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Journal Abstract Search

281 related items for PubMed ID: 9696792

  • 1. The second-site mutation in the herpes simplex virus recombinants lacking the gamma134.5 genes precludes shutoff of protein synthesis by blocking the phosphorylation of eIF-2alpha.
    Cassady KA, Gross M, Roizman B.
    J Virol; 1998 Sep; 72(9):7005-11. PubMed ID: 9696792
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  • 2. The herpes simplex virus US11 protein effectively compensates for the gamma1(34.5) gene if present before activation of protein kinase R by precluding its phosphorylation and that of the alpha subunit of eukaryotic translation initiation factor 2.
    Cassady KA, Gross M, Roizman B.
    J Virol; 1998 Nov; 72(11):8620-6. PubMed ID: 9765401
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  • 3. Second-site mutation outside of the U(S)10-12 domain of Deltagamma(1)34.5 herpes simplex virus 1 recombinant blocks the shutoff of protein synthesis induced by activated protein kinase R and partially restores neurovirulence.
    Cassady KA, Gross M, Gillespie GY, Roizman B.
    J Virol; 2002 Feb; 76(3):942-9. PubMed ID: 11773369
    [Abstract] [Full Text] [Related]

  • 4. Suppression of the phenotype of gamma(1)34.5- herpes simplex virus 1: failure of activated RNA-dependent protein kinase to shut off protein synthesis is associated with a deletion in the domain of the alpha47 gene.
    He B, Chou J, Brandimarti R, Mohr I, Gluzman Y, Roizman B.
    J Virol; 1997 Aug; 71(8):6049-54. PubMed ID: 9223497
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  • 5. The gamma(1)34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1alpha to dephosphorylate the alpha subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase.
    He B, Gross M, Roizman B.
    Proc Natl Acad Sci U S A; 1997 Feb 04; 94(3):843-8. PubMed ID: 9023344
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  • 6. Association of a M(r) 90,000 phosphoprotein with protein kinase PKR in cells exhibiting enhanced phosphorylation of translation initiation factor eIF-2 alpha and premature shutoff of protein synthesis after infection with gamma 134.5- mutants of herpes simplex virus 1.
    Chou J, Chen JJ, Gross M, Roizman B.
    Proc Natl Acad Sci U S A; 1995 Nov 07; 92(23):10516-20. PubMed ID: 7479831
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  • 7. Activation of NF-kappaB in cells productively infected with HSV-1 depends on activated protein kinase R and plays no apparent role in blocking apoptosis.
    Taddeo B, Luo TR, Zhang W, Roizman B.
    Proc Natl Acad Sci U S A; 2003 Oct 14; 100(21):12408-13. PubMed ID: 14530405
    [Abstract] [Full Text] [Related]

  • 8. Dephosphorylation of eIF-2alpha mediated by the gamma(1)34.5 protein of herpes simplex virus type 1 is required for viral response to interferon but is not sufficient for efficient viral replication.
    Cheng G, Yang K, He B.
    J Virol; 2003 Sep 14; 77(18):10154-61. PubMed ID: 12941928
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  • 13. Regulation of eIF2alpha phosphorylation by different functions that act during discrete phases in the herpes simplex virus type 1 life cycle.
    Mulvey M, Poppers J, Sternberg D, Mohr I.
    J Virol; 2003 Oct 14; 77(20):10917-28. PubMed ID: 14512542
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  • 14. AlaArg motif in the carboxyl terminus of the gamma(1)34.5 protein of herpes simplex virus type 1 is required for the formation of a high-molecular-weight complex that dephosphorylates eIF-2alpha.
    Cheng G, Gross M, Brett ME, He B.
    J Virol; 2001 Apr 14; 75(8):3666-74. PubMed ID: 11264356
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  • 15. Herpes simplex virus 1 infection activates the endoplasmic reticulum resident kinase PERK and mediates eIF-2alpha dephosphorylation by the gamma(1)34.5 protein.
    Cheng G, Feng Z, He B.
    J Virol; 2005 Feb 14; 79(3):1379-88. PubMed ID: 15650164
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  • 17. Eukaryotic elongation factor 1delta is hyperphosphorylated by the protein kinase encoded by the U(L)13 gene of herpes simplex virus 1.
    Kawaguchi Y, Van Sant C, Roizman B.
    J Virol; 1998 Mar 14; 72(3):1731-6. PubMed ID: 9499021
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  • 19. Functional genomic analysis of herpes simplex virus type 1 counteraction of the host innate response.
    Pasieka TJ, Baas T, Carter VS, Proll SC, Katze MG, Leib DA.
    J Virol; 2006 Aug 14; 80(15):7600-12. PubMed ID: 16840339
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