The pro-fusion domain of herpes simplex virus glycoprotein D (gD) interacts with the gD N terminus and is displaced by soluble forms of viral receptors

Proceedings of the National Academy of Sciences of the United States of America

Volumn 102, Issue 26, 2005, Pages 9323-9328

  Fusco, Daniela ^a   Forghieri, Cristina ^a   Campadelli Fiume, Gabriella ^a  

^a UNIVERSITY OF BOLOGNA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; COMPLEMENTARY DNA; GLUTATHIONE; GLUTATHIONE TRANSFERASE; GLYCOPROTEIN D; HYBRID PROTEIN; PLASMID DNA; VIRUS GLYCOPROTEIN; VIRUS RECEPTOR;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; ENZYME LINKED IMMUNOSORBENT ASSAY; HERPES SIMPLEX VIRUS; IMMUNOBLOTTING; MEMBRANE FUSION; MUTAGENESIS; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PURIFICATION; VIRUS CELL INTERACTION;

AMINO ACID SEQUENCE; ANIMALS; CERCOPITHECUS AETHIOPS; COS CELLS; ENZYME-LINKED IMMUNOSORBENT ASSAY; GLUTATHIONE TRANSFERASE; IMMUNOBLOTTING; MOLECULAR SEQUENCE DATA; MUTAGENESIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; VERO CELLS; VIRAL ENVELOPE PROTEINS; VIRAL FUSION PROTEINS;

HERPESVIRIDAE; SIMPLEXVIRUS;

EID: 21544456647     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0503907102     Document Type: Article

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