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http://purl.uniprot.org/citations/9298990http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9298990http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9298990http://www.w3.org/2000/01/rdf-schema#comment"Inhibitory components in myelin are largely responsible for the lack of regeneration in the mammalian CNS. Myelin-associated glycoprotein (MAG), a sialic acid binding protein and a component of myelin, is a potent inhibitor of neurite outgrowth from a variety of neurons both in vitro and in vivo. Here, we show that MAG's sialic acid binding site is distinct from its neurite inhibitory activity. Alone, sialic acid-dependent binding of MAG to neurons is insufficient to effect inhibition of axonal growth. Thus, while soluble MAG-Fc (MAG extracellular domain fused to Fc), a truncated form of MAG-Fc missing Ig-domains 4 and 5, MAG(d1-3)-Fc, and another sialic acid binding protein, sialoadhesin, each bind to neurons in a sialic acid-dependent manner, only full-length MAG-Fc inhibits neurite outgrowth. These results suggest that a second site must exist on MAG which elicits this response. Consistent with this model, mutation of arginine 118 (R118) in MAG to either alanine or aspartate abolishes its sialic acid-dependent binding. However, when expressed at the surface of either CHO or Schwann cells, R118-mutated MAG retains the ability to inhibit axonal outgrowth. Hence, MAG has two recognition sites for neurons, the sialic acid binding site at R118 and a distinct inhibition site which is absent from the first three Ig domains."xsd:string
http://purl.uniprot.org/citations/9298990http://purl.org/dc/terms/identifier"doi:10.1083/jcb.138.6.1355"xsd:string
http://purl.uniprot.org/citations/9298990http://purl.org/dc/terms/identifier"doi:10.1083/jcb.138.6.1355"xsd:string
http://purl.uniprot.org/citations/9298990http://purl.uniprot.org/core/author"Tang S."xsd:string
http://purl.uniprot.org/citations/9298990http://purl.uniprot.org/core/author"Tang S."xsd:string
http://purl.uniprot.org/citations/9298990http://purl.uniprot.org/core/author"Mukhopadhyay G."xsd:string
http://purl.uniprot.org/citations/9298990http://purl.uniprot.org/core/author"Mukhopadhyay G."xsd:string
http://purl.uniprot.org/citations/9298990http://purl.uniprot.org/core/author"Crocker P.R."xsd:string
http://purl.uniprot.org/citations/9298990http://purl.uniprot.org/core/author"Crocker P.R."xsd:string
http://purl.uniprot.org/citations/9298990http://purl.uniprot.org/core/author"Salzer J.L."xsd:string
http://purl.uniprot.org/citations/9298990http://purl.uniprot.org/core/author"Salzer J.L."xsd:string
http://purl.uniprot.org/citations/9298990http://purl.uniprot.org/core/author"Filbin M.T."xsd:string
http://purl.uniprot.org/citations/9298990http://purl.uniprot.org/core/author"Filbin M.T."xsd:string
http://purl.uniprot.org/citations/9298990http://purl.uniprot.org/core/author"DeBellard M.E."xsd:string
http://purl.uniprot.org/citations/9298990http://purl.uniprot.org/core/author"DeBellard M.E."xsd:string
http://purl.uniprot.org/citations/9298990http://purl.uniprot.org/core/author"Shen Y.J."xsd:string
http://purl.uniprot.org/citations/9298990http://purl.uniprot.org/core/author"Shen Y.J."xsd:string
http://purl.uniprot.org/citations/9298990http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9298990http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9298990http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/9298990http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/9298990http://purl.uniprot.org/core/pages"1355-1366"xsd:string
http://purl.uniprot.org/citations/9298990http://purl.uniprot.org/core/pages"1355-1366"xsd:string