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相关概念视频

Proteoglycans01:05

Proteoglycans

4.0K
Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
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Protein Glycosylation01:25

Protein Glycosylation

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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
7.0K
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

2.9K
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...
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Protein Modifications in the RER01:26

Protein Modifications in the RER

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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...
5.3K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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相关实验视频

Updated: Jul 26, 2025

Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility
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Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility

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解读蛋白质O-GalNAcylation:方法开发和疾病影响

Shuang Yue1,2, Xiaotong Wang3,2, Wei Ge1

  • 1Center for Clinical Mass Spectrometry, Department of Pharmaceutical Analysis, College of Pharmaceutical Sciences, Soochow University, Suzhou, Jiangsu 215123, China.

ACS omega
|June 12, 2023
PubMed
概括

类型O-糖化,特别是截断的O-糖化 (Tn抗原),对于粘膜壁垒至关重要,但其调节失调与疾病有关. 新的分析方法正在出现,以研究这个具有挑战性的甘氨酸.

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The Application of Open Searching-based Approaches for the Identification of Acinetobacter baumannii O-linked Glycopeptides
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相关实验视频

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Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility
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科学领域:

  • 生物化学 生物化学
  • 葡萄糖生物学 葡萄糖生物学
  • 免疫学 免疫学 免疫学

背景情况:

  • 类型O-糖化是细胞表面蛋白质的关键翻译后修饰,对生物功能和免疫反应至关重要.
  • 高度O-糖化粘膜形成粘膜屏障,防止病原体. 失调会损害这种防御.
  • 截断的O-糖化 (Tn抗原/O-GalNAcylation) 在癌症和自身免疫性疾病等疾病中被上调调节.

研究的目的:

  • 总结O-GalNAcylation丰富和鉴定分析方法的最新进展.
  • 突出Tn抗原在各种疾病中的生物学作用.
  • 讨论识别异常O-GalNAcylation的临床影响.

主要方法:

  • 对O-GalNAcylation分析方法的最新文献的综述.
  • 对Tn抗原的生物学作用和疾病关联的分析.
  • 讨论临床影响.

主要成果:

  • O-糖化,特别是Tn抗原,在健康和疾病中起着重要的作用.
  • 与N-糖化相比,O-GalNAcylation的可靠丰富和鉴定存在挑战.
  • 分析方法的进步正在改善对O-GalNAcylation的研究.

结论:

  • 了解O-GalNAcylation对于破译其在生理病理学中的作用和开发治疗方法至关重要.
  • 需要改进的分析技术来进行强大的O-GalNAcylation特征.
  • 异常的O-GalNAcylation对各种疾病具有重要的临床影响.