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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2017: 3.022

CiteScore 2017: 2.81

SCImago Journal Rank (SJR) 2017: 1.562
Source Normalized Impact per Paper (SNIP) 2017: 0.705

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1437-4315
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Volume 393, Issue 11

Issues

Interaction between natural compounds and human topoisomerase I

Silvia Castelli
  • Department of Biology, University of Rome Tor Vergata, Via Della Ricerca Scientifica, I-00133 Rome, Italy
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/ Andrea Coletta
  • Department of Biology, University of Rome Tor Vergata, Via Della Ricerca Scientifica, I-00133 Rome, Italy
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/ Ilda D’Annessa
  • Department of Biology, University of Rome Tor Vergata, Via Della Ricerca Scientifica, I-00133 Rome, Italy
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/ Paola Fiorani
  • Institute of Translational Pharmacology, National Research Council, CNR, Via Del Fosso del Cavaliere 100, I-00133 Rome, Italy
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/ Cinzia Tesauro
  • Department of Biology, University of Rome Tor Vergata, Via Della Ricerca Scientifica, I-00133 Rome, Italy
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/ Alessandro Desideri
  • Corresponding author
  • Department of Biology, University of Rome Tor Vergata, Via Della Ricerca Scientifica, I-00133 Rome, Italy
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Published Online: 2012-10-11 | DOI: https://doi.org/10.1515/hsz-2012-0240

Abstract

Eukaryotic topoisomerase I (Top1) is a monomeric enzyme that catalyzes the relaxation of supercoiled DNA during important processes including DNA replication, transcription, recombination and chromosome condensation. Human Top1 I is of significant medical interest since it is the unique cellular target of camptothecin (CPT), a plant alkaloid that rapidly blocks both DNA and RNA synthesis. In this review, together with CPT, we point out the interaction between human Top1 and some natural compounds, such us terpenoids, flavonoids, stilbenes and fatty acids. The drugs can interact with the enzyme at different levels perturbing the binding, cleavage, rotation or religation processes. Here we focus on different assays that can be used to identify the catalytic step of the enzyme inhibited by different natural compounds.

Keywords: enzymatic catalytic steps; inhibition mechanism; natural compounds; topoisomerase I

About the article

Corresponding author: Alessandro Desideri, Department of Biology, University of Rome Tor Vergata, Via Della Ricerca Scientifica, I-00133 Rome, Italy


Received: 2012-06-25

Accepted: 2012-07-22

Published Online: 2012-10-11

Published in Print: 2012-11-01


Citation Information: , Volume 393, Issue 11, Pages 1327–1340, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/hsz-2012-0240.

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