http://www.cnr.it/ontology/cnr/individuo/prodotto/ID61435
Glutathione transferases as targets for cancer therapy (Articolo in rivista)
- Type
- Label
- Glutathione transferases as targets for cancer therapy (Articolo in rivista) (literal)
- Anno
- 2009-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.2174/187152009789056895 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Paolo Ruzza; Antonio Rosato; Carlo Riccardo Rossi; Maura Floreani; Luigi Quintieri (literal)
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- Rivista
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
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- Scopu (literal)
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Institute of Biomolecular Chemistry of CNR, Padova Unit, Padova, Italy; Department of Oncology and Surgical Sciences, University of Padova, Italy; Istituto Oncologico Veneto, IOV, Padova, Italy; Department of Pharmacology and Anesthesiology, University of Padova, Italy (literal)
- Titolo
- Glutathione transferases as targets for cancer therapy (literal)
- Abstract
- Besides catalyzing the inactivation of various electrophile-producing anticancer agents via conjugation to the tripeptide glutathione, some cytosolic proteins belonging to the glutathione transferase (formerly glutatione-S-transferase; GST) superfamily are emerging as negative modulators of stress/drug-induced cell apoptosis through the interaction with specific signaling kinases. In addition, several data link the overexpression of some GSTs, in particular GSTP1-1, to both natural and acquired resistance to various structurally unrelated anticancer drugs. Tumor overexpression of these proteins has provided a rationale for the search of GST inhibitors and GSTactivated cytotoxic prodrugs. In the present review we discuss the current structural and pharmacological knowledge of both types of GST-targeting compounds. (literal)
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