Hydrophobic and charged residues in the central segment of the measles virus hemagglutinin stalk mediate transmission of the fusion-triggering signal

Journal of Virology

Volumn 87, Issue 18, 2013, Pages 10401-10404

  Apte Sengupta, Swapna ^a   Navaratnarajah, Chanakha K ^a   Cattaneo, Roberto ^a  

^a MAYO CLINIC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; HYBRID PROTEIN; SERINE; VIRUS HEMAGGLUTININ;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; DIMERIZATION; GENETIC CONSERVATION; HYDROPHOBICITY; IMMUNOPRECIPITATION; MEASLES VIRUS; MEMBRANE FUSION; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; QUANTITATIVE ANALYSIS; VIRUS ATTACHMENT; VIRUS MUTATION; VIRUS TRANSMISSION;

AMINO ACID SUBSTITUTION; DNA MUTATIONAL ANALYSIS; MEASLES VIRUS; PROTEIN BINDING; PROTEIN INTERACTION MAPPING; VIRAL FUSION PROTEINS; VIRAL PROTEINS; VIRUS INTERNALIZATION;

EID: 84883261324     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01547-13     Document Type: Article

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