The N terminus of PA polymerase of swine-origin influenza virus H1N1 determines its compatibility with PB2 and PB1 subunits through a strain-specific amino acid serine 186

Virus Research

Volumn 155, Issue 1, 2011, Pages 325-333

  Wanitchang, Asawin ^a   Jengarn, Juggragarn ^a   Jongkaewwattana, Anan ^a  

^a NATIONAL SCIENCE AND TECHNOLOGY DEVELOPMENT AGENCY   (Thailand)

Author keywords

Compatibility; Influenza virus polymerase complex; PA; Swine origin influenza virus

Indexed keywords

PROTEIN PA; PROTEIN PB1; PROTEIN PB2; RNA POLYMERASE; SERINE; UNCLASSIFIED DRUG; VIRUS PROTEIN;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CELL STRAIN; CHIMERA; COMPLEX FORMATION; CONTROLLED STUDY; ENZYME ACTIVITY; HUMAN; HUMAN CELL; INFLUENZA A (H1N1); INFLUENZA VIRUS A H1N1; MUTATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PANDEMIC INFLUENZA; PHENOTYPE; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; SWINE INFLUENZA; VIROGENESIS; VIRUS RECOMBINANT; VIRUS REPLICATION; VIRUS STRAIN; ZYGOTE;

AMINO ACID SUBSTITUTION; ANIMALS; CELL LINE; CHICK EMBRYO; DOGS; HUMANS; INFLUENZA A VIRUS, H1N1 SUBTYPE; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; RNA REPLICASE; SERINE; VIRAL PROTEINS; VIRUS REPLICATION;

ORTHOMYXOVIRIDAE; SUIDAE;

EID: 78650548182     PISSN: 01681702     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virusres.2010.10.032     Document Type: Article

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