The UL41 protein of herpes simplex virus 1 degrades RNA by endonucleolytic cleavage in absence of other cellular or viral proteins

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

Volumn 103, Issue 8, 2006, Pages 2827-2832

  Taddeo, Brunella ^a   Zhang, Weiran ^a   Roizman, Bernard ^a  

^a UNIVERSITY OF CHICAGO   (United States)

Author keywords

Endoribonuclease; mRNA; Virion host shutoff

Indexed keywords

ALANINE; BETA ACTIN; GLUTATHIONE TRANSFERASE; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN D; MESSENGER RNA; PROTEIN; PROTEIN GAPDH; PROTEIN IEX 1; PROTEIN UL41; TRISTETRAPROLIN; UNCLASSIFIED DRUG; VIRION HOST SHUTOFF PROTEIN; VIRUS PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CELL GRANULE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME PURIFICATION; ESCHERICHIA COLI; GENETIC TRANSCRIPTION; HERPES; HERPES SIMPLEX VIRUS 1; HUMAN; HUMAN CELL; IN VITRO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; RNA DEGRADATION; VIRUS PARTICLE;

3' UNTRANSLATED REGIONS; APOPTOSIS REGULATORY PROTEINS; CELLS, CULTURED; CYTOPLASM; ENDORIBONUCLEASES; GLUTATHIONE TRANSFERASE; HERPES SIMPLEX; HERPESVIRUS 1, HUMAN; HUMANS; MEMBRANE PROTEINS; RECOMBINANT FUSION PROTEINS; RNA, MESSENGER; TRISTETRAPROLIN; VIRAL PROTEINS;

ESCHERICHIA COLI; HERPES; HUMAN HERPESVIRUS 1;

EID: 33644552729     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0510712103     Document Type: Article

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