I-type Lectins
Open Access
- 1 June 1995
- journal article
- review article
- Published by Elsevier
- Vol. 270 (24), 14243-14246
- https://doi.org/10.1074/jbc.270.24.14243
Abstract
No abstract availableThis publication has 48 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
- A novel role for myelin-associated glycoprotein as an inhibitor of axonal regenerationNeuron, 1994
- Biology of Animal LectinsAnnual Review of Cell Biology, 1993
- 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
- Cell cycle-dependent regulation of CDw75 (β-galactoside α-2,6-sialyltransferase) on human B lymphocytesEuropean Journal of Immunology, 1992
- Diversity in the sialic acidsGlycobiology, 1992
- The c-Ha-ras oncogene induces increased expression of β-galactoside α-2,6-sialyltransferase in rat fibroblast (FR3T3) cellsGlycobiology, 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