The alternate triad motif of the poly(ADP-ribose) polymerase-like domain of the human zinc finger antiviral protein is essential for its antiviral activity

Journal of General Virology

Volumn 95, Issue PART 4, 2014, Pages 816-822

  Gläsker, Sabine ^a   Töller, Maren ^a   Kümmerer, Beate Mareike ^a  

^a UNIVERSITY HOSPITAL BONN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMINO ACID; MESSENGER RNA; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; SMALL INTERFERING RNA; ZINC FINGER PROTEIN;

ALPHA VIRUS; AMINO ACID SUBSTITUTION; ANTIVIRAL ACTIVITY; ARTICLE; CONTROLLED STUDY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN MOTIF; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SINDBIS VIRUS; WESTERN BLOTTING;

AMINO ACID SUBSTITUTION; ANTIVIRAL AGENTS; CELL LINE; CELL SURVIVAL; DNA MUTATIONAL ANALYSIS; HUMANS; MUTAGENESIS, SITE-DIRECTED; MUTANT PROTEINS; POLY(ADP-RIBOSE) POLYMERASES; PROTEIN STRUCTURE, TERTIARY; RNA-BINDING PROTEINS; SINDBIS VIRUS; VIRAL LOAD; VIRUS REPLICATION;

EID: 84897101110     PISSN: 00221317     EISSN: 14652099     Source Type: Journal    
DOI: 10.1099/vir.0.060988-0     Document Type: Article

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