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Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG
Rheumatoid arthritis (RA) is a widely prevalent (1–3%) chronic systemic disease thought to have an autoimmune component1; both humoral1–4 and cellular5,6 mechanisms have been implicated. PrimaryExpand
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Glycosylation differences between the normal and pathogenic prion protein isoforms.
  • P. Rudd, T. Endo, +8 authors R. Dwek
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences…
  • 9 November 1999
Prion protein consists of an ensemble of glycosylated variants or glycoforms. The enzymes that direct oligosaccharide processing, and hence control the glycan profile for any given glycoprotein, areExpand
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Structures and application of oligosaccharides in human milk
  • A. Kobata
  • Biology, Medicine
  • Proceedings of the Japan Academy. Series B…
  • 21 July 2010
Comparative study of the oligosaccharide profiles of individual human milk revealed the presence of three different patterns. Four oligosaccharides containing the Fucα1-2Gal group were missing in theExpand
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Structures and functions of the sugar chains of glycoproteins.
  • A. Kobata
  • Chemistry, Medicine
  • European journal of biochemistry
  • 1992
Most proteins within living organisms contain sugar chains. Recent advancements in cell biology have revealed that many of these sugar chains play important roles as signals for cell-surfaceExpand
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Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve alpha-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of alpha-dystroglycan with laminin.
alpha-Dystroglycan is a heavily glycosylated protein, which is localized on the Schwann cell membrane as well as the sarcolemma, and links the transmembrane protein beta-dystroglycan to laminin inExpand
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Structures of Sialylated O-Linked Oligosaccharides of Bovine Peripheral Nerve α-Dystroglycan
α-Dystroglycan is a heavily glycosylated protein, which is localized on the Schwann cell membrane as well as the sarcolemma, and links the transmembrane protein β-dystroglycan to laminin in theExpand
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Diversity of oligosaccharide structures linked to asparagines of the scrapie prion protein.
Prion proteins from humans and rodents contain two consensus sites for asparagine-linked glycosylation near their C-termini. The asparagine-linked oligosaccharides of the scrapie isoform of theExpand
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Fractionation of L-fucose-containing oligosaccharides on immobilized Aleuria aurantia lectin.
The carbohydrate-binding specificity of Aleuria aurantia lectin was investigated by analyzing the behavior of a variety of fucose-containing oligosaccharides on an A. aurantia lectin-SepharoseExpand
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Comparative study of the asparagine-linked sugar chains of human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells.
The asparagine-linked sugar chains of human erythropoietin produced by recombinant Chinese hamster ovary cells and naturally occurring human urinary erythropoietin were liberated by hydrazinolysisExpand
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Comparative study of the sugar chains of factor VIII purified from human plasma and from the culture media of recombinant baby hamster kidney cells.
The asparagine-linked sugar chains of blood coagulation factor VIII preparations purified from human plasma of blood group A donors and from the culture media of recombinant BHK cells were releasedExpand
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