(Q27631190)

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M W Wien

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J Navaza

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S D Fuller

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G Wengler

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F A Rey

The nucleocapsid-binding spike subunit E2 of Semliki Forest virus requires complex formation with the E1 subunit for activity

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language of work or name

English

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publication date

6 April 2001

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published in

Cell

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volume

105

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issue

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page(s)

137-48

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cites work

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Nucleocapsid and glycoprotein organization in an enveloped virus

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Structural intermediates in influenza haemagglutinin-mediated fusion

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Structure of Semliki Forest virus core protein

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Membrane fusion activity of tick-borne encephalitis virus and recombinant subviral particles in a liposomal model system

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The first step: activation of the Semliki Forest virus spike protein precursor causes a localized conformational change in the trimeric spike.

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Molecular organization of a recombinant subviral particle from tick-borne encephalitis virus

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Membrane proteins organize a symmetrical virus

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Low pH induces swiveling of the glycoprotein heterodimers in the Semliki Forest virus spike complex

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Formation and characterization of the trimeric form of the fusion protein of Semliki Forest Virus

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Semlike Forest virus membrane proteins. Preparation and characterization of spike complexes soluble in detergent-free medium

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On the entry of Semliki forest virus into BHK-21 cells

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Membrane fusion and exocytosis

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Cryo-Electron Microscopy Reveals the Functional Organization of an Enveloped Virus, Semliki Forest Virus

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Semliki forest virus particles containing only the E1 envelope glycoprotein are infectious and can induce cell-cell fusion

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Structural Localization of the E3 Glycoprotein in Attenuated Sindbis Virus Mutants

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