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相关概念视频

Protein Glycosylation01:25

Protein Glycosylation

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...
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

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...
Protein Modifications in the RER01:26

Protein Modifications in the RER

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 sequences.
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

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...
Proteoglycans01:05

Proteoglycans

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,...
Peptidoglycan Synthesis01:28

Peptidoglycan Synthesis

Structure of PeptidoglycanPeptidoglycan is a vital structural component of the bacterial cell wall, providing mechanical strength and shape to the cell. It consists of repeating units of two sugars—N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM)—linked by β-1,4 glycosidic bonds. These sugar chains are cross-linked by short peptide chains, forming a mesh-like polymer that surrounds the bacterial plasma membrane.Cytoplasmic Phase – Precursor SynthesisPeptidoglycan biosynthesis begins in...

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相关实验视频

Updated: May 12, 2026

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
09:54

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases

Published on: December 26, 2011

O-GlcNAc修改调节了层层A尾部的加工过程.

Katherine Augspurger1,2,3, Elizabeth Martin1,2, Jason Maynard4

  • 1Department of Biochemistry and Biophysics, University of California San Francisco, San Francisco, United States.

bioRxiv : the preprint server for biology
|March 31, 2025
PubMed
概括
此摘要是机器生成的。

O-GlcNAcylation是一种对葡萄糖敏感的修饰,通过增强尾部裂变来促进层A处理. 这一发现将葡萄糖代谢与核膜生物发生和膜A调节联系起来.

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Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines
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相关实验视频

Last Updated: May 12, 2026

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
09:54

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases

Published on: December 26, 2011

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines
12:06

Metabolic Glycoengineering of Sialic Acid Using N-acyl-modified Mannosamines

Published on: November 25, 2017

Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling
11:08

Chemo-enzymatic Synthesis of N-glycans for Array Development and HIV Antibody Profiling

Published on: February 5, 2018

科学领域:

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

背景情况:

  • 层A处理对于核层组装,核结构和染色质组织至关重要.
  • 预层A经过法尼基化和C端切割,产生成熟的层A.
  • O-GlcNAc转移酶 (OGT) 是一种对葡萄糖敏感的酶,参与了翻译后的修饰.

研究的目的:

  • 调查OGT和O-GlcNAcylation在调节层A生物发生和加工中的作用.
  • 探索葡萄糖代谢与核膜形成之间的潜在联系.

主要方法:

  • 研究了不同水平的OGT和OGT抑制对内源层A的影响.
  • 使用修改后尾切割试验来评估O-GlcNAcylation对层A处理的直接影响.
  • 引入了OGT结合基因和O-GlcNAc修饰位点的突变.

主要成果:

  • 改变OGT水平或活动并没有影响内源性层状A的丰度或分布.
  • 破坏OGT结合或O-GlcNAc修饰位点的突变降低了尾部裂解效率.
  • 发现O-GlcNAcylation促进了层层A的加工,特别是尾部的裂变.

结论:

  • O-GlcNAcylation 在层A处理中起着促进作用.
  • 这些发现确立了葡萄糖代谢和核膜生物生成之间的联系.
  • 识别了O-GlcNAcylation作为层层A裂变的调节机制.