A non-canonical Lon proteinase lacking the ATPase domain employs the Ser-Lys catalytic dyad to exercise broad control over the life cycle of a double-stranded RNA virus

EMBO Journal

Volumn 19, Issue 1, 2000, Pages 114-123

  Birghan, Christoph ^a   Mundt, Egbert ^a   Gorbalenya, Alexander E ^b  

^a FEDERAL RESEARCH INSTITUTE FOR ANIMAL HEALTH   (Germany)

^b NATIONAL CANCER INSTITUTE   (United States)

Author keywords

Autoproteolysis; Birnavirus; Capsid biogenesis; La (Lon) protein; Serine lysine protease

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DOUBLE STRANDED RNA; LYSINE; PROTEINASE; RNA DIRECTED RNA POLYMERASE; SERINE; VIRUS PROTEIN;

ARTICLE; CATALYSIS; CELL CULTURE; CELL ORGANELLE; GENETIC CONSERVATION; LIFE CYCLE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROCESSING; REOVIRUS; RNA VIRUS; VIROGENESIS;

EID: 0034602847     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/19.1.114     Document Type: Article

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