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@ARTICLE{Minniti:841291,
      author       = {Minniti, Elirosa and Byl, Jo Ann W. and Riccardi, Laura and
                      Sissi, Claudia and Rosini, Michela and De Vivo, Marco and
                      Minarini, Anna and Osheroff, Neil},
      title        = {{N}ovel xanthone-polyamine conjugates as catalytic
                      inhibitors of human topoisomerase {II}α},
      journal      = {Bioorganic $\&$ medicinal chemistry letters},
      volume       = {27},
      number       = {20},
      issn         = {0960-894X},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {FZJ-2017-08382},
      pages        = {4687 - 4693},
      year         = {2017},
      abstract     = {It has been proposed that xanthone derivatives with
                      anticancer potential act as topoisomerase II inhibitors
                      because they interfere with the ability of the enzyme to
                      bind its ATP cofactor. In order to further characterize
                      xanthone mechanism and generate compounds with potential as
                      anticancer drugs, we synthesized a series of derivatives in
                      which position 3 was substituted with different polyamine
                      chains. As determined by DNA relaxation and decatenation
                      assays, the resulting compounds are potent topoisomerase
                      IIα inhibitors. Although xanthone derivatives inhibit
                      topoisomerase IIα-catalyzed ATP hydrolysis, mechanistic
                      studies indicate that they do not act at the ATPase site.
                      Rather, they appear to function by blocking the ability of
                      DNA to stimulate ATP hydrolysis. On the basis of activity,
                      competition, and modeling studies, we propose that xanthones
                      interact with the DNA cleavage/ligation active site of
                      topoisomerase IIα and inhibit the catalytic activity of the
                      enzyme by interfering with the DNA strand passage step.},
      cin          = {IAS-5 / INM-9},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121},
      pnm          = {574 - Theory, modelling and simulation (POF3-574)},
      pid          = {G:(DE-HGF)POF3-574},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:28919339},
      UT           = {WOS:000412863700018},
      doi          = {10.1016/j.bmcl.2017.09.011},
      url          = {https://juser.fz-juelich.de/record/841291},
}