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相关概念视频

Oligosaccharide Assembly01:24

Oligosaccharide Assembly

2.8K
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 Glycosylation01:25

Protein Glycosylation

6.9K
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...
6.9K
Proteoglycans01:05

Proteoglycans

3.9K
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,...
3.9K

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相关实验视频

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Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins
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使用双功能小分子进行向蛋白O-GLNAcylation

Bowen Ma1, Khadija Shahed Khan1,2, Tongyang Xu1

  • 1School of Pharmacy, Faculty of Medicine, The Chinese University of Hong Kong, Sha Tin, Hong Kong.

Journal of the American Chemical Society
|April 1, 2024
PubMed
概括

研究人员开发了新的O-GlcNAcylation TArgeting Chimeras (OGTACs),以精确控制活细胞中的蛋白质O-GlcNAcylation. 这一突破使得在疾病和治疗开发中对O-GlcNAcylation进行有针对性的研究.

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Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
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The Application of Open Searching-based Approaches for the Identification of Acinetobacter baumannii O-linked Glycopeptides
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科学领域:

  • 生物化学
  • 分子生物学
  • 化学生物学

背景情况:

  • 与蛋白质O结合的β-N-乙糖胺修饰 (O-GlcNAcylation) 对细胞过程至关重要.
  • 失调的O-GlcNAcylation与癌症,糖尿病和神经退行等疾病有关.
  • 现有的化学工具缺乏研究O-GlcNAcylation的蛋白质和位点特异性.

研究的目的:

  • 开发用于精确控制蛋白质O-GLNAcylation的新型化学工具.
  • 在活细胞中实现蛋白特异性O-GlcNAcylation.
  • 促进研究O-GlcNAcylation在疾病和治疗发展中的作用.

主要方法:

  • 开发称为O-GlcNAcylation TTargeting Chimeras (OGTACs) 的异构功能小分子.
  • 使用OGTAC来招募FKBP12F36V融合的O-GlcNAc转移酶 (OGT) 来向蛋白质.
  • 证明细胞质中O-GlcNAcylation的时间,大小和可逆控制.

主要成果:

  • 在活细胞中,OGTACs成功诱导了BRD4,CK2α和EZH2的蛋白特异O- GlcNAcylation.
  • 实现可控的O-GlcNAcylation,具有时间,大小和可逆性特征.
  • 验证的OGTAC作为调节O-GlcNAcylation的有效工具.

结论:

  • OGTACs提供了一个强大的化学平台来诱导特定蛋白质的O-GlcNAcylation.
  • 这项技术能够对O-GlcNAcylation路径进行详细的功能剖析.
  • 对于与O-GlcNAcylation相关的疾病,OGTAC提供了新的治疗途径.