Research Topics
Genomes and Genes | A AspbergSummaryCountry: Sweden Publications
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Publications
Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and versicanA Aspberg
Department of Cell and Molecular Biology, Section for Connective Tissue Biology, Lund University, P O Box 94, SE 221 00 Lund, Sweden
J Biol Chem 274:20444-9. 1999..No difference in affinity was found for deglycosylated fibulin-1, indicating that the proteoglycan C-type lectin domains bind to the protein part of fibulin-1...
The proteoglycans aggrecan and Versican form networks with fibulin-2 through their lectin domain bindingA I Olin
Department of Cell and Molecular Biology, Section for Connective Tissue Biology, Lund University, BMC Plan C12, SE 221 84 Lund, Sweden
J Biol Chem 276:1253-61. 2001..Electron microscopy confirmed the mapping and demonstrated that hyaluronan-aggrecan complexes can be cross-linked by the fibulins...
Identification and characterization of asporin. a novel member of the leucine-rich repeat protein family closely related to decorin and biglycanP Lorenzo
Department of Cell and Molecular Biology, Section for Connective Tissue Biology, Lund University, BMC Plan C12, SE 221 84 Lund, Sweden
J Biol Chem 276:12201-11. 2001..The name asporin reflects the aspartate-rich amino terminus and the overall similarity to decorin...
The amino-terminal part of PRELP binds to heparin and heparan sulfateE Bengtsson
Department of Cell and Molecular Biology, Section for Connective Tissue Biology, Lund University, Lund, Sweden
J Biol Chem 275:40695-702. 2000..Fibroblasts bind PRELP, and this interaction is inhibited with heparin, suggesting a function for PRELP as a linker between the matrix and cell surface proteoglycans...
The C-type lectin domains of lecticans, a family of aggregating chondroitin sulfate proteoglycans, bind tenascin-R by protein-protein interactions independent of carbohydrate moietyA Aspberg
The Burnham Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA
Proc Natl Acad Sci U S A 94:10116-21. 1997..These results demonstrate that the C-type lectin domain can interact with fibronectin type III domains through protein-protein interactions, and suggest that brevican is a physiological tenascin-R ligand in the adult brain...
