Single amino acid substitutions in the HSV-1 helicase protein that confer resistance to the helicase-primase inhibitor BAY 57-1293 are associated with increased or decreased virus growth characteristics in tissue culture-Reference-Cited by-同舟云学术

Single amino acid substitutions in the HSV-1 helicase protein that confer resistance to the helicase-primase inhibitor BAY 57-1293 are associated with increased or decreased virus growth characteristics in tissue culture

Published:2007-04-04 Issue:8 Volume:152 Page:1489-1500
ISSN:0304-8608
Container-title:Archives of Virology
language:en
Short-container-title:Arch Virol

Author:

Biswas S.,Jennens L.,Field H. J.

Publisher

Springer Science and Business Media LLC

Subject

Virology,General Medicine

Link

http://link.springer.com/content/pdf/10.1007/s00705-007-0964-7.pdf

Reference25 articles.

1. Herpes simplex virus zosteriform lesions with adoptive transfer of immune cells: a murine model which mimics human recurrent disease

2. Potent In Vivo Antiviral Activity of the Herpes Simplex Virus Primase-Helicase Inhibitor BAY 57-1293

3. Biswas S, Jennens L, Field HJ (2006) The helicase primase inhibitor, BAY 57-1293 shows potent therapeutic antiviral activity superior to famciclovir in BALB/c mice infected with herpes simplex virus type 1. Antiviral Res [Epub ahead of print]

4. High Frequency of Spontaneous Helicaseprimase Inhibitor (BAY 57–1293) Drug-Resistant Variants in Certain Laboratory Isolates of HSV-1

5. Antiherpesvirus activity of 9-(4-hydroxy-3-hydroxymethylbut-1-yl) guanine (BRL 39123) in animals

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