Site-specific S-acylation of influenza virus hemagglutinin: The location of the acylation site relative to the membrane border is the decisive factor for attachment of stearate

Journal of Biological Chemistry

Volumn 289, Issue 50, 2014, Pages 34978-34989

  Brett, Katharina ^a   Kordyukova, Larisa V ^b   Serebryakova, Marina V ^b,c   Mintaev, Ramil R ^b,d   Alexeevski, Andrei V ^b   Veit, Michael ^a  

^a FREIE UNIVERSITÄT BERLIN   (Germany)

^b MOSCOW STATE UNIVERSITY   (Russian Federation)

^c INSTITUTE OF GENE BIOLOGY   (Russian Federation)

^d MECHNIKOV RESEARCH INSTITUTE FOR VACCINES AND SERA   (Russian Federation)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; LOCATION; MAMMALS; MASS SPECTROMETRY; PALMITIC ACID; PROTEINS; VIRUSES;

CELLULAR PROTEINS; INFECTIOUS VIRUS; METABOLIC LABELING; MOLECULAR SIGNALS; PREFERENTIAL ATTACHMENTS; SAMPLE PREPARATION; TRANSMEMBRANE REGIONS; VIRUS REPLICATION;

ACYLATION;

INFLUENZA VIRUS HEMAGGLUTININ; PALMITIC ACID; STEARIC ACID; STEARIC ACID DERIVATIVE;

ACYLATION; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; BIRD; CHLOROCEBUS; CONTROLLED STUDY; CYTOPLASM; HUMAN; HUMAN CELL; INFLUENZA VIRUS; MASS SPECTROMETRY; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; MOLECULAR RECOGNITION; NONHUMAN; PROTEIN DOMAIN; PROTEIN EXPRESSION; SITE SPECIFIC ACYLATION; ANIMAL; BINDING SITE; CELL LINE; CELL MEMBRANE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME SPECIFICITY; GENETICS; INFLUENZA A VIRUS (H1N1); METABOLISM; MOLECULAR GENETICS; MUTAGENESIS; PHYSIOLOGY; POINT MUTATION; PROTEIN TERTIARY STRUCTURE; VIROLOGY;

AVES; MAMMALIA; ORTHOMYXOVIRIDAE;

ACYLATION; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CELL LINE; CELL MEMBRANE; CYTOPLASM; HEMAGGLUTININ GLYCOPROTEINS, INFLUENZA VIRUS; HUMANS; INFLUENZA A VIRUS, H1N1 SUBTYPE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS; POINT MUTATION; PROTEIN STRUCTURE, TERTIARY; STEARATES; SUBSTRATE SPECIFICITY;

EID: 84918572900     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.586180     Document Type: Article

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