These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


BIOMARKERS

Molecular Biopsy of Human Tumors

- a resource for Precision Medicine *

194 related articles for article (PubMed ID: 10882068)

  • 1. 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]  

  • 2. 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]  

  • 3. The herpes simplex virus processivity factor, UL42, binds DNA as a monomer.
    Randell JC; Coen DM
    J Mol Biol; 2004 Jan; 335(2):409-13. PubMed ID: 14672651
    [TBL] [Abstract][Full Text] [Related]  

  • 4. The positively charged surface of herpes simplex virus UL42 mediates DNA binding.
    Komazin-Meredith G; Santos WL; Filman DJ; Hogle JM; Verdine GL; Coen DM
    J Biol Chem; 2008 Mar; 283(10):6154-61. PubMed ID: 18178550
    [TBL] [Abstract][Full Text] [Related]  

  • 5. 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]  

  • 6. 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]  

  • 7. Genotypic characterization of herpes simplex virus DNA polymerase UL42 processivity factor.
    Burrel S; Aït-Arkoub Z; Agut H; Boutolleau D
    Antiviral Res; 2012 Jan; 93(1):199-203. PubMed ID: 22061617
    [TBL] [Abstract][Full Text] [Related]  

  • 8. 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]  

  • 9. 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]  

  • 10. Mutations that increase DNA binding by the processivity factor of herpes simplex virus affect virus production and DNA replication fidelity.
    Jiang C; Komazin-Meredith G; Tian W; Coen DM; Hwang CB
    J Virol; 2009 Aug; 83(15):7573-80. PubMed ID: 19474109
    [TBL] [Abstract][Full Text] [Related]  

  • 11. 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]  

  • 12. 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]  

  • 13. 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]  

  • 14. Crystal structure of the cytomegalovirus DNA polymerase subunit UL44 in complex with the C terminus from the catalytic subunit. Differences in structure and function relative to unliganded UL44.
    Appleton BA; Brooks J; Loregian A; Filman DJ; Coen DM; Hogle JM
    J Biol Chem; 2006 Feb; 281(8):5224-32. PubMed ID: 16371349
    [TBL] [Abstract][Full Text] [Related]  

  • 15. 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]  

  • 16. The herpes simplex virus type 1 DNA polymerase processivity factor increases fidelity without altering pre-steady-state rate constants for polymerization or excision.
    Chaudhuri M; Song L; Parris DS
    J Biol Chem; 2003 Mar; 278(11):8996-9004. PubMed ID: 12519753
    [TBL] [Abstract][Full Text] [Related]  

  • 17. 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]  

  • 18. Herpes simplex virus processivity factor UL42 imparts increased DNA-binding specificity to the viral DNA polymerase and decreased dissociation from primer-template without reducing the elongation rate.
    Weisshart K; Chow CS; Coen DM
    J Virol; 1999 Jan; 73(1):55-66. PubMed ID: 9847307
    [TBL] [Abstract][Full Text] [Related]  

  • 19. Secondary structure and structure-activity relationships of peptides corresponding to the subunit interface of herpes simplex virus DNA polymerase.
    Bridges KG; Hua Q; Brigham-Burke MR; Martin JD; Hensley P; Dahl CE; Digard P; Weiss MA; Coen DM
    J Biol Chem; 2000 Jan; 275(1):472-8. PubMed ID: 10617641
    [TBL] [Abstract][Full Text] [Related]  

  • 20. Specific residues in the connector loop of the human cytomegalovirus DNA polymerase accessory protein UL44 are crucial for interaction with the UL54 catalytic subunit.
    Loregian A; Appleton BA; Hogle JM; Coen DM
    J Virol; 2004 Sep; 78(17):9084-92. PubMed ID: 15308704
    [TBL] [Abstract][Full Text] [Related]  

    [Next]    [New Search]
    of 10.