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Träfflista för sökning "(WFRF:(Jemth Ann Sofie)) srt2:(2009)"

Sökning: (WFRF:(Jemth Ann Sofie)) > (2009)

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1.
  • Bryant, Helen E, et al. (författare)
  • PARP is activated at stalled forks to mediate Mre11-dependent replication restart and recombination.
  • 2009
  • Ingår i: The EMBO journal. - : Wiley. - 1460-2075 .- 0261-4189. ; 28:17, s. 2601-15
  • Tidskriftsartikel (refereegranskat)abstract
    • If replication forks are perturbed, a multifaceted response including several DNA repair and cell cycle checkpoint pathways is activated to ensure faithful DNA replication. Here, we show that poly(ADP-ribose) polymerase 1 (PARP1) binds to and is activated by stalled replication forks that contain small gaps. PARP1 collaborates with Mre11 to promote replication fork restart after release from replication blocks, most likely by recruiting Mre11 to the replication fork to promote resection of DNA. Both PARP1 and PARP2 are required for hydroxyurea-induced homologous recombination to promote cell survival after replication blocks. Together, our data suggest that PARP1 and PARP2 detect disrupted replication forks and attract Mre11 for end processing that is required for subsequent recombination repair and restart of replication forks.
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2.
  • Lehtiö, Lari, et al. (författare)
  • Structural basis for inhibitor specificity in human poly(ADP-ribose) polymerase-3.
  • 2009
  • Ingår i: Journal of medicinal chemistry. - : American Chemical Society (ACS). - 1520-4804 .- 0022-2623. ; 52:9, s. 3108-11
  • Tidskriftsartikel (refereegranskat)abstract
    • Poly(ADP-ribose) polymerases (PARPs) activate DNA repair mechanisms upon stress- and cytotoxin-induced DNA damage, and inhibition of PARP activity is a lead in cancer drug therapy. We present a structural and functional analysis of the PARP domain of human PARP-3 in complex with several inhibitors. Of these, KU0058948 is the strongest inhibitor of PARP-3 activity. The presented crystal structures highlight key features for potent inhibitor binding and suggest routes for creating isoenzyme-specific PARP inhibitors.
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