The Amino-terminal Immunoglobulin-like Domain of Sialoadhesin Contains the Sialic Acid Binding Site

This publication has 51 references indexed in Scilit:

• Identification of the ligand-binding domains of CD22, a member of the immunoglobulin superfamily that uniquely binds a sialic acid-dependent ligand.
  The Journal of Experimental Medicine, 1995
• Sialoadhesin, myelin-associated glycoprotein and CD22 define a new family of sialic acid-dependent adhesion molecules of the immunoglobulin superfamily
  Current Biology, 1994
• Homophilic adhesion between Ig superfamily carcinoembryonic antigen molecules involves double reciprocal bonds
  The Journal of cell biology, 1993
• Association of CD22 with the B cell antigen receptor
  European Journal of Immunology, 1993
• Endothelial-Leukocyte Adhesion Molecules
  Annual Review of Immunology, 1993
• Identification of a peptide sequence involved in homophilic binding in the neural cell adhesion molecule NCAM.
  The Journal of cell biology, 1992
• The binding site on ICAM-1 for plasmodium falciparum-infected erythrocytes overlaps, but is distinct from, the LFA-1-binding site
  Cell, 1992
• The B lymphocyte adhesion molecule CD22 interacts with leukocyte common antigen CD45RO on T cells and α2–6 sialyltransferase, CD75, on B cells
  Cell, 1991
• Crystal structure of an HIV-binding recombinant fragment of human CD4
  Nature, 1990
• The Immunoglobulin Superfamily—Domains for Cell Surface Recognition
  Annual Review of Immunology, 1988