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

Journal of Cell Biology

Volumn 151, Issue 2, 2000, Pages 425-437

  Armstrong, R Todd ^a   Kushnir, Anna S ^a   White, Judith M ^a  

^a UNIVERSITY OF VIRGINIA HEALTH SYSTEM   (United States)

Author keywords

Glycosylphosphatidylinositol anchor; Hemagglutinin; Hemifusion; SNARE proteins; Transmembrane domain

Indexed keywords

ARGININE; GLYCOSYLPHOSPHATIDYLINOSITOL; MEMBRANE PROTEIN; SNARE PROTEIN; VIRUS HEMAGGLUTININ;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BIOCHEMISTRY; CARBOXY TERMINAL SEQUENCE; CELL SURFACE; CHIMERA; CONTROLLED STUDY; CYTOPLASM; GENE DELETION; HYDROPHILICITY; HYDROPHOBICITY; INFLUENZA VIRUS; MEMBRANE FUSION; NONHUMAN; PHENOTYPE; POINT MUTATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION;

AMINO ACID SEQUENCE; CHLORPROMAZINE; GLYCOSYLPHOSPHATIDYLINOSITOLS; HEMAGGLUTININ GLYCOPROTEINS, INFLUENZA VIRUS; INTRACELLULAR MEMBRANES; LIPID BILAYERS; MEMBRANE FUSION; MEMBRANE MICRODOMAINS; MEMBRANE PROTEINS; MICROSOMES; MODELS, BIOLOGICAL; MOLECULAR SEQUENCE DATA; MUTATION; ORTHOMYXOVIRIDAE; PROTEIN STRUCTURE, TERTIARY; SEQUENCE DELETION; SNARE PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; VESICULAR TRANSPORT PROTEINS;

EID: 0034676041     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.151.2.425     Document Type: Article

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