Point mutations in exon I of the herpes simplex virus putative terminase subunit, UL15, indicate that the most conserved residues are essential for cleavage and packaging

Journal of Virology

Volumn 77, Issue 17, 2003, Pages 9613-9621

  Przech, Angela J ^a   Yu, Dong ^a,b   Weller, Sandra K ^a  

^a UNIVERSITY OF CONNECTICUT HEALTH CENTER   (United States)

^b PRINCETON UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GENE PRODUCT; PROTEIN SUBUNIT; PROTEIN UL15; PROTEIN UL28; UNCLASSIFIED DRUG; VIRUS PROTEIN;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; BACTERIOPHAGE; CONTROLLED STUDY; CORRELATION ANALYSIS; EXON; GENE LOCUS; GENE MUTATION; GENE TRANSFER; GENE UL15; HERPES SIMPLEX VIRUS; IMMUNOFLUORESCENCE; MARKER GENE; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN LOCALIZATION; PROTEIN STABILITY; VERO CELL; VIRUS CAPSID; VIRUS DETECTION; VIRUS GENE; VIRUS REPLICATION;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; CAPSID PROTEINS; CELL LINE; CERCOPITHECUS AETHIOPS; CONSERVED SEQUENCE; DNA, VIRAL; EXONS; GENES, VIRAL; HERPESVIRUS 1, HUMAN; MOLECULAR SEQUENCE DATA; POINT MUTATION; SEQUENCE HOMOLOGY, AMINO ACID; VERO CELLS; VIRAL PROTEINS; VIRUS REPLICATION;

EID: 0042389525     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.77.17.9613-9621.2003     Document Type: Article

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