HN Protein

"HN Protein" 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.

MeSH information

Definition | Details | More General Concepts | Related Concepts | More Specific Concepts

Glycoprotein from Sendai, para-influenza, Newcastle Disease, and other viruses that participates in binding the virus to cell-surface receptors. The HN protein possesses both hemagglutinin and neuraminidase activity.

Descriptor ID

D015707

MeSH Number(s)

D12.776.964.970.880.350

D23.050.327.461.350

Concept/Terms

HN Protein

HN Glycoprotein, Sendai Virus

Below are MeSH descriptors whose meaning is more general than "HN Protein".

Chemicals and Drugs [D]
Amino Acids, Peptides, and Proteins [D12]
Proteins [D12.776]
Viral Proteins [D12.776.964]
Viral Structural Proteins [D12.776.964.970]
Viral Envelope Proteins [D12.776.964.970.880]
HN Protein [D12.776.964.970.880.350]
Biological Factors [D23]
Antigens [D23.050]
Antigens, Viral [D23.050.327]
Hemagglutinins, Viral [D23.050.327.461]
HN Protein [D23.050.327.461.350]

Below are MeSH descriptors whose meaning is related to "HN Protein".

Below are MeSH descriptors whose meaning is more specific than "HN Protein".

publications

Timeline | Most Recent

This graph shows the total number of publications written about "HN Protein" by people in Harvard Catalyst Profiles by year, and whether "HN Protein" was a major or minor topic of these publication.

Bar chart showing 4 publications over 3 distinct years, with a maximum of 2 publications in 2001

To see the data from this visualization as text, click here.

Year	Major Topic	Total
1998	1	1
2001	2	2
2003	1	1

Below are the most recent publications written about "HN Protein" by people in Profiles.

Fusion activation through attachment protein stalk domains indicates a conserved core mechanism of paramyxovirus entry into cells. J Virol. 2014 Apr; 88(8):3925-41.

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Mutations in the parainfluenza virus 5 fusion protein reveal domains important for fusion triggering and metastability. J Virol. 2013 Dec; 87(24):13520-31.

View in: PubMed
Structure of the parainfluenza virus 5 (PIV5) hemagglutinin-neuraminidase (HN) ectodomain. PLoS Pathog. 2013; 9(8):e1003534.

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Fusion activation by a headless parainfluenza virus 5 hemagglutinin-neuraminidase stalk suggests a modular mechanism for triggering. Proc Natl Acad Sci U S A. 2012 Sep 25; 109(39):E2625-34.

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Structure and mutagenesis of the parainfluenza virus 5 hemagglutinin-neuraminidase stalk domain reveals a four-helix bundle and the role of the stalk in fusion promotion. J Virol. 2011 Dec; 85(24):12855-66.

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Newcastle disease virus-like particles containing respiratory syncytial virus G protein induced protection in BALB/c mice, with no evidence of immunopathology. J Virol. 2010 Jan; 84(2):1110-23.

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In vitro and in vivo characterization of new swine-origin H1N1 influenza viruses. Nature. 2009 Aug 20; 460(7258):1021-5.

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Over-expression of mammalian sialidase NEU3 reduces Newcastle disease virus entry and propagation in COS7 cells. Biochim Biophys Acta. 2008 Mar; 1780(3):504-12.

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IL-13 is sufficient for respiratory syncytial virus G glycoprotein-induced eosinophilia after respiratory syncytial virus challenge. J Immunol. 2003 Feb 15; 170(4):2037-45.

View in: PubMed
Haemagglutinating activity of the lentogenic Newcastle disease virus strain MET95. Avian Pathol. 2003 Feb; 32(1):39-45.

View in: PubMed

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