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  2. Glycoprotein - Wikipedia

    en.wikipedia.org/wiki/Glycoprotein

    One example of glycoproteins found in the body is mucins, which are secreted in the mucus of the respiratory and digestive tracts. The sugars when attached to mucins give them considerable water-holding capacity and also make them resistant to proteolysis by digestive enzymes. Glycoproteins are important for white blood cell recognition.

  3. Glycoconjugate - Wikipedia

    en.wikipedia.org/wiki/Glycoconjugate

    Glycoconjugates are very important compounds in biology and consist of many different categories such as glycoproteins, glycopeptides, peptidoglycans, glycolipids, glycosides, and lipopolysaccharides. They are involved in cell–cell interactions, including cell–cell recognition; in cell–matrix interactions; and in detoxification processes.

  4. Glycoprotein Ib-IX-V complex - Wikipedia

    en.wikipedia.org/wiki/Glycoprotein_Ib-IX-V_complex

    The GPIb-IX-V complex is a profuse membrane receptor complex originating in megakaryocytes and exclusively functional on the surface of platelets. [1] It primarily functions to mediate the first critical step in platelet adhesion, by facilitating binding to von Willebrand factor (VWF) on damaged sub-endothelium under conditions of high fluid shear stress.

  5. Glycosylation - Wikipedia

    en.wikipedia.org/wiki/Glycosylation

    N-linked glycosylation is a very prevalent form of glycosylation and is important for the folding of many eukaryotic glycoproteins and for cell–cell and cell–extracellular matrix attachment. The N -linked glycosylation process occurs in eukaryotes in the lumen of the endoplasmic reticulum and widely in archaea , but very rarely in bacteria .

  6. P-glycoprotein - Wikipedia

    en.wikipedia.org/wiki/P-glycoprotein

    P-gp is a 170 kDa transmembrane glycoprotein, which includes 10–15 kDa of N-terminal glycosylation.The N-terminal half of the protein contains six transmembrane helixes, followed by a large cytoplasmic domain with an ATP-binding site, and then a second section with six transmembrane helixes and an ATP-binding domain that shows over 65% of amino acid similarity with the first half of the ...

  7. Oligosaccharide - Wikipedia

    en.wikipedia.org/wiki/Oligosaccharide

    Glycoproteins have distinct Oligosaccharide structures which have significant effects on many of their properties, [11] affecting critical functions such as antigenicity, solubility, and resistance to proteases. Glycoproteins are relevant as cell-surface receptors, cell-adhesion molecules, immunoglobulins, and tumor antigens. [12]

  8. Glycopeptide - Wikipedia

    en.wikipedia.org/wiki/Glycopeptide

    Glycopeptides are peptides that contain carbohydrate moieties covalently attached to the side chains of the amino acid residues that constitute the peptide.. Over the past few decades it has been recognised that glycans on cell surface (attached to membrane proteins or lipids) and those bound to proteins (glycoproteins) play a critical role in biology.

  9. Viral envelope - Wikipedia

    en.wikipedia.org/wiki/Viral_envelope

    A viral envelope is the outermost layer of many types of viruses. [1] It protects the genetic material in their life cycle when traveling between host cells. Not all viruses have envelopes. A viral envelope protein or E protein is a protein in the envelope, which may be acquired by the capsid from an infected host cell.