Control of IgG/Fc glycosylation: A comparison of oligosaccharides from chimeric human/mouse and mouse subclass immunoglobulin Gs

This publication has 25 references indexed in Scilit:

• A protein structural change in aglycosylated IgG3 correlates with loss of huFcγR1 and hufcγR111 binding and/or activation
  Molecular Immunology, 1990
• Site-specific attachment to recombinant antibodies via introduced surface cysteine residues
  Protein Engineering, Design and Selection, 1990
• The occurrence of mouse-type oligosaccharides in mouse-human chimeric immunoglobulin G
  Biochemical and Biophysical Research Communications, 1989
• The binding site for C1q on IgG
  Nature, 1988
• Comparison of the effector functions of human immunoglobulins using a matched set of chimeric antibodies.
  The Journal of Experimental Medicine, 1987
• Construction of novel antibodies by use of DNA transfection: design of plasmid vectors
  Philosophical Transactions of the Royal Society of London. Series A, Mathematical and Physical Sciences, 1986
• Xylose-containing common structural unit in N-linked oligosaccharides of laccase from sycamore cells
  Biochemistry, 1986
• Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG
  Nature, 1985
• Effector functions of a monoclonal aglycosylated mouse IgG2a: Binding and activation of complement component C1 and interaction with human monocyte Fc receptor
  Molecular Immunology, 1985
• Control of glycoprotein synthesis. Bovine milk UDPgalactose:N-acetylglucosamine 4-.beta.-galactosyltransferase catalyzes the preferential transfer of galactose to the GlcNAc.beta.l1,2Man.alpha.1,3- branch of both bisected and nonbisected complex biantennary asparagine-linked oligosaccharides
  Biochemistry, 1985