A structurally unresolved head segment of defined length favors proper measles virus hemagglutinin tetramerization and efficient membrane fusion triggering

Journal of Virology

Volumn 90, Issue 1, 2016, Pages 68-75

  Navaratnarajah, Chanakha K ^a   Rosemarie, Quincy ^a   Cattaneo, Roberto ^a  

^a MAYO CLINIC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; VIRUS HEMAGGLUTININ; HEMAGGLUTININ PROTEIN G, MEASLES VIRUS; MUTANT PROTEIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CELL SURFACE; CONTROLLED STUDY; GENE MUTATION; HUMAN; HUMAN CELL; INTRACELLULAR TRANSPORT; MEASLES VIRUS; MEMBRANE FUSION; MOLECULAR INTERACTION; MOLECULAR WEIGHT; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN MODIFICATION; PROTEIN STRUCTURE; PROTEIN TETRAMERIZATION; ANIMAL; CELL LINE; CELL MEMBRANE; DNA MUTATIONAL ANALYSIS; GENE DELETION; GENETICS; METABOLISM; PHYSIOLOGY; PROTEIN MULTIMERIZATION; PROTEIN TRANSPORT; VIRUS ENTRY;

AMINO ACID SUBSTITUTION; ANIMALS; CELL LINE; CELL MEMBRANE; DNA MUTATIONAL ANALYSIS; HEMAGGLUTININS, VIRAL; HUMANS; MEASLES VIRUS; MUTANT PROTEINS; PROTEIN MULTIMERIZATION; PROTEIN TRANSPORT; SEQUENCE DELETION; VIRUS INTERNALIZATION;

EID: 84953897262     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.02253-15     Document Type: Article

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