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Variation in Diagnostic Testing and Empiric Acyclovir Use for HSV Infection in Febrile InfantsTreasure, Jennifer 25 May 2022 (has links)
No description available.
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On The Lattice Size With Respect To The Standard Simplex in 3D.Alajmi, Abdulrahman N. 03 September 2020 (has links)
No description available.
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The Joint Distribution of Two Linear Combinations of Random Variables Uniformly Distributed on a SimplexLim, Siok 09 1900 (has links)
<p> This thesis deals with linear combinations of a set of
random variables uniformly distributed on a simplex. The exact
joint distribution of two general linear combinations with real
constant coefficients is considered and the results found in the
form of the joint probability density function. Application of
the result is also illustrated. </p> / Thesis / Master of Science (MSc)
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Herpes virus-based packaging systems for gene delivery of the RIIA sodium channelSadl, Virginia. January 1996 (has links)
No description available.
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MematineHCI and Amino-Alkyl-Cyclohexanes (621,625) Inhibit HSV-1 in SK-N-SH Neuronal CellsCaplinger, John N. 14 December 2001 (has links)
No description available.
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Herpes Simplex Virus-1: Crosstalk Between the Host Immunity and the Virus during Infection, Latency and ReanimationGasilina, Anjelika 10 June 2016 (has links)
No description available.
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Functional significance of the physical interaction between the herpes simplex virus type 1 origin-binding protein, UL9, and the DNA polymerase processivity factor, UL42Trego, Kelly S. 16 October 2003 (has links)
No description available.
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mRNA Decapitation Induced by the Herpes Simplex Virus Virion Host Shutoff Protein / mRNA Decapitation Induced by VHSHayes, Christopher 08 1900 (has links)
Cells infected with herpes simplex virus show a rapid cessation of protein synthesis and a dramatic decline in the levels of mRNA; a process known as host shutoff. This effect is attributed to a viral tegument protein called the virion host shutoff protein, or vhs. The mechanism by which vhs induces mRNA degradation is not yet understood. It is not known whether vhs possesses RNase activities or if it acts in combination with other cellular factors. To gain a better understanding of the function of vhs, I examined RNA degradation in detail by analyzing the RNA decay products generated in the presence of vhs. 𝘐𝘯 𝘷𝘪𝘷𝘰 experiments, performed by infecting murine erythroid leukemia cells with HSV, revealed that beta-globin mRNA is rapidly degraded, in the presence of vhs, without being converted to detectable decay intermediates. The half-life of this mRNA was 15 and 60 minutes for HSV-2 and HSV-1, respectively. Using vhs translated in a rabbit reticulocyte lysate system, I found that vhs induced rapid decay at the 5' end of a capped RNA molecule. The decay event was endonucleolytic and occurred at preferred sites downstream of the cap, generating capped oligonucleotides. Unlike influenza RNA polymerase, the cleavage event did not occur at a fixed distance from the cap since capped oligos of differing size were generated from different RNA substrates. My data indicate that vhs induced cleavage exhibits a strong, but not absolute preference for RNAs possessing an m⁷G cap, which may account for vhs' specificity for m RNAs 𝘪𝘯 𝘷𝘪𝘷𝘰. / Thesis / Master of Science (MSc)
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Characterization of Monoclonal Antibodies of Herpes Simplex Virus Type 2 Antigens / Monoclonal Antibodies to Herpes Simplex Type 2 AntigensGulck, Karen 09 1900 (has links)
A HSV 2 immediate early antigen was prepared and used as an immunogen in an attempt to produce monoclonal antibodies to this set to proteins. The results of three screening assays, ELISA, immunodiffusion and radioimmunoprecipitation with cell extracts and Protein A-Sepharose beads indicated that the hybrid cell lines are nonsecretors of antiHSV 2 antibodies. Other monoclonal cell lines from Dr. Bacchetti's laboratory were characterized by radioimmunoprecipitation with Protein A-Sepharose beads and cell extracts. / Thesis / Master of Science (MS)
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Mutational Analysis of the Hydrophobic Region of Herpes Simplex Virus-1 Glycoprotein gB / Mutational Analysis of Herpes Simplex Virus Glycoprotein gBEfler, Susan 11 1900 (has links)
The role of highly conserved amino acids within the carboxy-terminal hydrophobic domain of herpes
simplex virus I (HSV-I) glycoprotein gB was studied by introducing point mutations using the method of site
directed mutagenesis. A segment of this hydrophobic domain of glycoprotein gB contains a nuclear envelope
(NE) targeting signal and the effect of these point mutations on targeting to the nuclear envelope was
determined. A complementation assay was employed to determine the effect these mutations have on HSV-I infectivity .The point mutations created within the transmembrane domain of glycoprotein gB had no effect on nuclear envelope targeting and localization. However, single point mutations introduced into the first and
second hydrophobic domains of glycoprotein gB, G₇₄₃R and F₇₇₀S, affected the targeting and localization of
full-length glycoprotein gB at the nuclear envelope. When the transmembrane domain ofHSV-I glycoprotein
gB containing the following point mutations A₇₉₀Q, A₇₉₁S, A₇₈₆S, A₇₈₆Y and A₇₉₀S, was introduced into a
chimeric protein consisting of the cytoplasmic domain and ectodomain of a plasma membrane protein,
vesicular stomatitis virus glycoprotein G, NE targeting and localization were affected. These point mutations
may affect the targeting of glycoprotein gB by altering the structure of the targeting signal within the protein.
It can be hypothesized that the presence of the cytoplasmic domain. ectodomain domain, and the first and
second transmembrane domains within full-length glycoprotein gB can compensate for the effect these point
mutations have on nuclear envelope targeting. since the same point mutations had no effect on the targeting · and localization of full-length glycoprotein gB. Complementation assays showed that the glycoprotein gB mutants, A₇₈₆S, A₇₈₆Y, A₇₈₆N, A₇₉₀Q, A₇₉₁S, F₇₇₀S, or G₇₄₃R, were unable to complement a gB-null virus even though these mutant proteins are localized at the nuclear envelope. These proteins may not have been incorporated into the viral capsid due to misfolding or due to the fact that sequences required for interaction with other viral proteins were lost. Another possibility is that the mutant proteins were incorporated into the HSV virion but were not biologically active. / Thesis / Master of Science (MS)
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