A Single N-linked Glycosylation Site Is Implicated in the Regulation of Ligand Recognition by the I-type Lectins CD22 and CD33
Open Access
- 1 August 1996
- journal article
- Published by Elsevier
- Vol. 271 (31) , 18803-18809
- https://doi.org/10.1074/jbc.271.31.18803
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- Glycosylation of CD44 is implicated in CD44-mediated cell adhesion to hyaluronan.The Journal of cell biology, 1996
- I-type LectinsPublished by Elsevier ,1995
- Regulation of CD45 engagement by the B-cell receptor CD22.Proceedings of the National Academy of Sciences, 1995
- 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
- Natural ligands of the B cell adhesion molecule CD22 beta can be masked by 9-O-acetylation of sialic acids.The Journal of cell biology, 1994
- The B lymphocyte adhesion molecule CD22 interacts with leukocyte common antigen CD45RO on T cells and α2–6 sialyltransferase, CD75, on B cellsCell, 1991
- The B-cell antigen CD22 mediates monocyte and erythrocyte adhesionNature, 1990
- Site-directed mutagenesis by overlap extension using the polymerase chain reactionGene, 1989
- Molecular cloning of a CD28 cDNA by a high-efficiency COS cell expression system.Proceedings of the National Academy of Sciences, 1987