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  2. 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.

  3. Congenital disorder of glycosylation - Wikipedia

    en.wikipedia.org/wiki/Congenital_disorder_of...

    A congenital disorder of glycosylation (previously called carbohydrate-deficient glycoprotein syndrome) is one of several rare inborn errors of metabolism in which glycosylation of a variety of tissue proteins and/or lipids is deficient or defective. Congenital disorders of glycosylation are sometimes known as CDG syndromes.

  4. Glycation - Wikipedia

    en.wikipedia.org/wiki/Glycation

    Glycation (non-enzymatic glycosylation) is the covalent attachment of a sugar to a protein, lipid or nucleic acid molecule. [1] Typical sugars that participate in glycation are glucose , fructose , and their derivatives.

  5. List of therapeutic monoclonal antibodies - Wikipedia

    en.wikipedia.org/wiki/List_of_therapeutic...

    human: Y: treatment of Zaire ebolavirus (Ebola virus) Atorolimumab [2] mab: human: Rhesus factor: hemolytic disease of the newborn [citation needed] Avelumab [12] Bavencio: mab: human: PD-L1: Y: cancer Axatilimab [27] Niktimvo: mab: humanized: CSF1R: Y: chronic graft-versus-host disease: Azintuxizumab vedotin [28] mab: chimeric/ humanized ...

  6. Fucosidosis - Wikipedia

    en.wikipedia.org/wiki/Fucosidosis

    4 Treatment. 5 History. 6 Other forms. 7 See also. ... Typically affecting dogs between 18 months and four years, ... As in the human version, canine fucosidosis is a ...

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  8. 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 ...

  9. Glutamate carboxypeptidase II - Wikipedia

    en.wikipedia.org/wiki/Glutamate_carboxypeptidase_II

    In addition, human GCPII has ten sites of potential glycosylation, and many of these sites (including some far from the catalytic domain) affect the ability of GCPII to hydrolyze NAAG. [6] The human FOLH1 gene is positioned at the 11p11.12 locus of chromosome 11. The gene is 4,110 base pairs in length and composed of 22 exons.