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相关概念视频

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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.
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...
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...
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...
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...
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...

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相关实验视频

Updated: May 10, 2026

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry
11:54

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

Published on: March 23, 2020

在ubiquitin识别中的结构复杂性.

J Wade Harper1, Brenda A Schulman

  • 1Department of Pathology, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115, USA. wade_harper@hms.harvard.edu

Cell
|March 28, 2006
PubMed
概括
此摘要是机器生成的。

乌比奎化蛋白质分类依赖于乌比奎结合域蛋白. 最近的发现揭示了新的蛋白质类和无处不在的相互作用,澄清了无处不在的蛋白质是如何引导到特定的细胞通路的.

更多相关视频

Ubiquitin Chain Analysis by Parallel Reaction Monitoring
08:33

Ubiquitin Chain Analysis by Parallel Reaction Monitoring

Published on: June 17, 2020

In Vitro Analysis of E3 Ubiquitin Ligase Function
06:06

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

相关实验视频

Last Updated: May 10, 2026

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry
11:54

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

Published on: March 23, 2020

Ubiquitin Chain Analysis by Parallel Reaction Monitoring
08:33

Ubiquitin Chain Analysis by Parallel Reaction Monitoring

Published on: June 17, 2020

In Vitro Analysis of E3 Ubiquitin Ligase Function
06:06

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

科学领域:

  • 生物化学 生化学
  • 细胞生物学 细胞生物学
  • 分子生物学分子生物学

背景情况:

  • 乌比基化蛋白对细胞调节至关重要.
  • 特定的蛋白质相互作用决定了无处不在的蛋白质的命运.
  • 了解这些相互作用是细胞功能的关键.

研究的目的:

  • 阐明无处不在的蛋白质分类的机制.
  • 要突出在这个过程中泛素结合域 (UBD) 蛋白质的作用.
  • 审查UBD蛋白质及其与ubiquitin相互作用领域的最新进展.

主要方法:

  • 关于UBD蛋白质的最近研究的文献综述.
  • 已知泛素-泛素结合域相互作用的分析.
  • 整合发现,以解释蛋白质分类途径.

主要成果:

  • 识别各种类别的UBD蛋白质.
  • 在ubiquitin上新型相互作用表面的表征.
  • 展示这些相互作用如何为无处不在的蛋白质提供不同的分类途径.

结论:

  • UBD蛋白质的多样性及其特定的泛胺相互作用是精确分类泛胺蛋白质的核心.
  • 最近的研究大大提高了我们对这些复杂的细胞机制的理解.
  • 这种知识使我们更清楚地了解了蛋白质泛化如何调节细胞路径.