Cyclo[n]pyrroles:  Size and Site-Specific Binding to G-Quadruplexes

Dataset UNKNOWN
Baker, Erin Shammel; Lee, Jeong Tae; Sessler, Jonathan L.; Bowers, Michael T.;
(2006)
  • Publisher: Figshare
  • Related identifiers: doi: 10.1021/ja0564968.s003, doi: 10.1021/ja0564968.s002, doi: 10.1021/ja0564968.s005, doi: 10.1021/ja0564968.s004
  • Subject: binding mode | Neuroscience | enzyme telomerase | dynamics calculations | AG | ion mobility | diprotonated cyclo | binding strength | pyrroles display | ion mobility measurements | Cell Biology | anticancer drug design | Biochemistry | Pharmacology | porphyrin analogues | mass spectrometry | Cancer | Biophysics | arrival time distributions
    • FOR: 29999 Physical Sciences not elsewhere classified | 110309 Infectious Diseases | 39999 Chemical Sciences not elsewhere classified

Inhibiting the enzyme telomerase by stabilizing the G-quadruplex has potential in anticancer drug design. Diprotonated cyclo[<i>n</i>]pyrroles represent a set of expanded porphyrin analogues with structures similar to that of telomestatin, a natural product known ... View more
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