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Lecticans, a family of hyaluronan binding proteoglycans, are represented by aggrecan (ACAN), versican (VCAN), neurocan (NCAN), and brevican (BCAN) [ 4, 6] and have an important role in neuronal growth mechanisms represented by neuroplasticity, axon guidance, or neuron repair processes following injury to the spinal cord or brain [ 4, 7– 9].
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Examples of this action are represented by fibronectin, vitronectin, collagens and proteoglycans, which bind FGFs, HGFs, VEGFs, BMPs and TGF-β.
In has been reported that in the in vivo infection process the first HPV binding site is represented by the basal membrane (BM) through an heparan sulphate proteoglycan (HSPG -dependent binding mecHSPG -dependent
The binding mode of 5l is represented in Fig. 1a.
A collagen fiber is represented by a bundle of proteoglycan cross-linked collagen fibrils that undergoes irreversible deformations when exceeding its elastic tensile limit.
The ligand binding to proteoglycans is extremely complex because proteoglycans carry multiple GAG chains that may function cooperatively.
Proteoglycans are known to act both as primary receptors and as co-receptors that facilitate binding of agonists to other receptors, and thus, the involvement of other receptors for HBP remains a possibility [32, 34].
It is known that proteoglycans are high-molecular-weight glycoproteins and interact via their multiple binding domains with many other structural macromolecules.
The major endothelial cell surface proteoglycans are syndecans, which are heparan sulfate proteoglycans.
The photolysis achieved with RBCs would therefore suggest that binding to heparan sulfate proteoglycans is not required for efficient photosensitization and that other membrane interactions are involved.
Recombinant APRIL binds to several cell lines that do not express detectable mRNA for TACI and BCMA and proteoglycans were identified as APRIL-specific binding partners.
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