Assembly of subtype 1 influenza neuraminidase is driven by both the transmembrane and head domains

Journal of Biological Chemistry

Volumn 288, Issue 1, 2013, Pages 644-653

  Da Silva, Diogo V ^a   Nordholm, Johan ^a   Madjo, Ursula ^a   Pfeiffer, Annika ^a   Daniels, Robert ^a  

^a STOCKHOLM UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

DRUG TARGETS; HOMOTETRAMERS; NEURAMINIDASE; OLIGOMERIC STATE; SOLUBLE DOMAINS; SURFACE ANTIGEN; TETRAMERS; TRANSMEMBRANE DOMAIN; TRANSMEMBRANES; WILD TYPES;

ACTIVATION ANALYSIS; CELL MEMBRANES; DIGITAL STORAGE; OLIGOMERIZATION;

OLIGOMERS;

OLIGOMER; TETRAMER; VIRUS SIALIDASE;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME DEFECT; ENZYME RELEASE; ENZYME SYNTHESIS; HUMAN; HUMAN CELL; INFLUENZA; INFLUENZA VIRUS; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN LOCALIZATION; STRUCTURE ACTIVITY RELATION;

ANIMALS; DIMERIZATION; DOGS; GLYCOPROTEINS; HEK293 CELLS; HELA CELLS; HUMANS; INFLUENZA, HUMAN; KINETICS; MEMBRANE PROTEINS; MODELS, MOLECULAR; MOLECULAR CONFORMATION; NEURAMINIDASE; PLASMIDS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY;

EID: 84872074817     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.424150     Document Type: Article

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