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Anders Aspberg

Researcher at Lund University

Publications -  56
Citations -  3701

Anders Aspberg is an academic researcher from Lund University. The author has contributed to research in topics: Aggrecan & C-type lectin. The author has an hindex of 25, co-authored 51 publications receiving 3423 citations. Previous affiliations of Anders Aspberg include University of Copenhagen & National Foundation for Cancer Research.

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BookDOI

Glycosylated matrix protein

TL;DR: This chapter focuses on cartilage and bone, covering many aspects of connective tissues, and gives special focus to the noncollagenous proteins in their matrices.
Journal ArticleDOI

The C-type lectin domains of lecticans, a family of aggregating chondroitin sulfate proteoglycans, bind tenascin-R by protein-protein interactions independent of carbohydrate moiety.

TL;DR: It is demonstrated 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.
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Identification and characterization of asporin. a novel member of the leucine-rich repeat protein family closely related to decorin and biglycan.

TL;DR: The deduced amino acid sequence of asporin was confirmed by mass spectrometry of the isolated protein resulting in 84% sequence coverage and reflects the aspartate-rich amino terminus and the overall similarity to decorin.
Journal ArticleDOI

Versican interacts with fibrillin-1 and links extracellular microfibrils to other connective tissue networks

TL;DR: Electro microscopic immunolocalization of anti-versican antibodies in tissues and in extracted microfibrils demonstrated that the C-terminal region of versican is found associated with fibrillin microfibils, suggesting that the versican C terminus is covalently bound to microFibrils.
Journal ArticleDOI

Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and versican.

TL;DR: It is reported that a 90-kDa protein copurifies with recombinant lectin domains from aggrecan and versican, but not from the brain-specific neurocan and brevican, although the interactions with fibulin-1 are Ca2+-dependent, withK D values in the low nanomolar range.