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Updated: Jul 1, 2026

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生物互換性のある化学的誘導体による二分化の条件性グリコシル化が,真核細胞で実施される

Jennifer L Czlapinski1, Michael W Schelle, Lawrence W Miller

  • 1Department of Chemistry, University of California, Berkeley, California 94720, USA.

Journal of the American Chemical Society
|September 16, 2008
PubMed
まとめ

新しい生物互換性化学誘導体 (CID),Tmp-SLFは,望ましくない副作用なしに標的タンパク質の二酸化を可能にします. この新しいCIDは,酵母における遺伝子発現をうまく調節し,精密な生物学的制御のために哺乳類の細胞を設計しました.

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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...
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,...