Hydrophobic and Charged Residues in the Central Segment of the Measles Virus Hemagglutinin Stalk Mediate Transmission of the Fusion-Triggering Signal
Author:
Affiliation:
1. Department of Molecular Medicine, Mayo Clinic, and Virology and Gene Therapy Track, Mayo Graduate School, Rochester, Minnesota, USA
Abstract
Publisher
American Society for Microbiology
Subject
Virology,Insect Science,Immunology,Microbiology
Link
https://journals.asm.org/doi/pdf/10.1128/JVI.01547-13
Reference16 articles.
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2. Targeted entry of enveloped viruses: measles and herpes simplex virus I;Navaratnarajah CK;Curr. Opin. Virol.,2012
3. Crystal structure of measles virus hemagglutinin provides insight into effective vaccines
4. Membrane fusion triggering: three modules with different structure and function in the upper half of the measles virus attachment protein stalk J;Navaratnarajah CK;Biol. Chem.,2012
5. The Measles Virus Hemagglutinin β-Propeller Head β4-β5 Hydrophobic Groove Governs Functional Interactions with Nectin-4 and CD46 but Not Those with the Signaling Lymphocytic Activation Molecule
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