Probing the Spatial Organization of Measles Virus Fusion Complexes

No abstract is available for this paper.

• Publication year

  2009

• Venue

  Journal of Virology

• Publication date

  2009-08-05

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1128/JVI.01195-09PMID 19656895PMCID PMC2753148
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• A Novel Receptor-induced Activation Site in the Nipah Virus Attachment Glycoprotein (G) Involved in Triggering the Fusion Glycoprotein (F)*

  2009cited by this paper
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• N-Glycans on Nipah Virus Fusion Protein Protect against Neutralization but Reduce Membrane Fusion and Viral Entry

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• Addition of N-Glycans in the Stalk of the Newcastle Disease Virus HN Protein Blocks Its Interaction with the F Protein and Prevents Fusion

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• Single-Chain Antibody Displayed on a Recombinant Measles Virus Confers Entry through the Tumor-Associated Carcinoembryonic Antigen

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• Evidence That the Transition of HIV-1 Gp41 into a Six-Helix Bundle, Not the Bundle Configuration, Induces Membrane Fusion

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• Clinical Isolates of Measles Virus Use CD46 as a Cellular Receptor

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• Observation of Measles Virus Cell-to-Cell Spread in Astrocytoma Cells by Using a Green Fluorescent Protein-Expressing Recombinant Virus

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  1999cited by this paper
• Mutations in the Newcastle disease virus hemagglutinin-neuraminidase protein that interfere with its ability to interact with the homologous F protein in the promotion of fusion.

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