therefore, scientists can add histone-modifying enzymes, histone variants, and chromatin remodeling complexes to somatic cells to aid reprogramming into pluripotent stem (iPS) cells.
Compact chromatin makes reprogramming difficult. Enzymes, such as histone demethylases and acetyltransferases, are often added during reprogramming to loosen the chromatin, making the DNA more accessible to transcription factors. Molecules that inhibit histone...
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: Jul 10, 2026

Purification of Hsp104, a Protein Disaggregase
07:17

Purification of Hsp104, a Protein Disaggregase

Published on: September 30, 2011

蛋白重塑赋予了立即的表型开关.

Prasanna Satpute-Krishnan1, Tricia R Serio

  • 1Department of Molecular Biology, Cell Biology and Biochemistry, Brown University, Providence, Rhode Island 02912, USA.

Nature
|September 9, 2005
PubMed
概括

子或非典型蛋白质可以在功能状态之间切换. 这项研究表明成熟的蛋白,Sup35,可以进入新的状态,导致快速的细胞表型变化.

科学领域:

  • 分子生物学分子生物学
  • 蛋白质生物化学 蛋白质生物化学
  • 酵母遗传学 酵母遗传学

背景情况:

  • 蛋白质,称为子,可以在体内采用多种功能状态,影响诸如遗传等过程.
  • 新合成的子蛋白通常采用现有的细胞构造,确保忠实的表型传播.
  • 控制表型转换的机制以及这些转换期间现有的蛋白质的命运仍然不清楚.

研究的目的:

  • 调查激发酵母子Sup35/[PSI(+) 的表型切换的蛋白质状态变化.
  • 为了确定子形成是否需要在蛋白质合成过程中特定的错折路径,或者是否可以在成熟的蛋白质中发生.

主要方法:

  • 在酵母Sup35/[PSI(+) ]中分析蛋白质状态转换.
  • 研究成熟蛋白重塑在诱导的表型变化中的作用.

主要成果:

  • 在合成过程中,Sup35的子形式不需要新的错折路径.
  • 成熟的Sup35蛋白可以通过重塑进入子状态.
  • 这种过渡与Sup35活动的丧失有关,导致细胞表型的快速改变.

结论:

  • 酵母子的表型切换可以通过成熟蛋白质构成的变化来启动.

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Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

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High-throughput Screening for Protein-based Inheritance in S. cerevisiae
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High-throughput Screening for Protein-based Inheritance in S. cerevisiae

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Purification of Hsp104, a Protein Disaggregase
07:17

Purification of Hsp104, a Protein Disaggregase

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Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
12:57

Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

Published on: January 8, 2015

High-throughput Screening for Protein-based Inheritance in S. cerevisiae
08:12

High-throughput Screening for Protein-based Inheritance in S. cerevisiae

Published on: August 8, 2017

  • 现有的Sup35蛋白的重塑在单个细胞周期内推动了快速的表型变化.
  • 这一发现为子生物学和基于蛋白质的遗传机制提供了新的见解.