|1.||Garry, Robert F: 2 articles (01/2013 - 01/2004)|
|2.||Nunberg, Jack H: 2 articles (01/2012 - 12/2005)|
|3.||York, Joanne: 2 articles (01/2012 - 12/2005)|
|4.||Hong, Mei: 1 article (09/2015)|
|5.||Yao, Hongwei: 1 article (09/2015)|
|6.||Lee, Michelle W: 1 article (09/2015)|
|7.||Waring, Alan J: 1 article (09/2015)|
|8.||Wong, Gerard C L: 1 article (09/2015)|
|9.||Enquist, Lynn W: 1 article (09/2013)|
|10.||Granstedt, Andrea E: 1 article (09/2013)|
01/01/2013 - "Finally, we illuminate key unanswered questions and suggest how further studies can elucidate how this clinically important paramyxovirus fusion protein may have evolved to initiate infection by a unique mechanism."
09/10/2013 - "We propose that the viral fusion proteins produced by virulent PRV infection induce electrical coupling in unmyelinated axons in vivo. "
01/01/1999 - "Best understood are the viral fusion proteins that are responsible for merging the viral with the host cell membrane during infection. "
03/01/1994 - "Proteolytic cleavage is common for activation of viral fusion proteins, and it has been shown that herpesvirus gB homologs are essential for membrane fusion events during infection, e.g., virus penetration and direct viral cell-to-cell spread. "
03/09/2012 - "Peptides corresponding to N- and C-terminal heptad repeat regions (HR1 and HR2, respectively) of viral fusion proteins can block infection of viruses in a dominant negative manner by interfering with refolding of the viral HR1 and HR2 to form a six-helix bundle (6HB) that drives fusion between viral and host cell membranes. "
12/20/2005 - "These findings support the inclusion of the arenavirus GP-C among the Class I viral fusion proteins and suggest pharmacologic and immunologic strategies for targeting arenavirus infection and hemorrhagic fever."
01/01/2012 - "Through our studies of the GPC envelope glycoprotein of the hemorrhagic fever arenaviruses, we have shown that GPC is unique among class I viral fusion proteins in that the mature complex retains a stable signal peptide (SSP) in addition to the conventional receptor-binding and transmembrane fusion subunits. "
|3.||Human Influenza (Influenza)
05/26/1998 - "Electron microscopy indicates that Gp2 folds into a rod-like structure like influenza HA2 and HIV-1 gp41, providing further evidence that viral fusion proteins from diverse families such as Orthomyxoviridae (Influenza), Retroviridae (HIV-1), and Filoviridae (Ebola) share common structural features, and suggesting a common membrane fusion mechanism."
09/01/2015 - "The C-terminal transmembrane domain (TMD) of viral fusion proteins such as HIV gp41 and influenza hemagglutinin (HA) is traditionally viewed as a passive α-helical anchor of the protein to the virus envelope during its merger with the cell membrane. "
12/01/2003 - "Class I viral fusion proteins, including HIV Env and influenza hemagglutinin (HA), form six-helix bundles in their fusogenic forms. "
08/01/2007 - "The group of class I viral fusion proteins includes the influenza hemagglutinin, paramyxovirus F, HIV env, and other mechanistically related fusogens, but these proteins are unrelated in sequence and exhibit clearly distinct structural features. "
09/01/1997 - "The mechanisms of merger of lipid bilayers of two membranes mediated by influenza hemagglutinin and other viral fusion proteins apparently involve local lipidic connections that evolve into a bilayer septum in which a pore forms and expands."
01/01/2013 - "Further, we show that infectivity can be inhibited for diverse, unrelated RNA viruses that have Class I (Ebola virus), Class II (Andes virus), or Class III (vesicular stomatitis virus) fusion proteins using this single peptide. "
01/01/2010 - "The background levels were lower compared to alternative strategies involving Sindbis virus strain TR339 or vesicular stomatitis virus fusion proteins."
11/01/2012 - "Vesicular stomatitis virus glycoprotein G (VSV-G) belongs to a new class of viral fusion proteins (Class III). "
|5.||Severe Acute Respiratory Syndrome
|2.||Protein Sorting Signals (Signal Peptide)
|4.||Proteins (Proteins, Gene)
|6.||Staphylococcal Protein A (A, Protein)
|7.||Lipid Bilayers (Lipid Bilayer)