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関連する概念動画

The Proteasome Structure01:17

The Proteasome Structure

The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

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関連する実験動画

Updated: Jun 21, 2026

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
09:57

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach

Published on: December 17, 2016

プロテアソーム組立の第一基にたどり着く

Henrike C Besche1, Andreas Peth, Alfred L Goldberg

  • 1Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA.

Cell
|July 15, 2009
PubMed
まとめ
この要約は機械生成です。

26S プロテアソームは,26S プロテアソームである.

さらに関連する動画

Assaying Proteasomal Degradation in a Cell-free System in Plants
07:43

Assaying Proteasomal Degradation in a Cell-free System in Plants

Published on: March 26, 2014

Quantifying Subcellular Ubiquitin-proteasome Activity in the Rodent Brain
09:25

Quantifying Subcellular Ubiquitin-proteasome Activity in the Rodent Brain

Published on: May 21, 2019

関連する実験動画

Last Updated: Jun 21, 2026

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach
09:57

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach

Published on: December 17, 2016

Assaying Proteasomal Degradation in a Cell-free System in Plants
07:43

Assaying Proteasomal Degradation in a Cell-free System in Plants

Published on: March 26, 2014

Quantifying Subcellular Ubiquitin-proteasome Activity in the Rodent Brain
09:25

Quantifying Subcellular Ubiquitin-proteasome Activity in the Rodent Brain

Published on: May 21, 2019

科学分野:

  • 細胞生物学 細胞生物学
  • 分子生物学は分子生物学である.
  • バイオケミストリー バイオケミストリー

背景:

  • ユカリオット26Sプロテアソームは,細胞タンパク質の分解に不可欠な大きなタンパク質複合体です.
  • その組み立ては,サブユニットの相互作用の正確な規制を必要とする複雑なプロセスです.
  • 19S 調節粒子の組成を理解することは,プロテアソームの機能を理解する上で極めて重要です.

研究 の 目的:

  • 19S 調節粒子基の秩序ある組立経路を解明する.
  • この組み立てプロセスに関与する新しい前駆体複合体とチャペロンを特定する.

主な方法:

  • 細胞抽出物のプロテオミック分析. 細胞抽出物のプロテオミック分析.
  • タンパク質の相互作用を特徴付けるための生化学的分析.
  • シェーパロン機能を研究するための遺伝子操作.

主要な成果:

  • 19Sベースアセンブリで以前未知だった前駆体複合体の特定.
  • 特定の組み立てのステップを容易にする4つの専用のチャペロンの発見.
  • サブユニットの組み込みの順序の特徴.

結論:

  • 19S 調節粒子基の組み立ては,段階的なプロセスです.
  • 専用のチャペロンと特定の前駆体複合体は,19Sベースアセンブリの忠誠性を確保するために不可欠です.
  • この研究は,26Sプロテアゾームの複雑な組み立てを理解するための枠組みを提供します.