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Fusion inhibition: Bioassay of a Type C viral protein
Virology, 1975Abstract Based on the observation that concentrated RD-114 virus directly induces fusion in a Rous sarcoma virus-transformed human glioma cell line, KC, an RD-114 virus protein was identified which had the property of inhibiting this fusion. The protein was irreversibly denatured by 2-mercaptoethanol, reacted with neutralizing sera to RD-114 virus ...
James Davis +4 more
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Pore Formation in Target Liposomes by Viral Fusion Proteins
2003Publisher Summary This chapter introduces methodologies to characterize plasma-membrane and viral-membrane interactions in a model system using liposomes as target membranes. It focuses on hemagglutinin (HA), a trimeric integral membrane protein that protrudes from the viral membrane as a spike, with a long stem and a globular tip.
Pierre Bonnafous, Toon Stegmann
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Virology, 1994
Wild-type vaccinia virus WR strain forms non-fusogenic (F-) large plaques and is hemagglutinin positive (HA+) under normal conditions of virus infection. We have analyzed a collection of spontaneous, highly attenuated mutants of vaccinia virus isolated from persistently infected Friend erythroleukemia cells (E. Paez, S. Dallo, and M. Esteban, J. Virol.
Eduardo Paez, María Ortiz
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Wild-type vaccinia virus WR strain forms non-fusogenic (F-) large plaques and is hemagglutinin positive (HA+) under normal conditions of virus infection. We have analyzed a collection of spontaneous, highly attenuated mutants of vaccinia virus isolated from persistently infected Friend erythroleukemia cells (E. Paez, S. Dallo, and M. Esteban, J. Virol.
Eduardo Paez, María Ortiz
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A Dissection of Steps Leading to Viral Envelope Protein‐Mediated Membrane Fusion
Annals of the New York Academy of Sciences, 1991increase in [Ca”] at the presynaptic nerve terminal sets a complex set of biochemical events in motion that finally terminates in the specific fusion of the membrane of the secretory vesicle with the plasma membrane.’ In studying the action of CaZ+ at the presynaptic terminal a distinction has to be made between processes that occur in the cytosol that
Christian Schoch +3 more
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Delivery of Macromolecules into Cells Expressing a Viral Membrane Fusion Protein
1989Publisher Summary This chapter reviews a macromolecular delivery technique that employs cells that express a potent membrane fusion protein, the influenza virus hemagglutinin (HA). Briefly, the protein or nucleic acid of interest is loaded into either red blood cells (RBC) or liposomes.
Judith M. White +3 more
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Role of the N-terminal peptides of viral envelope proteins in membrane fusion
Advanced Drug Delivery Reviews, 1999Membrane fusion is an important biological process that is observed in a wide variety of intra and intercellular events. In this review, work done in the last few years on the molecular mechanism of viral membrane fusion is highlighted, focusing in particular on the role of the fusion peptide and the modification of the lipid bilayer structure.
Martin, Isabelle +2 more
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Mechanism and energetics of lipid recognition by viral fusion proteins
2023During viral infection, viral fusion proteins bind to the host cell membrane prior to catalyzing the fusion of the viral envelope with the host membrane. The atomic architectures of fusion proteins and their interactions with membrane receptors have been revealed by numerous structural studies, however, the interactions of fusion proteins with the host
Poojari, Chetan +2 more
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Patch clamp studies of single cell-fusion events mediated by a viral fusion protein
Nature, 1989To enter cells, viruses must fuse their envelope with a host cell membrane. Fusion is mediated by specific, membrane-spanning fusion proteins, of which the influenza virus haemagglutinins (HA) are the best characterized. Several HAs have been sequenced, and the crystal structure of the major part of one HA is known.
J. M. White +3 more
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Probing the Function of Viral Fusion Proteins with Synthetic Peptides
1987Synthetic peptides offer several unique approaches to studying molecular and cellular interactions. Not only do these peptides provide A. large quantity of material for experimental analysis, but they also offer A. degree of homogeneity that is difficult to obtain through routine biochemical purification.
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Structural comparison of three viral “fusion” proteins
Biochemical Society Transactions, 1991Mahmoud Naase, Bruce H. Nicholson
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