Jove
Visualize
联系我们
JoVE
x logofacebook logolinkedin logoyoutube logo
关于 JoVE
概览领导团队博客JoVE 帮助中心
作者
出版流程编辑委员会范围与政策同行评审常见问题投稿
图书馆员
用户评价订阅访问资源图书馆顾问委员会常见问题
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experiments存档
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教师资源中心教师网站
使用条款与条件
隐私政策
政策

相关概念视频

Histone Modification02:32

Histone Modification

15.8K
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
15.8K
Histone Modification02:32

Histone Modification

4.3K
4.3K
Protein Modifications in the RER01:26

Protein Modifications in the RER

6.8K
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
6.8K
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

3.5K
Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
3.5K
Regulated Protein Degradation02:58

Regulated Protein Degradation

3.0K
3.0K
Regulated Protein Degradation02:58

Regulated Protein Degradation

8.7K
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...
8.7K

您也可能阅读

相关文章

通过共同作者、期刊和引用图与本文相关的文章。

排序
Same author

Evaluating the impact of artificial intelligence scribes on clinical documentation in primary care: a simulation study.

JAMIA open·2026
Same author

Selective Bidentate Coordination Reconstructs Residual PbI<sub>2</sub> to Homogenize Interfacial Energetics in Perovskite Solar Cells.

Journal of the American Chemical Society·2026
Same author

Pan-cancer analysis of tissue-plasma genomic concordance reveals enhanced concordance with liver metastasis and plasma clonality as predictor of poorer overall survival.

NPJ precision oncology·2026
Same author

Mechanical loading primes MSC-derived exosomes to promote cartilage repair.

Bioactive materials·2026
Same author

Dehydration/1,6-addition-based Site-specific Bioconjugation Unveils Norepinephrinylation as a Widespread Post-translational Modification in the Cellular Proteome.

bioRxiv : the preprint server for biology·2026
Same author

Perfluorooctanoic acid exposure disrupts gut microbiota and aggravates experimental colitis.

Environmental pollution (Barking, Essex : 1987)·2026

相关实验视频

Updated: Jan 8, 2026

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
14:32

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates

Published on: February 27, 2016

8.6K

赛尔图因2 调节 作为半降糖体的 希斯糖化.

Huapeng Li1,2, Yvonne Ritsema1,2, Zeng Lin1,2

  • 1Department of Medicinal Chemistry and Molecular Pharmacology, College of Pharmacy, Purdue University, West Lafayette, Indiana 47907, United States.

Biochemistry
|December 19, 2025
PubMed
概括

赛尔图因2 (SIRT2) 作为半脱糖体,从修改后的组织蛋白中去除酸. 这种酶与DJ-1一起,有助于预防癌症中甲基甘 (MGO) 和甘 (GO) 引起的细胞损伤.

更多相关视频

Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue
08:12

Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue

Published on: May 5, 2022

4.4K
Author Spotlight: Epigenetic Modifications and Metabolic Rewiring as Targets for Cancer Therapy
07:20

Author Spotlight: Epigenetic Modifications and Metabolic Rewiring as Targets for Cancer Therapy

Published on: October 18, 2024

894

相关实验视频

Last Updated: Jan 8, 2026

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
14:32

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates

Published on: February 27, 2016

8.6K
Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue
08:12

Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue

Published on: May 5, 2022

4.4K
Author Spotlight: Epigenetic Modifications and Metabolic Rewiring as Targets for Cancer Therapy
07:20

Author Spotlight: Epigenetic Modifications and Metabolic Rewiring as Targets for Cancer Therapy

Published on: October 18, 2024

894

科学领域:

  • 生物化学 生物化学
  • 分子生物学分子生物学
  • 癌症研究 癌症研究

背景情况:

  • 甲基醇 (MGO) 和醇 (GO) 是反应性碳类物种,涉及癌症的发展.
  • 由MGO/GO诱导的组织基因糖化会影响染色质结构和癌症进展.
  • 之前的研究确定了DJ-1和PAD4作为具有针对MGO/GO- 基因组修饰的glyoxalase/deglycase活性的酶.

研究的目的:

  • 为了确定新兴的组织素糖化调节剂.
  • 调查基脱乙酶SIRT2在对抗MGO/GO诱导的基修饰中的作用.
  • 为了阐明SIRT2调节组织糖化的机制.

主要方法:

  • 生物化学测试,以评估SIRT2在修改后的组素残留物上的酶活性.
  • 研究SIRT2和DJ-1的相互作用和联合功能.
  • 在实验中使用一种酶性不活的DJ-1突变体 (DJ-1-C106A).

主要成果:

  • 鉴定出SIRT2是一种"半脱糖体",可以从特定的质子添加物中去除乳酸和甘油酸.
  • 这些添加物 (ε-N-l-lactyllysine和hydroxyacetyllysine) 是从MGO/GO-lysine修饰中衍生而来的.
  • 与DJ-1-C106A一起的SIRT2将MGO/GO转化为乳酸和糖酸,减轻细胞毒性.

结论:

  • SIRT2是一种新发现的基因组糖化调节剂.
  • SIRT2对MGO和GO细胞毒性起着保护作用.
  • SIRT2-DJ-1轴为癌症中与MGO/GO相关的病理管理提供了潜在的治疗标.