Characterization of a Functional Hyaluronan-Binding Domain from the Human CD44 Molecule Expressed inEscherichia coli
- 1 December 1998
- journal article
- Published by Elsevier in Protein Expression and Purification
- Vol. 14 (3) , 371-381
- https://doi.org/10.1006/prep.1998.0971
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
- Identification of CD44 Residues Important for Hyaluronan Binding and Delineation of the Binding SiteJournal of Biological Chemistry, 1998
- Solution Structure of the Link Module: A Hyaluronan-Binding Domain Involved in Extracellular Matrix Stability and Cell MigrationCell, 1996
- Glycosylation of CD44 is implicated in CD44-mediated cell adhesion to hyaluronan.The Journal of cell biology, 1996
- CD44 and its ligand hyaluronate mediate rolling under physiologic flow: a novel lymphocyte-endothelial cell primary adhesion pathway.The Journal of Experimental Medicine, 1996
- Variant cell lines selected for alterations in the function of the hyaluronan receptor CD44 show differences in glycosylation.The Journal of Experimental Medicine, 1995
- Glycosylation of CD44 negatively regulates its recognition of hyaluronan.The Journal of Experimental Medicine, 1995
- Proteoglycan forms of the lymphocyte homing receptor CD44 are alternatively spliced variants containing the v3 exon.The Journal of cell biology, 1995
- A new variant of glycoprotein CD44 confers metastatic potential to rat carcinoma cellsCell, 1991
- CD44 is the principal cell surface receptor for hyaluronateCell, 1990
- A human lymphocyte homing receptor, the Hermes antigen, is related to cartilage proteoglycan core and link proteinsCell, 1989