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The Journal of Neuroscience, June 1, 2005, ():

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Nogo-A Interacts with the Nogo-66 Receptor through Multiple Sites to Create an Isoform-Selective Subnanomolar Agonist
J. Neurosci. Hu et al. 25: 5298

Supplemental Data

Files in this Data Supplement:

  • supplemental material - Suppl. Fig. 1 Model for NgR signaling. Both Nogo-A-24 and Nogo-66 bind to the LRR domain of NgR. Binding of Nogo-A-24 to NgR does not signal to inhibit outgrowth but the presence of both Nogo-A-24 and Nogo-66 in Nogo makes Nogo a high affinity agonist for NgR. Δ20 region of Amino-Nogo does not bind to NgR but inhibits fibroblast spreading and neurite outgrowth, probably through an unidentified receptor present in multiple cell types. The amino terminal domain of Nogo-B might act through another unidentified receptor to regulate vascular remodeling.



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