A single drug-resistance mutation in HSV-1 UL52 primase points to a difference between two helicase-primase inhibitors in their mode of interaction with the antiviral target

Journal of Antimicrobial Chemotherapy

Volumn 61, Issue 5, 2008, Pages 1044-1047

  Biswas, Subhajit ^a   Kleymann, Gerald ^b   Swift, Mihaiela ^a   Tiley, Laurence S ^a   Lyall, Jonathan ^a   Aguirre Hernéndez, Jesús ^a   Field, Hugh J ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b NONE   (Germany)

Author keywords

BAY 57 1293; BILS 22 BS; Herpes simplex virus; Mutation

Indexed keywords

ANTIVIRUS AGENT; BAY 51293; BAY 571293; BILS 22 BS; ENZYME; HELICASE; PRIMASE; UNCLASSIFIED DRUG; VIRUS DNA;

ANTIVIRAL RESISTANCE; ARTICLE; CONTROLLED STUDY; CROSS RESISTANCE; DNA SEQUENCE; DRUG POTENCY; DRUG PROTEIN BINDING; DRUG TARGETING; HERPES SIMPLEX VIRUS 1; MUTATIONAL ANALYSIS; NONHUMAN; SEQUENCE ALIGNMENT; VALIDATION STUDY; VERO CELL;

ANTIVIRAL AGENTS; DNA HELICASES; DNA PRIMASE; DOSE-RESPONSE RELATIONSHIP, DRUG; DRUG RESISTANCE, VIRAL; HERPESVIRUS 1, HUMAN; PYRIDINES; THIAZOLES; VIRAL PROTEINS;

EID: 42149087645     PISSN: 03057453     EISSN: 14602091     Source Type: Journal    
DOI: 10.1093/jac/dkn057     Document Type: Article

References (10)

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