Structure-Function Analysis of Reovirus Binding to Junctional Adhesion Molecule 1

@article{Forrest2003StructureFunctionAO,
  title={Structure-Function Analysis of Reovirus Binding to Junctional Adhesion Molecule 1},
  author={J Craig Forrest and Jacquelyn A. Campbell and Pierre Schelling and Thilo Stehle and Terence S Dermody},
  journal={Journal of Biological Chemistry},
  year={2003},
  volume={278},
  pages={48434 - 48444}
}
  • J Craig Forrest, Jacquelyn A. Campbell, +2 authors Terence S Dermody
  • Published 2003
  • Biology, Medicine
  • Journal of Biological Chemistry
  • Mammalian reoviruses are nonenveloped viruses with a long, filamentous attachment protein that dictates disease phenotypes following infection of newborn mice and is a structural homologue of the adenovirus attachment protein. Reoviruses use junctional adhesion molecule 1 (JAM1) as a serotype-independent cellular receptor. JAM1 is a broadly expressed immunoglobulin superfamily protein that forms stable homodimers and regulates tight-junction permeability and lymphocyte trafficking. We employed… CONTINUE READING

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