The Structure of the Poxvirus A33 Protein Reveals a Dimer of Unique C-Type Lectin-Like Domains

The Structure of the Poxvirus A33 Protein Reveals a Dimer of Unique C-Type Lectin-Like Domains

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http://www.wikidata.org/entity/Q27658759
Structural and Biochemical Characterization of the Vaccinia Virus Envelope Protein D8 and Its Recognition by the Antibody LA5Homodimerization of the Lymph Vessel Endothelial Receptor LYVE-1 through a Redox-labile Disulfide Is Critical for Hyaluronan Binding in Lymphatic EndotheliumThere is an A33-dependent mechanism for the incorporation of B5-GFP into vaccinia virus extracellular enveloped virions.The inability of vaccinia virus A33R protein to form intermolecular disulfide-bonded homodimers does not affect the production of infectious extracellular virus.Epitope mapping by random peptide phage display reveals essential residues for vaccinia extracellular enveloped virion spread.Identification and characterization of a phage display-derived peptide for orthopoxvirus detection.Structural and Functional Characterization of Anti-A33 Antibodies Reveal a Potent Cross-Species Orthopoxviruses Neutralizer.Increased interaction between vaccinia virus proteins A33 and B5 is detrimental to infectious extracellular enveloped virion production.Unusual features of vaccinia virus extracellular virion form neutralization resistance revealed in human antibody responses to the smallpox vaccine.Vaccinia virus Western Reserve induces rapid surface expression of a host molecule detected by the antibody 4C7 that is distinct from CLEC2D.Membrane fusion during poxvirus entry.Antibody Recognition of Immunodominant Vaccinia Virus Envelope Proteins.A novel bat herpesvirus encodes homologues of major histocompatibility complex classes I and II, C-type lectin, and a unique family of immune-related genes.Vaccinia virus proteins A36 and F12/E2 show strong preferences for different kinesin light chain isoforms.Protein B5 is required on extracellular enveloped vaccinia virus for repulsion of superinfecting virions.Transport and stability of the vaccinia virus A34 protein is affected by the A33 protein.
P2860

The Structure of the Poxvirus A33 Protein Reveals a Dimer of Unique C-Type Lectin-Like Domains

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http://www.wikidata.org/entity/Q27658759
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2010 nî lūn-bûn
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2010 թուականի Մարտին հրատարակուած գիտական յօդուած
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2010 թվականի մարտին հրատարակված գիտական հոդված
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2010年の論文
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2010年論文
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2010年論文
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2010年論文
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2010年論文
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2010年論文
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2010年论文
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name
The Structure of the Poxvirus ...... que C-Type Lectin-Like Domains
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The Structure of the Poxvirus ...... que C-Type Lectin-Like Domains
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The Structure of the Poxvirus ...... que C-Type Lectin-Like Domains
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type
label
The Structure of the Poxvirus ...... que C-Type Lectin-Like Domains
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The Structure of the Poxvirus ...... que C-Type Lectin-Like Domains
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The Structure of the Poxvirus ...... que C-Type Lectin-Like Domains
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prefLabel
The Structure of the Poxvirus ...... que C-Type Lectin-Like Domains
@ast
The Structure of the Poxvirus ...... que C-Type Lectin-Like Domains
@en
The Structure of the Poxvirus ...... que C-Type Lectin-Like Domains
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P1433
P1476
P2093
P2860
P304
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P3181
P356
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P478
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P698
P921
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P1476
The Structure of the Poxvirus ...... que C-Type Lectin-Like Domains
@en
P2093
P2860
P304
P31
P3181
P356
P433
P478
P577
P698
P921
P932