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herpes simplex/prolina
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Página 1 a partir de 71 resultados
Characterization of RNA determinants recognized by the arginine- and proline-rich region of Us11, a herpes simplex virus type 1-encoded double-stranded RNA binding protein that prevents PKR activation.
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The herpes simplex virus Us11 gene product inhibits activation of the cellular PKR kinase and associates with a limited number of unrelated viral and cellular RNA molecules via a carboxyl-terminal 68-amino-acid segment rich in arginine and proline. To characterize the determinants underlying the
Inhibition of PKR activation by the proline-rich RNA binding domain of the herpes simplex virus type 1 Us11 protein.
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Upon activation by double-stranded RNA in virus-infected cells, the cellular PKR kinase phosphorylates the translation initiation factor eukaryotic initiation factor 2 (eIF2) and thereby inhibits protein synthesis. The gamma 34.5 and Us11 gene products encoded by herpes simplex virus type 1 (HSV-1)
Proline and tyrosine residues in scaffold proteins of herpes simplex virus 1 critical to the interaction with portal protein and its incorporation into capsids.
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Previous results showed that amino acids 449 to 457 of pU(L)26, a component of the scaffold of herpes simplex virus 1 capsids, were critical for interaction with the portal protein encoded by U(L)6 and for incorporation of the portal into capsids. To identify residues in this scaffold domain
An N-terminal arginine-rich cluster and a proline-alanine-threonine repeat region determine the cellular localization of the herpes simplex virus type 1 ICP34.5 protein and its ligand, protein phosphatase 1.
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The ICP34.5 protein facilitates herpes simplex virus replication by binding and activating protein phosphatase 1 (PP1) by means of a very conserved C-terminal GADD34-like region. Natural variants of the ICP34.5 differing in the number of arginines in an Arg-rich cluster at the N terminus and the
Induction of arginases I and II in cornea during herpes simplex virus infection.
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Induction of inducible nitric oxide synthase (iNOS) following corneal infection with herpes simplex virus type-1 (HSV-1) generates nitric oxide (NO), an important player in the defense against viral infection. Changes in arginine metabolism during infection are not limited to effects of iNOS but can
Mapping of herpes simplex virus 1 genes with mutations which overcome host restrictions to infection.
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Earlier studies have shown that the thymidine kinase-negative baby hamster kidney (BHKTK-) cell lines expressing constitutively the herpes simplex virus 1 (HSV-1) glycoprotein D (gD), designated BJ, restrict infection by HSV-1 at the level of virus entry. U10, a HSV-1 mutant not restricted by the BJ
Analysis of the thymidine kinase gene from clinically isolated acyclovir-resistant herpes simplex viruses.
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The isolation and description of acyclovir-resistant (ACVR) herpes simplex-2 viruses from patients with AIDS has recently been reported. These ACVR viruses were all markedly decreased in their thymidine kinase (TK) activity, and 6 of 10 of these TK viruses were able to establish latency. In
Overexpression of CIN85 suppresses the growth of herpes simplex virus in HeLa cells.
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The adaptor protein CIN85 is widely distributed in different tissues and has three Src homology 3 (SH3) domains, a proline-rich region (PRR), and a coiled-coil domain. During studies on the function of CIN85, it was reported to form a complex with herpes simplex virus 1 (HSV-1) infected cell protein
Temperature-sensitive mutations in the putative herpes simplex virus type 1 terminase subunits pUL15 and pUL33 preclude viral DNA cleavage/packaging and interaction with pUL28 at the nonpermissive temperature.
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Terminases comprise essential components of molecular motors required to package viral DNA into capsids in a variety of DNA virus systems. Previous studies indicated that the herpes simplex virus type 1 U(L)15 protein (pU(L)15) interacts with the pU(L)28 moiety of a pU(L)28-pU(L)33 complex to form
Focal adhesion kinase plays a pivotal role in herpes simplex virus entry.
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Development of strategies to prevent herpes simplex virus (HSV) infection requires knowledge of cellular pathways harnessed by the virus for invasion. This study demonstrates that HSV induces rapid phosphorylation of focal adhesion kinase (FAK) in several human target cells and that phosphorylation
Stability of Asp-Pro bond under high and low energy collision induced dissociation conditions in the immunodominant epitope region of herpes simplex virion glycoprotein D.
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A series of truncated Herpes simplex virion peptides studied by fast atom bombardment mass spectrometry under high and low energy collision induced dissociation conditions showed preferential fragmentation of the aspartyl-proline amide bond, compared to other peptide bonds. Electrospray ionization
Herpes simplex virus type 1 infection of endothelium reduces collagen and fibronectin synthesis.
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Protein synthesis was assessed in virus-infected and -uninfected cultures of bovine aorta endothelial cells by following the incorporation of [14C]proline into nondialyzable protein and by use of an ELISA assay. Monolayers were infected at confluency by incubating with herpes simplex virus type I at
Permissible amino acid substitutions within the putative nucleoside binding site of herpes simplex virus type 1 encoded thymidine kinase established by random sequence mutagenesis [corrected].
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We determined the essentiality of all amino acid replacements within an 11-codon sequence in the putative nucleoside-binding site of thymidine kinase encoded by herpes simplex virus type 1. This involved partial randomization of 11 codons in the gene to create a degenerate library, followed by
ATP and SH3 binding sites in the protein kinase of the large subunit of herpes simplex virus type 2 of ribonucleotide reductase (ICP10).
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The large subunit of herpes simplex virus type 2 ribonucleotide reductase (ICP10) is a multifunctional protein. It consists of a ribonucleotide reductase and a serine/threonine protein kinase (PK) domain, which has three proline-rich motifs consistent with SH3-binding sites at positions 140, 149,
Fine structure analysis of type-specific and type-common antigenic sites of herpes simplex virus glycoprotein D.
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The fine structure of the antigenic determinants of herpes simplex virus type 1 and 2 glycoprotein D (gD) was analyzed to determine whether structural differences underlie the differential immunogenicity of these glycoproteins. A region common to herpes simplex virus type 1 and 2 gD (amino acid
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