Academic literature on the topic 'HSV-1 DNA polymerase'

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Journal articles on the topic "HSV-1 DNA polymerase"

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Thomsen, Darrell R., Nancee L. Oien, Todd A. Hopkins, et al. "Amino Acid Changes within Conserved Region III of the Herpes Simplex Virus and Human Cytomegalovirus DNA Polymerases Confer Resistance to 4-Oxo-Dihydroquinolines, a Novel Class of Herpesvirus Antiviral Agents." Journal of Virology 77, no. 3 (2003): 1868–76. http://dx.doi.org/10.1128/jvi.77.3.1868-1876.2003.

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ABSTRACT The 4-oxo-dihydroquinolines (PNU-182171 and PNU-183792) are nonnucleoside inhibitors of herpesvirus polymerases (R. J. Brideau et al., Antiviral Res. 54:19-28, 2002; N. L. Oien et al., Antimicrob. Agents Chemother. 46:724-730, 2002). In cell culture these compounds inhibit herpes simplex virus type 1 (HSV-1), HSV-2, human cytomegalovirus (HCMV), varicella-zoster virus (VZV), and human herpesvirus 8 (HHV-8) replication. HSV-1 and HSV-2 mutants resistant to these drugs were isolated and the resistance mutation was mapped to the DNA polymerase gene. Drug resistance correlated with a poin
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Aduma, P. J., S. V. Gupta, and A. L. Stuart. "Interaction of 5-Methoxymethyl-2′-Deoxyuridine Triphosphate with DNA Polymerases: Effects of the 5-Substituent and Comparison with the Deoxycytidine Derivative." Antiviral Chemistry and Chemotherapy 3, no. 4 (1992): 243–47. http://dx.doi.org/10.1177/095632029200300406.

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5-Methoxymethyl-2′-deoxyuridine (MMdUrd) is a selective anti-herpes agent that is dependent upon initial phosphorylation by Herpes simplex virus-induced deoxythymidine kinase. In order to determine its mechanism of action, MMdUrd was converted to the 5′-triphosphate (MMdUTP) and the nature of interaction of MMdUTP and dTTP with DNA polymerase of E. coli, HSV-1, and human α was investigated. The order of utilization of deoxyuridine analogues by bacterial and HSV-1 DNA polymerases for DNA synthesis was: dTTP > MMdUTP. In contrast, 5-methoxymethyl-2′-deoxycytidine-5′-triphosphate (MMdCTP) was
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Zhu, Yali, Jason Stroud, Liping Song, and Deborah S. Parris. "Kinetic Approaches to Understanding the Mechanisms of Fidelity of the Herpes Simplex Virus Type 1 DNA Polymerase." Journal of Nucleic Acids 2010 (2010): 1–15. http://dx.doi.org/10.4061/2010/631595.

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We discuss how the results of presteady-state and steady-state kinetic analysis of the polymerizing and excision activities of herpes simplex virus type 1 (HSV-1) DNA polymerase have led to a better understanding of the mechanisms controlling fidelity of this important model replication polymerase. Despite a poorer misincorporation frequency compared to other replicative polymerases with intrinsic 3′to 5′exonuclease (exo) activity, HSV-1 DNA replication fidelity is enhanced by a high kinetic barrier to extending a primer/template containing a mismatch or abasic lesion and by the dynamic abilit
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Zhu, Yali, Zetang Wu, M. Cristina Cardoso, and Deborah S. Parris. "Processing of Lagging-Strand Intermediates In Vitro by Herpes Simplex Virus Type 1 DNA Polymerase." Journal of Virology 84, no. 15 (2010): 7459–72. http://dx.doi.org/10.1128/jvi.01875-09.

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ABSTRACT The processing of lagging-strand intermediates has not been demonstrated in vitro for herpes simplex virus type 1 (HSV-1). Human flap endonuclease-1 (Fen-1) was examined for its ability to produce ligatable products with model lagging-strand intermediates in the presence of the wild-type or exonuclease-deficient (exo−) HSV-1 DNA polymerase (pol). Primer/templates were composed of a minicircle single-stranded DNA template annealed to primers that contained 5′ DNA flaps or 5′ annealed DNA or RNA sequences. Gapped DNA primer/templates were extended but not significantly strand displaced
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Piret, Jocelyne, Nathalie Goyette, Brian E. Eckenroth, Emilien Drouot, Matthias Götte, and Guy Boivin. "Contrasting Effects of W781V and W780V Mutations in Helix N of Herpes Simplex Virus 1 and Human Cytomegalovirus DNA Polymerases on Antiviral Drug Susceptibility." Journal of Virology 89, no. 8 (2015): 4636–44. http://dx.doi.org/10.1128/jvi.03360-14.

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ABSTRACTDNA polymerases of theHerpesviridaeand bacteriophage RB69 belong to the α-like DNA polymerase family. In spite of similarities in structure and function, the RB69 enzyme is relatively resistant to foscarnet, requiring the mutation V478W in helix N to promote the closed conformation of the enzyme to make it susceptible to the antiviral. Here, we generated recombinant herpes simplex virus 1 (HSV-1) and human cytomegalovirus (HCMV) mutants harboring the revertant in UL30 (W781V) and UL54 (W780V) DNA polymerases, respectively, to further investigate the impact of this tryptophan on antivir
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Hassan, Sherif T. S., Miroslava Šudomová, Kateřina Berchová-Bímová, Karel Šmejkal, and Javier Echeverría. "Psoromic Acid, a Lichen-Derived Molecule, Inhibits the Replication of HSV-1 and HSV-2, and Inactivates HSV-1 DNA Polymerase: Shedding Light on Antiherpetic Properties." Molecules 24, no. 16 (2019): 2912. http://dx.doi.org/10.3390/molecules24162912.

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Psoromic acid (PA), a bioactive lichen-derived compound, was investigated for its inhibitory properties against herpes simplex virus type 1 (HSV-1) and type 2 (HSV-2), along with the inhibitory effect on HSV-1 DNA polymerase, which is a key enzyme that plays an essential role in HSV-1 replication cycle. PA was found to notably inhibit HSV-1 replication (50% inhibitory concentration (IC50): 1.9 μM; selectivity index (SI): 163.2) compared with the standard drug acyclovir (ACV) (IC50: 2.6 μM; SI: 119.2). The combination of PA with ACV has led to potent inhibitory activity against HSV-1 replicatio
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Kamiyama, Tomoko, Masahiko Kurokawa, and Kimiyasu Shiraki. "Characterization of the DNA polymerase gene of varicella-zoster viruses resistant to acyclovir." Journal of General Virology 82, no. 11 (2001): 2761–65. http://dx.doi.org/10.1099/0022-1317-82-11-2761.

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The nucleotide changes of the DNA polymerase gene and the susceptibility of acyclovir (ACV)-resistant varicella-zoster virus (VZV) mutants to anti-herpetic drugs were determined and compared to those of herpes simplex virus type 1 (HSV-1) mutants. The seven ACV-resistant VZV mutants were classified into three groups, N779S, G805C and V855M, according to the sequences of their DNA polymerase genes. The amino acid substitutions N779S and G805C were identical in position to the N815S and G814C mutations in the HSV-1 DNA polymerase mutants, respectively, and the V855M amino acid substitution was s
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Oien, Nancee L., Roger J. Brideau, Todd A. Hopkins, et al. "Broad-Spectrum Antiherpes Activities of 4-Hydroxyquinoline Carboxamides, a Novel Class of Herpesvirus Polymerase Inhibitors." Antimicrobial Agents and Chemotherapy 46, no. 3 (2002): 724–30. http://dx.doi.org/10.1128/aac.46.3.724-730.2002.

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ABSTRACT Through broad screening of the compound library at Pharmacia, a naphthalene carboxamide was identified as a nonnucleoside inhibitor of human cytomegalovirus (HCMV) polymerase. Structure-activity relationship studies demonstrated that a quinoline ring could be substituted for naphthalene, resulting in the discovery of a 4-hydroxyquinoline-3-carboxamide (4-HQC) class of antiviral agents with unique biological properties. In vitro assays with the 4-HQCs have demonstrated potent inhibition of HCMV, herpes simplex virus type 1 (HSV-1), and varicella-zoster virus (VZV) polymerases but no in
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Danovich, R. M., and N. Frenkel. "Herpes simplex virus induces the replication of foreign DNA." Molecular and Cellular Biology 8, no. 8 (1988): 3272–81. http://dx.doi.org/10.1128/mcb.8.8.3272.

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Plasmids containing the simian virus 40 (SV40) DNA replication origin and the large T gene are replicated efficiently in Vero monkey cells but not in rabbit skin cells. Efficient replication of the plasmids was observed in rabbit skin cells infected with herpes simplex virus type 1 (HSV-1) and HSV-2. The HSV-induced replication required the large T antigen and the SV40 replication origin. However, it produced concatemeric molecules resembling replicative intermediates of HSV DNA and was sensitive to phosphonoacetate at concentrations known to inhibit the HSV DNA polymerase. Therefore, it invol
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Danovich, R. M., and N. Frenkel. "Herpes simplex virus induces the replication of foreign DNA." Molecular and Cellular Biology 8, no. 8 (1988): 3272–81. http://dx.doi.org/10.1128/mcb.8.8.3272-3281.1988.

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Plasmids containing the simian virus 40 (SV40) DNA replication origin and the large T gene are replicated efficiently in Vero monkey cells but not in rabbit skin cells. Efficient replication of the plasmids was observed in rabbit skin cells infected with herpes simplex virus type 1 (HSV-1) and HSV-2. The HSV-induced replication required the large T antigen and the SV40 replication origin. However, it produced concatemeric molecules resembling replicative intermediates of HSV DNA and was sensitive to phosphonoacetate at concentrations known to inhibit the HSV DNA polymerase. Therefore, it invol
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Dissertations / Theses on the topic "HSV-1 DNA polymerase"

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Terrell, Shariya Louise. "Importance of the Pre-\(NH_2\)-Terminal Domain of HSV-1 DNA Polymerase for Viral Replication." Thesis, Harvard University, 2012. http://dissertations.umi.com/gsas.harvard:10705.

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The catalytic subunit of the herpes simplex virus 1 DNA polymerase (HSV-1 Pol) has been extensively studied; however, its full complement of functional domains has yet to be characterized. The previously uncharacterized pre-NH2-terminal domain (residues 1-140) within HSV-1 Pol is unique to the herpesvirus Pol family. We sought to investigate the importance of this domain for viral replication in cell culture and an animal model of infection. We evaluated the enzymatic activity of purified pre-NH2-terminal Pol mutant proteins in which conserved residues had been deleted or substituted. Subseque
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Henschel, Annika Maria [Verfasser], and Klaus [Akademischer Betreuer] Hamprecht. "Mutationsanalyse des HSV-1 DNA-Polymerase-Gens (UL30) im Kontext von Polymorphismus und ACV-Resistenz bei Patienten nach Stammzelltransplantation / Annika Maria Henschel ; Betreuer: Klaus Hamprecht." Tübingen : Universitätsbibliothek Tübingen, 2015. http://d-nb.info/1197057307/34.

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Song, Liping. "The role of the associated 3' to 5' exonuclease activity and processivity factor (UL42) of Herpes simplex virus type 1 DNA polymerase on the fidelity of DNA replication." Columbus, Ohio : Ohio State University, 2004. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1083958702.

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Thesis (Ph. D.)--Ohio State University, 2004.<br>Title from first page of PDF file. Document formatted into pages; contains xii, 208 p.; also includes graphics (some col.). Includes abstract and vita. Advisor: Deborah S. Parris, Dept. of Molecular Genetics. Includes bibliographical references (p. 191-208).
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Books on the topic "HSV-1 DNA polymerase"

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Khodari, Yousif Abdulwahed Mohammad. Quantification of Herpes simplex virus type 1(HSV-1) DNA by the polymerase chain reaction. University of Manchester, 1995.

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