CD31 (PECAM-1) Exists as a Dimer and Is Heavily N-Glycosylated

This publication has 32 references indexed in Scilit:

• Molecular and functional aspects of PECAM-1/CD31
  Published by Elsevier ,2003
• Differential association of cytoplasmic signalling molecules SHP‐1, SHP‐2, SHIP and phospholipase C‐γ1 with PECAM‐1/CD31
  FEBS Letters, 1999
• Analysis of site-specific N-glycosylation of recombinant Desmodus rotundus salivary plasminogen activator rDSPAα1 expressed in Chinese hamster ovary cells
  Glycobiology, 1997
• The biology of PECAM-1.
  Journal of Clinical Investigation, 1997
• Individually Distinct Ig Homology Domains in PECAM-1 Regulate Homophilic Binding and Modulate Receptor Affinity
  Journal of Biological Chemistry, 1996
• Self-Association of Spectrin's Repeating Segments
  Biochemistry, 1996
• Evidence for carbohydrate-mediated interactions between the neural-cell-adhesion molecules NCAM and L1
  Trends in Biochemical Sciences, 1994
• Different epitopes of the CD31 antigen identified by monoclonal antibodies: cell type‐specific patterns of expression
  Tissue Antigens, 1991
• PECAM-1 (CD31) Cloning and Relation to Adhesion Molecules of the Immunoglobulin Gene Superfamily
  Science, 1990
• Cross-linking of epidermal growth factor receptors in intact cells: detection of initial stages of receptor clustering and determination of molecular weight of high-affinity receptors
  Biochemistry, 1986