Structural analyses of O-glycan sugar chains on IgA1 hinge region using SELDI-TOFMS with various lectins

This publication has 17 references indexed in Scilit:

• Evanescent-field fluorescence-assisted lectin microarray: a new strategy for glycan profiling
  Nature Methods, 2005
• Aberrantly glycosylated serum IgA1 are closely associated with pathologic phenotypes of IgA nephropathy
  Kidney International, 2005
• Glycoform composition profiling of O-glycopeptides derived from human serum IgA1 by matrix-assisted laser desorption ionization-time of flight-mass spectrometry
  Analytical Biochemistry, 2004
• The SELDI-TOF MS Approach to Proteomics: Protein Profiling and Biomarker Identification
  Biochemical and Biophysical Research Communications, 2002
• Mass spectrometry proves under-O-glycosylation of glomerular IgA1 in IgA nephropathy
  Kidney International, 2001
• Direct Evidence for Decreased Sialylation and Galactosylation of Human Serum IgA1 Fc O-Glycosylated Hinge Peptides in IgA Nephropathy by Mass Spectrometry
  Biochemical and Biophysical Research Communications, 2000
• The Glycosylation and Structure of Human Serum IgA1, Fab, and Fc Regions and the Role of N-Glycosylation on Fcα Receptor Interactions
  Journal of Biological Chemistry, 1998
• Estimation of the Number of O-Linked Oligosaccharides per Heavy Chain of Human Serum IgA1 by Matrix-Assisted Laser Desorption Ionization Time-of-Flight Mass Spectrometry (MALDI-TOFMS) Analysis of the Hinge Glycopeptide
  The Journal of Biochemistry, 1996
• Galactosylation of N- and O-linked carbohydrate moieties of IgA1 and IgG in IgA nephropathy
  Clinical and Experimental Immunology, 1995
• Agalactosyl glycoforms of IgG autoantibodies are pathogenic.
  Proceedings of the National Academy of Sciences, 1994