Mutations that specifically impair the DNA binding activity of the herpes simplex virus protein UL42.

Por Chow, C S, Coen, D M
Publicado em 1995

Examination of the roles of transcription factor Sp1-binding sites and an octamer motif in trans induction of the herpes simplex virus thymidine kinase gene.

Por Böni, J, Coen, D M
Publicado em 1989

Herpes simplex virus mutants resistant to arabinosyladenine in the presence of deoxycoformycin.

Por Fleming, H E, Coen, D M
Publicado em 1984

Quantification of transcripts from the ICP4 and thymidine kinase genes in mouse ganglia latently infected with herpes simplex virus.

Por Kramer, M F, Coen, D M
Publicado em 1995

Analysis of the transcript of the herpes simplex virus DNA polymerase gene provides evidence that polymerase expression is inefficient at the level of translation.

Por Yager, D R, Coen, D M
Publicado em 1988

Pathogenicity of herpes simplex virus mutants containing drug resistance mutations in the viral DNA polymerase gene.

Por Field, H J, Coen, D M
Publicado em 1986

Two distinct loci confer resistance to acycloguanosine in herpes simplex virus type 1.

Por Coen, D M, Schaffer, P A
Publicado em 1980

Herpes simplex virus ribonucleotide reductase mutants are hypersensitive to acyclovir.

Por Coen, D M, Goldstein, D J, Weller, S K
Publicado em 1989

Quantitative polymerase chain reaction analysis of herpes simplex virus DNA in ganglia of mice infected with replication-incompetent mutants.

Por Katz, J P, Bodin, E T, Coen, D M
Publicado em 1990

A conserved open reading frame that overlaps the herpes simplex virus thymidine kinase gene is important for viral growth in cell culture.

Por Jacobson, J G, Martin, S L, Coen, D M
Publicado em 1989

Promoter domains required for expression of plasmid-borne copies of the herpes simplex virus thymidine kinase gene in virus-infected mouse fibroblasts and microinjected frog oocyte...

Por Eisenberg, S P, Coen, D M, McKnight, S L
Publicado em 1985

Mutation within the herpes simplex virus DNA polymerase gene conferring resistance to (R)-9-(3,4-dihydroxybutyl)guanine.

Por Chiou, H C, Kerns, K M, Coen, D M
Publicado em 1986

Functional analysis of the herpes simplex virus UL42 protein.

Por Digard, P, Chow, C S, Pirrit, L, Coen, D M
Publicado em 1993

A point mutation within a distinct conserved region of the herpes simplex virus DNA polymerase gene confers drug resistance.

Por Hwang, C B, Ruffner, K L, Coen, D M
Publicado em 1992

Restricted expression of herpes simplex virus lytic genes during establishment of latent infection by thymidine kinase-negative mutant viruses.

Por Kosz-Vnenchak, M, Coen, D M, Knipe, D M
Publicado em 1990

Isolation and characterization of herpes simplex virus mutants containing engineered mutations at the DNA polymerase locus.

Por Marcy, A I, Yager, D R, Coen, D M
Publicado em 1990

Translational regulation of herpes simplex virus DNA polymerase.

Por Yager, D R, Marcy, A I, Coen, D M
Publicado em 1990

The extreme C terminus of herpes simplex virus DNA polymerase is crucial for functional interaction with processivity factor UL42 and for viral replication.

Por Digard, P, Bebrin, W R, Weisshart, K, Coen, D M
Publicado em 1993

Unusual regulation of expression of the herpes simplex virus DNA polymerase gene.

Por Wobbe, K K, Digard, P, Staknis, D, Coen, D M
Publicado em 1993

Herpes simplex virus transactivator ICP4 operationally substitutes for the cellular transcription factor Sp1 for efficient expression of the viral thymidine kinase gene.

Por Imbalzano, A N, Coen, D M, DeLuca, N A
Publicado em 1991