相关实验视频

Updated: Feb 28, 2026

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

13.4K

甘氨酸结构在调节GM-CSF生物活性中的作用:从甘氨酸工程的见解

Ece Cagdas, Sarah Line Skovbakke, Judit Pina Agullet

    bioRxiv : the preprint server for biology
    |February 27, 2026
    PubMed
    概括

    颗粒细胞-巨细胞殖民地刺激因子 (GM-CSF) 的糖化对其治疗活性至关重要. 受到MGAT5影响的N-甘氨酸分支显著影响GM-CSF生物活性,突出了改善治疗的甘氨酸工程的潜力.

    更多相关视频

    Rapid Antibody Glycoengineering in Chinese Hamster Ovary Cells06:53

    Rapid Antibody Glycoengineering in Chinese Hamster Ovary Cells

    Published on: June 2, 2022

    3.8K
    Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions11:21

    Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions

    Published on: January 20, 2022

    4.2K

    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...
    10.0K
    Glycocalyx and its Functions01:14

    Glycocalyx and its Functions

    The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.
    9.5K
    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,...
    5.0K
    Matrix Proteoglycans and Glycoproteins01:21

    Matrix Proteoglycans and Glycoproteins

    Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...
    5.3K
    Glycosaminoglycans01:23

    Glycosaminoglycans

    Glycosaminoglycans (GAGs), also known as mucopolysaccharides, are long and linear polymers comprising of specific repeating disaccharides - the amino sugar that can be N-acetylglucosamine or N-acetylgalactosamine, and a uronic acid that is usually glucuronic acid or iduronic acid.
    GAGS are found in the extracellular matrix of vertebrates, invertebrates, and bacteria. Due to their polar nature they attract water, and serve as excellent lubricants or shock absorbers in an animal body.
    Hyaluronic...
    7.4K
    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...
    3.8K