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Structural basis for inhibitor specificity in human poly(ADP-ribose) polymerase-3.
Stockholm University, Faculty of Science, Department of Genetics, Microbiology and Toxicology.
Stockholm University, Faculty of Science, Department of Genetics, Microbiology and Toxicology.
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2009 (English)In: Journal of medicinal chemistry, ISSN 1520-4804, Vol. 52, no 9, 3108-11 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2009. Vol. 52, no 9, 3108-11 p.
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URN: urn:nbn:se:su:diva-32010DOI: 10.1021/jm900052jISI: 000265911800050PubMedID: 19354255OAI: oai:DiVA.org:su-32010DiVA: diva2:279203
Available from: 2009-12-02 Created: 2009-12-02 Last updated: 2009-12-02Bibliographically approved

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Jemth, Ann-SofieLoseva, OlgaHelleday, Thomas
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