BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

138 related articles for article (PubMed ID: 7964622)

  • 1. Role of the carboxy terminus of herpes simplex virus type 1 DNA polymerase in its interaction with UL42.
    Marsden HS; Murphy M; McVey GL; MacEachran KA; Owsianka AM; Stow ND
    J Gen Virol; 1994 Nov; 75 ( Pt 11)():3127-35. PubMed ID: 7964622
    [TBL] [Abstract][Full Text] [Related]  

  • 2. The catalytic subunit of herpes simplex virus type 1 DNA polymerase contains a nuclear localization signal in the UL42-binding region.
    Loregian A; Piaia E; Cancellotti E; Papini E; Marsden HS; Palù G
    Virology; 2000 Jul; 273(1):139-48. PubMed ID: 10891416
    [TBL] [Abstract][Full Text] [Related]  

  • 3. Identification of crucial hydrogen-bonding residues for the interaction of herpes simplex virus DNA polymerase subunits via peptide display, mutational, and calorimetric approaches.
    Bridges KG; Chow CS; Coen DM
    J Virol; 2001 Jun; 75(11):4990-8. PubMed ID: 11333878
    [TBL] [Abstract][Full Text] [Related]  

  • 4. Analysis of in vitro activities of herpes simplex virus type 1 UL42 mutant proteins: correlation with in vivo function.
    Thornton KE; Chaudhuri M; Monahan SJ; Grinstead LA; Parris DS
    Virology; 2000 Sep; 275(2):373-90. PubMed ID: 10998337
    [TBL] [Abstract][Full Text] [Related]  

  • 5. Deletions of the carboxy terminus of herpes simplex virus type 1 UL42 define a conserved amino-terminal functional domain.
    Tenney DJ; Hurlburt WW; Bifano M; Stevens JT; Micheletti PA; Hamatake RK; Cordingley MG
    J Virol; 1993 Apr; 67(4):1959-66. PubMed ID: 8383221
    [TBL] [Abstract][Full Text] [Related]  

  • 6. Effects of substitutions of arginine residues on the basic surface of herpes simplex virus UL42 support a role for DNA binding in processive DNA synthesis.
    Randell JC; Komazin G; Jiang C; Hwang CB; Coen DM
    J Virol; 2005 Sep; 79(18):12025-34. PubMed ID: 16140778
    [TBL] [Abstract][Full Text] [Related]  

  • 7. Mutations in the C terminus of herpes simplex virus type 1 DNA polymerase can affect binding and stimulation by its accessory protein UL42 without affecting basal polymerase activity.
    Tenney DJ; Micheletti PA; Stevens JT; Hamatake RK; Matthews JT; Sanchez AR; Hurlburt WW; Bifano M; Cordingley MG
    J Virol; 1993 Jan; 67(1):543-7. PubMed ID: 8380091
    [TBL] [Abstract][Full Text] [Related]  

  • 8. DNA and protein interactions of the small subunit of herpes simplex virus type 1 DNA polymerase.
    Franz C; Kühn FJ; Knopf CW
    Virology; 1999 Jan; 253(1):55-64. PubMed ID: 9887318
    [TBL] [Abstract][Full Text] [Related]  

  • 9. Interaction of herpes simplex virus type 1 DNA polymerase and the UL42 accessory protein with a model primer template.
    Gottlieb J; Challberg MD
    J Virol; 1994 Aug; 68(8):4937-45. PubMed ID: 8035492
    [TBL] [Abstract][Full Text] [Related]  

  • 10. The herpes simplex virus type 1 DNA polymerase accessory protein, UL42, contains a functional protease-resistant domain.
    Hamatake RK; Bifano M; Tenney DJ; Hurlburt WW; Cordingley MG
    J Gen Virol; 1993 Oct; 74 ( Pt 10)():2181-9. PubMed ID: 8409941
    [TBL] [Abstract][Full Text] [Related]  

  • 11. Two regions of the herpes simplex virus type 1 UL42 protein are required for its functional interaction with the viral DNA polymerase.
    Monahan SJ; Barlam TF; Crumpacker CS; Parris DS
    J Virol; 1993 Oct; 67(10):5922-31. PubMed ID: 8396660
    [TBL] [Abstract][Full Text] [Related]  

  • 12. The essential in vivo function of the herpes simplex virus UL42 protein correlates with its ability to stimulate the viral DNA polymerase in vitro.
    Reddig PJ; Grinstead LA; Monahan SJ; Johnson PA; Parris DS
    Virology; 1994 May; 200(2):447-56. PubMed ID: 8178434
    [TBL] [Abstract][Full Text] [Related]  

  • 13. Sequences at the C-terminus of the herpes simplex virus type 1 UL30 protein are dispensable for DNA polymerase activity but not for viral origin-dependent DNA replication.
    Stow ND
    Nucleic Acids Res; 1993 Jan; 21(1):87-92. PubMed ID: 8382792
    [TBL] [Abstract][Full Text] [Related]  

  • 14. The extreme C terminus of herpes simplex virus DNA polymerase is crucial for functional interaction with processivity factor UL42 and for viral replication.
    Digard P; Bebrin WR; Weisshart K; Coen DM
    J Virol; 1993 Jan; 67(1):398-406. PubMed ID: 8380085
    [TBL] [Abstract][Full Text] [Related]  

  • 15. Functional analysis of the herpes simplex virus UL42 protein.
    Digard P; Chow CS; Pirrit L; Coen DM
    J Virol; 1993 Mar; 67(3):1159-68. PubMed ID: 8437207
    [TBL] [Abstract][Full Text] [Related]  

  • 16. Evidence against a simple tethering model for enhancement of herpes simplex virus DNA polymerase processivity by accessory protein UL42.
    Chaudhuri M; Parris DS
    J Virol; 2002 Oct; 76(20):10270-81. PubMed ID: 12239303
    [TBL] [Abstract][Full Text] [Related]  

  • 17. Interaction between the herpes simplex virus type 1 origin-binding and DNA polymerase accessory proteins.
    Monahan SJ; Grinstead LA; Olivieri W; Parris DS
    Virology; 1998 Feb; 241(1):122-30. PubMed ID: 9454723
    [TBL] [Abstract][Full Text] [Related]  

  • 18. Nuclear import of HSV-1 DNA polymerase processivity factor UL42 is mediated by a C-terminally located bipartite nuclear localization signal.
    Alvisi G; Avanzi S; Musiani D; Camozzi D; Leoni V; Ly-Huynh JD; Ripalti A
    Biochemistry; 2008 Dec; 47(52):13764-77. PubMed ID: 19053255
    [TBL] [Abstract][Full Text] [Related]  

  • 19. The crystal structure of an unusual processivity factor, herpes simplex virus UL42, bound to the C terminus of its cognate polymerase.
    Zuccola HJ; Filman DJ; Coen DM; Hogle JM
    Mol Cell; 2000 Feb; 5(2):267-78. PubMed ID: 10882068
    [TBL] [Abstract][Full Text] [Related]  

  • 20. The catalytic subunit of the DNA polymerase of herpes simplex virus type 1 interacts specifically with the C terminus of the UL8 component of the viral helicase-primase complex.
    Marsden HS; McLean GW; Barnard EC; Francis GJ; MacEachran K; Murphy M; McVey G; Cross A; Abbotts AP; Stow ND
    J Virol; 1997 Sep; 71(9):6390-7. PubMed ID: 9261356
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 7.