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Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2010, Volume 107, Issue 52, pp. 22641 - 22646
The Epstein-Barr virus (EBV) is a γ-herpesvirus that infects B cells and epithelial cells and that has been linked to malignancies in both cell types in vivo.... 
Proteins | Epithelial cells | B lymphocytes | Herpesviridae | Human herpesvirus 2 | Viruses | Glycoproteins | Epstein Barr virus infections | Human herpesvirus 4 | Integrins | B-CELLS | GH | EPITHELIAL-CELLS | GL | FORM | GP42 | MULTIDISCIPLINARY SCIENCES | MEMBRANE-FUSION PROTEINS | MUTATIONS | REVEAL | BINDING | Disulfides - metabolism | Herpesvirus 4, Human - genetics | Molecular Chaperones - metabolism | Membrane Glycoproteins - metabolism | Humans | Membrane Glycoproteins - chemistry | Protein Multimerization | Molecular Sequence Data | Molecular Chaperones - chemistry | Viral Proteins - metabolism | Cysteine - genetics | Spodoptera | Multiprotein Complexes - metabolism | Disulfides - chemistry | Viral Envelope Proteins - metabolism | Cysteine - metabolism | Protein Structure, Tertiary | Amino Acid Sequence | Cell Line | Viral Envelope Proteins - genetics | Membrane Fusion | Viral Proteins - chemistry | Crystallization | Molecular Chaperones - genetics | Models, Molecular | Viral Proteins - genetics | Binding Sites - genetics | Cysteine - chemistry | Microscopy, Electron | Membrane Glycoproteins - genetics | Sequence Homology, Amino Acid | Multiprotein Complexes - ultrastructure | Multiprotein Complexes - chemistry | Animals | Viral Envelope Proteins - chemistry | Protein Binding | Herpesvirus 4, Human - metabolism | Virus diseases | Epstein-Barr virus | Research | Chemical properties | Structure | Crystals | Biological Sciences
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 10/2012, Volume 109, Issue 41, pp. 16672 - 16677
Journal Article
Nature Communications, ISSN 2041-1723, 05/2016, Volume 7, Issue 1, p. 11610
Omalizumab is a widely used therapeutic anti-IgE antibody. Here we report the crystal structure of the omalizumab-Fab in complex with an IgE-Fc fragment. This... 
HIGH-AFFINITY RECEPTOR | DISSOCIATION | EPSILON-RI EXPRESSION | MULTIDISCIPLINARY SCIENCES | IN-VIVO | MAST-CELLS | CONFORMATIONAL FLEXIBILITY | ANTIBODY | BINDING | CD23 | IMMUNOGLOBULIN-E | BASIC BIOLOGICAL SCIENCES
Journal Article