Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus (Q27643010)

inferred from title

author

Marie-Christine Vaney

2

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Margaret Kielian

7

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Armelle Vigouroux

4

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Felix Rey

object named as

Félix A Rey

8

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author name string

Don L Gibbons

1

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Alain Roussel

3

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Brigid Reilly

5

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Jean Lepault

https://api.crossref.org/works/10.1038%2FNATURE02239

6

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language of work or name

English

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publication date

22 January 2004

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published in

Nature

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volume

427

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page(s)

320-5

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issue

6972

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Structural basis for membrane fusion by enveloped viruses

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Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers

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Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events

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Synchronized activation and refolding of influenza hemagglutinin in multimeric fusion machines

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

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The Fusion glycoprotein shell of Semliki Forest virus: an icosahedral assembly primed for fusogenic activation at endosomal pH

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Placement of the structural proteins in Sindbis virus

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The envelope glycoprotein from tick-borne encephalitis virus at 2 A resolution

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A ligand-binding pocket in the dengue virus envelope glycoprotein

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Membrane fusion process of Semliki Forest virus. I: Low pH-induced rearrangement in spike protein quaternary structure precedes virus penetration into cells

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Molecular dissection of the Semliki Forest virus homotrimer reveals two functionally distinct regions of the fusion protein

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The fusion peptide of Semliki Forest virus associates with sterol-rich membrane domains

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Visualization of the target-membrane-inserted fusion protein of Semliki Forest virus by combined electron microscopy and crystallography

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Mechanisms of viral membrane fusion and its inhibition

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Membrane fusion of Semliki Forest virus involves homotrimers of the fusion protein

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HIV-1 envelope proteins complete their folding into six-helix bundles immediately after fusion pore formation

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Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion

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The transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transition

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Truncation of the COOH-terminal region of the paramyxovirus SV5 fusion protein leads to hemifusion but not complete fusion

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Role of the cytoplasmic tail of ecotropic moloney murine leukemia virus Env protein in fusion pore formation

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Rabies virus-induced membrane fusion pathway

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Evolution of intermediates of influenza virus hemagglutinin-mediated fusion revealed by kinetic measurements of pore formation

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Structure of the dengue virus envelope protein after membrane fusion

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Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation

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Purification and crystallization reveal two types of interactions of the fusion protein homotrimer of Semliki Forest virus

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Processing of X-ray diffraction data collected in oscillation mode

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[27] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods.

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Electron-density map interpretation

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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