Hemagglutinin Glycoproteins, Influenza Virus
"Hemagglutinin Glycoproteins, Influenza Virus" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Membrane glycoproteins from influenza viruses which are involved in hemagglutination, virus attachment, and envelope fusion. Fourteen distinct subtypes of HA glycoproteins and nine of NA glycoproteins have been identified from INFLUENZA A VIRUS; no subtypes have been identified for Influenza B or Influenza C viruses.
Descriptor ID |
D019267
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MeSH Number(s) |
D12.776.964.970.880.345.500
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Concept/Terms |
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Below are MeSH descriptors whose meaning is more general than "Hemagglutinin Glycoproteins, Influenza Virus".
Below are MeSH descriptors whose meaning is more specific than "Hemagglutinin Glycoproteins, Influenza Virus".
This graph shows the total number of publications written about "Hemagglutinin Glycoproteins, Influenza Virus" by people in this website by year, and whether "Hemagglutinin Glycoproteins, Influenza Virus" was a major or minor topic of these publications.
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Year | Major Topic | Minor Topic | Total |
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1999 | 2 | 0 | 2 |
2000 | 2 | 0 | 2 |
2001 | 2 | 0 | 2 |
2003 | 1 | 1 | 2 |
2013 | 0 | 1 | 1 |
2016 | 1 | 0 | 1 |
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Below are the most recent publications written about "Hemagglutinin Glycoproteins, Influenza Virus" by people in Profiles.
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The hemifusion structure induced by influenza virus haemagglutinin is determined by physical properties of the target membranes. Nat Microbiol. 2016 04 18; 1(6):16050.
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IFITM proteins restrict viral membrane hemifusion. PLoS Pathog. 2013 Jan; 9(1):e1003124.
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Nanodisc-incorporated hemagglutinin provides protective immunity against influenza virus infection. J Virol. 2010 Jan; 84(1):361-71.
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Completion of trimeric hairpin formation of influenza virus hemagglutinin promotes fusion pore opening and enlargement. Virology. 2003 Nov 25; 316(2):234-44.
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Induction of tumor cell apoptosis in vivo increases tumor antigen cross-presentation, cross-priming rather than cross-tolerizing host tumor-specific CD8 T cells. J Immunol. 2003 May 15; 170(10):4905-13.
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Implications of a fusion peptide structure. Nat Struct Biol. 2001 Aug; 8(8):653-5.
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Evolution of intermediates of influenza virus hemagglutinin-mediated fusion revealed by kinetic measurements of pore formation. Biophys J. 2001 Feb; 80(2):812-21.
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A point mutation in the transmembrane domain of the hemagglutinin of influenza virus stabilizes a hemifusion intermediate that can transit to fusion. Mol Biol Cell. 2000 Nov; 11(11):3765-75.
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The lipid-anchored ectodomain of influenza virus hemagglutinin (GPI-HA) is capable of inducing nonenlarging fusion pores. Mol Biol Cell. 2000 Apr; 11(4):1143-52.
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A specific point mutant at position 1 of the influenza hemagglutinin fusion peptide displays a hemifusion phenotype. Mol Biol Cell. 1999 Aug; 10(8):2759-69.