Viral Fusion Proteins
"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
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MeSH Number(s) |
D12.776.543.512.500 D12.776.964.970.880.910
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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
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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 |
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1986 | 1 | 0 | 1 | 1987 | 0 | 2 | 2 | 1988 | 1 | 1 | 2 | 1991 | 1 | 0 | 1 | 1992 | 2 | 0 | 2 | 1993 | 3 | 0 | 3 | 1994 | 1 | 1 | 2 | 1995 | 3 | 0 | 3 | 1997 | 2 | 1 | 3 | 1998 | 2 | 0 | 2 | 1999 | 2 | 0 | 2 | 2000 | 1 | 1 | 2 | 2001 | 4 | 0 | 4 | 2002 | 1 | 0 | 1 | 2003 | 4 | 0 | 4 | 2004 | 2 | 1 | 3 | 2005 | 2 | 0 | 2 | 2006 | 3 | 1 | 4 | 2007 | 2 | 0 | 2 | 2008 | 4 | 0 | 4 | 2009 | 1 | 1 | 2 | 2010 | 1 | 1 | 2 | 2011 | 3 | 0 | 3 | 2012 | 2 | 0 | 2 | 2013 | 1 | 0 | 1 | 2014 | 2 | 0 | 2 | 2015 | 1 | 0 | 1 |
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Below are the most recent publications written about "Viral Fusion Proteins" by people in Profiles.
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McGinnes Cullen L, Schmidt MR, Kenward SA, Woodland RT, Morrison TG. Murine immune responses to virus-like particle-associated pre- and postfusion forms of the respiratory syncytial virus F protein. J Virol. 2015 Jul; 89(13):6835-47.
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Schmidt MR, McGinnes-Cullen LW, Kenward SA, Willems KN, Woodland RT, Morrison TG. Modification of the respiratory syncytial virus f protein in virus-like particles impacts generation of B cell memory. J Virol. 2014 Sep 1; 88(17):10165-76.
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Wei Y, Zhang Y, Cai H, Mirza AM, Iorio RM, Peeples ME, Niewiesk S, Li J. Roles of the putative integrin-binding motif of the human metapneumovirus fusion (f) protein in cell-cell fusion, viral infectivity, and pathogenesis. J Virol. 2014 Apr; 88(8):4338-52.
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Mirza AM, Iorio RM. A mutation in the stalk of the newcastle disease virus hemagglutinin-neuraminidase (HN) protein prevents triggering of the F protein despite allowing efficient HN-F complex formation. J Virol. 2013 Aug; 87(15):8813-5.
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Wei Y, Feng K, Yao X, Cai H, Li J, Mirza AM, Iorio RM, Li J. Localization of a region in the fusion protein of avian metapneumovirus that modulates cell-cell fusion. J Virol. 2012 Nov; 86(21):11800-14.
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Aguilar HC, Iorio RM. Henipavirus membrane fusion and viral entry. Curr Top Microbiol Immunol. 2012; 359:79-94.
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Postler TS, Martinez-Navio JM, Yuste E, Desrosiers RC. Evidence against extracellular exposure of a highly immunogenic region in the C-terminal domain of the simian immunodeficiency virus gp41 transmembrane protein. J Virol. 2012 Jan; 86(2):1145-57.
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Mahon PJ, Mirza AM, Iorio RM. Role of the two sialic acid binding sites on the newcastle disease virus HN protein in triggering the interaction with the F protein required for the promotion of fusion. J Virol. 2011 Nov; 85(22):12079-82.
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Côté M, Misasi J, Ren T, Bruchez A, Lee K, Filone CM, Hensley L, Li Q, Ory D, Chandran K, Cunningham J. Small molecule inhibitors reveal Niemann-Pick C1 is essential for Ebola virus infection. Nature. 2011 Aug 24; 477(7364):344-8.
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Plemper RK, Brindley MA, Iorio RM. Structural and mechanistic studies of measles virus illuminate paramyxovirus entry. PLoS Pathog. 2011 Jun; 7(6):e1002058.
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