A Unique Sugar-binding Site Mediates the Distinct Anti-influenza Activity of Pig Surfactant Protein D
Published 2012 View Full Article
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Title
A Unique Sugar-binding Site Mediates the Distinct Anti-influenza Activity of Pig Surfactant Protein D
Authors
Keywords
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Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 287, Issue 32, Pages 26666-26677
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Online
2012-06-09
DOI
10.1074/jbc.m112.368571
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Note: Only part of the references are listed.- Multimerization of Surfactant Protein D, but Not Its Collagen Domain, Is Required for Antiviral and Opsonic Activities Related to Influenza Virus
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- (2011) Marine L. B. Hillaire et al. PLoS One
- PHENIX: a comprehensive Python-based system for macromolecular structure solution
- (2010) Paul D. Adams et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
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- Seroprevalence and genetic characteristics of five subtypes of influenza A viruses in the Chinese pig population: A pooled data analysis
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- Critical role for cross-linking of trimeric lectin domains of surfactant protein D in antiviral activity against influenza A virus
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- Innate immunity to influenza virus: implications for future therapy
- (2008) Mitchell R White et al. Expert Review of Clinical Immunology
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- Recognition of Heptoses and the Inner Core of Bacterial Lipopolysaccharides by Surfactant Protein D†
- (2007) Hua Wang et al. BIOCHEMISTRY
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