The Amino-terminal Immunoglobulin-like Domain of Sialoadhesin Contains the Sialic Acid Binding Site
Open Access
- 1 November 1995
- journal article
- research article
- Published by Elsevier BV
- Vol. 270 (44), 26184-26191
- https://doi.org/10.1074/jbc.270.44.26184
Abstract
No abstract availableKeywords
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 superfamilyCurrent Biology, 1994
- Homophilic adhesion between Ig superfamily carcinoembryonic antigen molecules involves double reciprocal bondsThe Journal of cell biology, 1993
- Association of CD22 with the B cell antigen receptorEuropean Journal of Immunology, 1993
- Endothelial-Leukocyte Adhesion MoleculesAnnual 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 siteCell, 1992
- The B lymphocyte adhesion molecule CD22 interacts with leukocyte common antigen CD45RO on T cells and α2–6 sialyltransferase, CD75, on B cellsCell, 1991
- Crystal structure of an HIV-binding recombinant fragment of human CD4Nature, 1990
- The Immunoglobulin Superfamily—Domains for Cell Surface RecognitionAnnual Review of Immunology, 1988