Role of the vaccinia virus O3 protein in cell entry can be fulfilled by its Sequence flexible transmembrane domain

Virology

Volumn 444, Issue 1-2, 2013, Pages 148-157

  Satheshkumar, P S ^a   Chavre, James ^a   Moss, Bernard ^a  

^a NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES   (United States)

Author keywords

Entry fusion complex; Membrane fusion; Mutagenesis; Poxvirus entry; Transmembrane protein

Indexed keywords

O3 VIRUS PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; SEQUENCE ANALYSIS; SITE DIRECTED MUTAGENESIS; TRANSMEMBRANE DOMAIN; VIRUS ENTRY; VIRUS MUTANT; VIRUS PLAQUE; WILD TYPE;

ENTRY-FUSION COMPLEX; MEMBRANE FUSION; MUTAGENESIS; POXVIRUS ENTRY; TRANSMEMBRANE PROTEIN;

AMINO ACID SUBSTITUTION; DNA MUTATIONAL ANALYSIS; MUTANT PROTEINS; SEQUENCE DELETION; VACCINIA VIRUS; VIRAL FUSION PROTEINS; VIRUS INTERNALIZATION;

POXVIRIDAE; VACCINIA VIRUS;

EID: 84882912381     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2013.06.003     Document Type: Article

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