"Viral Fusion Proteins" 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.
Proteins, usually glycoproteins, found in the viral envelopes of a variety of viruses. They promote cell membrane fusion and thereby may function in the uptake of the virus by cells.
| Descriptor ID |
D014760
|
| MeSH Number(s) |
D12.776.543.512.500 D12.776.964.970.880.910
|
| Concept/Terms |
Viral Fusion Proteins- Viral Fusion Proteins
- Virus Fusion Proteins
- Fusion Proteins, Virus
- Proteins, Virus Fusion
- Fusion Proteins, Viral
Viral Fusion Glycoproteins- Viral Fusion Glycoproteins
- Fusion Glycoproteins, Viral
- Glycoproteins, Viral Fusion
- Glycoprotein, Viral Fusion
- Viral Fusion-GP
- Fusion-GP, Viral
- Viral Fusion GP
- Fusion Glycoprotein, Viral
- Viral Fusion Glycoprotein
|
Below are MeSH descriptors whose meaning is more general than "Viral Fusion Proteins".
Below are MeSH descriptors whose meaning is more specific than "Viral Fusion Proteins".
This graph shows the total number of publications written about "Viral Fusion Proteins" by people in this website by year, and whether "Viral Fusion Proteins" was a major or minor topic of these publications.
To see the data from this visualization as text,
click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1995 | 1 | 0 | 1 |
| 1996 | 1 | 0 | 1 |
| 1998 | 2 | 0 | 2 |
| 2003 | 0 | 1 | 1 |
| 2004 | 1 | 0 | 1 |
| 2005 | 3 | 0 | 3 |
| 2006 | 2 | 0 | 2 |
| 2007 | 3 | 0 | 3 |
| 2009 | 1 | 1 | 2 |
| 2012 | 3 | 0 | 3 |
| 2013 | 1 | 2 | 3 |
| 2014 | 2 | 1 | 3 |
| 2015 | 1 | 1 | 2 |
| 2016 | 4 | 1 | 5 |
| 2017 | 3 | 1 | 4 |
| 2018 | 4 | 0 | 4 |
| 2019 | 2 | 0 | 2 |
| 2020 | 0 | 2 | 2 |
| 2021 | 2 | 3 | 5 |
| 2023 | 0 | 4 | 4 |
| 2024 | 1 | 1 | 2 |
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Below are the most recent publications written about "Viral Fusion Proteins" by people in Profiles.
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Functional and structural basis of human parainfluenza virus type 3 neutralization with human monoclonal antibodies. Nat Microbiol. 2024 Aug; 9(8):2128-2143.
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Potent HPIV3-neutralizing IGHV5-51 Antibodies Identified from Multiple Individuals Show L Chain and CDRH3 Promiscuity. J Immunol. 2024 May 01; 212(9):1450-1456.
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Potent cross-neutralization of respiratory syncytial virus and human metapneumovirus through a structurally conserved antibody recognition mode. Cell Host Microbe. 2023 08 09; 31(8):1288-1300.e6.
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Development of a Kinetic ELISA and Reactive B Cell Frequency Assay to Detect Respiratory Syncytial Virus Pre-Fusion F Protein-Specific Immune Responses in Infants. J Pediatric Infect Dis Soc. 2023 May 31; 12(5):298-305.
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The Efficiency of p27 Cleavage during In Vitro Respiratory Syncytial Virus (RSV) Infection Is Cell Line and RSV Subtype Dependent. J Virol. 2023 05 31; 97(5):e0025423.
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Diversity and evolution of computationally predicted T cell epitopes against human respiratory syncytial virus. PLoS Comput Biol. 2023 Jan; 19(1):e1010360.
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Antibody responses of healthy adults to the p27 peptide of respiratory syncytial virus fusion protein. Vaccine. 2022 01 24; 40(3):536-543.
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Herpesvirus Nuclear Egress across the Outer Nuclear Membrane. Viruses. 2021 11 24; 13(12).
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Profile of respiratory syncytial virus prefusogenic fusion protein nanoparticle vaccine. Expert Rev Vaccines. 2021 04; 20(4):351-364.
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Potent neutralization of Rift Valley fever virus by human monoclonal antibodies through fusion inhibition. Proc Natl Acad Sci U S A. 2021 04 06; 118(14).