Structure of Epstein-Barr Virus Glycoprotein 42 Suggests a Mechanism for Triggering Receptor-Activated Virus Entry
- 1 February 2009
- Vol. 17 (2) , 223-233
- https://doi.org/10.1016/j.str.2008.12.010
Abstract
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This publication has 39 references indexed in Scilit:
- Engineered Disulfide Bonds in Herpes Simplex Virus Type 1 gD Separate Receptor Binding from Fusion Initiation and Viral EntryJournal of Virology, 2008
- Binding-Site Interactions between Epstein-Barr Virus Fusion Proteins gp42 and gH/gL Reveal a Peptide That Inhibits both Epithelial and B-Cell Membrane FusionJournal of Virology, 2007
- Polyspecificity of T cell and B cell receptor recognitionPublished by Elsevier ,2007
- Herpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and BProceedings of the National Academy of Sciences, 2007
- Soluble Epstein-Barr Virus Glycoproteins gH, gL, and gp42 Form a 1:1:1 Stable Complex That Acts Like Soluble gp42 in B-Cell Fusion but Not in Epithelial Cell FusionJournal of Virology, 2006
- Solvent content of protein crystalsPublished by Elsevier ,2006
- Coot: model-building tools for molecular graphicsActa Crystallographica Section D-Biological Crystallography, 2004
- Refinement of Macromolecular Structures by the Maximum-Likelihood MethodActa Crystallographica Section D-Biological Crystallography, 1997
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Improvement of macromolecular electron-density maps by the simultaneous application of real and reciprocal space constraintsActa Crystallographica Section D-Biological Crystallography, 1993