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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

7.1K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
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The Proteasome01:13

The Proteasome

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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...
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Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

2.6K
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...
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Regulated Protein Degradation02:58

Regulated Protein Degradation

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It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
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Conservative Site-specific Recombination and Phase Variation02:53

Conservative Site-specific Recombination and Phase Variation

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Because the DNA segments are cut and reorganized in a direction-specific manner, site-specific recombination has emerged as an efficient genetic engineering technique. Flippase and Cyclization recombinases or Flp and Cre, respectively, are two members of the tyrosine recombinase family derived from bacteriophages, that are used to mediate site-specific DNA insertions, deletions, and targeted expression of proteins in mammalian cell lines.
The recognition sites for Cre recombinase called LoxP...
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Updated: Sep 9, 2025

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
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In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity

Published on: January 29, 2018

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定義されたウビキチン改変SUMOダイマーの合成

Kai-Yu Hsu1, Yane-Shih Wang2,3

  • 1Institute of Biological Chemistry, Academia Sinica, Taipei, Taiwan.

Methods in molecular biology (Clifton, N.J.)
|August 28, 2025
PubMed
まとめ

研究者は拡大する遺伝子コードを使って新しい Ub-SUMO ヘテロダイマーを作り出した. これらのツールは,生物学的プロセスと疾患におけるタンパク質のユビキチン化とSUMOylationのクロストークの研究に役立ちます.

キーワード:
マイケルの反応非正規のアミノ酸SUMO2 についてUb-SUMOヘテロディマー合成ウビキチン

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In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells
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SUMO-Binding Entities SUBEs as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer

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関連する実験動画

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In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
09:45

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In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells
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SUMO-Binding Entities SUBEs as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer
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科学分野:

  • 生物化学
  • 分子生物学
  • プロテオミクス

背景:

  • タンパク質のユビキチン化とSUMOylationは,多数の細胞機能に関与する重要な翻訳後の修正です.
  • これらの経路の調節不良は様々な病気に 関わっている.
  • ユビキチン化とSUMOylationの間の直接的なクロストークを理解することは,複雑な生物学的メカニズムを解明するために不可欠です.

研究 の 目的:

  • 均質なUb-SUMOヘテロジマーを合成する方法を開発する.
  • Ubiquitination-SUMOylationのクロストラックの生化学的調査のためのツールを作成する.
  • Ub-SUMOの鎖形成とタンパク質の相互作用に関する詳細な研究を可能にします.

主な方法:

  • 非正規のアミノ酸 (ncAAs) を組み込むために,拡張遺伝コードアプローチを使用する.
  • バイオートゴナル機能グループ誘導コンジュガーション技術を使用する.
  • 定義された構造を持つUb-タグされたSUMO2ダイマーを合成する.

主要な成果:

  • 均質のUb-SUMOヘテロダイマーの合成が成功しました
  • 複雑なタンパク質の結合を作るための新しい方法の実証.
  • 精密に設計された生物化学測定器具の可用性

結論:

  • 開発された方法は,均質なUb-SUMOヘテロジマーを生成するための強力なプラットフォームを提供します.
  • これらのヘテロジメは,ユビキチン化とSUMOylationのクロストークのメカニズムを調査するための貴重なツールです.
  • この研究は,健康と病気におけるタンパク質変化のダイナミクスをより深く理解することを容易にする.