Interaction between natural compounds and human topoisomerase i (Articolo in rivista)

Type
Label
  • Interaction between natural compounds and human topoisomerase i (Articolo in rivista) (literal)
Anno
  • 2012-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1515/hsz-2012-0240 (literal)
Alternative label
  • Castelli S.; Coletta A.; D'Annessa I.; Fiorani P.; Tesauro C.; Desideri A. (2012)
    Interaction between natural compounds and human topoisomerase i
    in Biological chemistry (Internet)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Castelli S.; Coletta A.; D'Annessa I.; Fiorani P.; Tesauro C.; Desideri A. (literal)
Pagina inizio
  • 1327 (literal)
Pagina fine
  • 1340 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://www.scopus.com/inward/record.url?eid=2-s2.0-84869469288&partnerID=q2rCbXpz (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 393 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 11 (literal)
Note
  • Scopu (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Department of Biology, University of Rome Tor Vergata, Via della Ricerca Scientifica, I-00133 Rome, Italy; Institute of Translational Pharmacology, National Research Council, CNR, Via Del Fosso del Cavaliere 100, I-00133 Rome, Italy (literal)
Titolo
  • Interaction between natural compounds and human topoisomerase i (literal)
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. © 2012 Walter de Gruyter GmbH, Berlin/Boston. (literal)
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