Selected cytotoxic gold compounds cause significant inhibition of 20S proteasome catalytic activities
- Publikationstyp:
- Zeitschriftenaufsatz
- Metadaten:
-
- Autoren
- Nicola Micale
- Tanja Schirmeister
- Roberta Ettari
- Maria A Cinellu
- Laura Maiore
- Maria Serratrice
- Chiara Gabbiani
- Lara Massai
- Luigi Messori
- Autoren-URL
- https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000343790700010&DestLinkType=FullRecord&DestApp=WOS_CPL
- DOI
- 10.1016/j.jinorgbio.2014.08.001
- eISSN
- 1873-3344
- Externe Identifier
- Clarivate Analytics Document Solution ID: AR7XQ
- PubMed Identifier: 25217719
- ISSN
- 0162-0134
- Zeitschrift
- JOURNAL OF INORGANIC BIOCHEMISTRY
- Schlüsselwörter
- Proteasome
- Gold compounds
- Anticancer drugs
- Enzyme inhibition
- Paginierung
- 79 - 82
- Datum der Veröffentlichung
- 2014
- Status
- Published
- Titel
- Selected cytotoxic gold compounds cause significant inhibition of 20S proteasome catalytic activities
- Sub types
- Article
- Ausgabe der Zeitschrift
- 141
Datenquelle: Web of Science (Lite)
- Andere Metadatenquellen:
-
- Autoren
- Nicola Micale
- Tanja Schirmeister
- Roberta Ettari
- Maria A Cinellu
- Laura Maiore
- Maria Serratrice
- Chiara Gabbiani
- Lara Massai
- Luigi Messori
- DOI
- 10.1016/j.jinorgbio.2014.08.001
- ISSN
- 0162-0134
- Zeitschrift
- Journal of Inorganic Biochemistry
- Sprache
- en
- Paginierung
- 79 - 82
- Datum der Veröffentlichung
- 2014
- Status
- Published
- Herausgeber
- Elsevier BV
- Herausgeber URL
- http://dx.doi.org/10.1016/j.jinorgbio.2014.08.001
- Datum der Datenerfassung
- 2018
- Titel
- Selected cytotoxic gold compounds cause significant inhibition of 20S proteasome catalytic activities
- Ausgabe der Zeitschrift
- 141
Datenquelle: Crossref
- Abstract
- Six structurally diverse cytotoxic gold compounds are reported to cause profound and differential inhibition of the three main catalytic activities of purified 20S proteasome whilst auranofin, an established gold(I) drug in clinical use, is nearly ineffective. In particular, the gold(I) complex [(pbiH)Au(PPh3)]PF6, turns out to be the most potent inhibitor of all three enzyme activities with sub-micromolar IC50 values. The present results further support the view that proteasome inhibition may play a major--yet not exclusive--role in the cytotoxic actions of gold based anticancer agents.
- Addresses
- Department of Drug Sciences and Health Products, University of Messina, Viale Annunziata, 98168 Messina, Italy. Electronic address: nmicale@unime.it.
- Autoren
- Nicola Micale
- Tanja Schirmeister
- Roberta Ettari
- Maria A Cinellu
- Laura Maiore
- Maria Serratrice
- Chiara Gabbiani
- Lara Massai
- Luigi Messori
- DOI
- 10.1016/j.jinorgbio.2014.08.001
- eISSN
- 1873-3344
- Externe Identifier
- PubMed Identifier: 25217719
- Funding acknowledgements
- Beneficentia Stiftung (Vaduz, Liechtenstein):
- AIRC: IG- 12085
- Regione Autonoma della Sardegna (RAS):
- COST Action: CM1105
- Open access
- false
- ISSN
- 0162-0134
- Zeitschrift
- Journal of inorganic biochemistry
- Schlüsselwörter
- Humans
- Auranofin
- Proteasome Endopeptidase Complex
- Antineoplastic Agents
- Cytotoxins
- Inhibitory Concentration 50
- Structure-Activity Relationship
- Organogold Compounds
- Biocatalysis
- Coordination Complexes
- Proteasome Inhibitors
- Sprache
- eng
- Medium
- Print-Electronic
- Online publication date
- 2014
- Paginierung
- 79 - 82
- Datum der Veröffentlichung
- 2014
- Status
- Published
- Datum der Datenerfassung
- 2014
- Titel
- Selected cytotoxic gold compounds cause significant inhibition of 20S proteasome catalytic activities.
- Sub types
- Research Support, Non-U.S. Gov't
- Journal Article
- Ausgabe der Zeitschrift
- 141
Datenquelle: Europe PubMed Central
- Abstract
- Six structurally diverse cytotoxic gold compounds are reported to cause profound and differential inhibition of the three main catalytic activities of purified 20S proteasome whilst auranofin, an established gold(I) drug in clinical use, is nearly ineffective. In particular, the gold(I) complex [(pbiH)Au(PPh3)]PF6, turns out to be the most potent inhibitor of all three enzyme activities with sub-micromolar IC50 values. The present results further support the view that proteasome inhibition may play a major--yet not exclusive--role in the cytotoxic actions of gold based anticancer agents.
- Date of acceptance
- 2014
- Autoren
- Nicola Micale
- Tanja Schirmeister
- Roberta Ettari
- Maria A Cinellu
- Laura Maiore
- Maria Serratrice
- Chiara Gabbiani
- Lara Massai
- Luigi Messori
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/25217719
- DOI
- 10.1016/j.jinorgbio.2014.08.001
- eISSN
- 1873-3344
- Zeitschrift
- J Inorg Biochem
- Schlüsselwörter
- Anticancer drugs
- Enzyme inhibition
- Gold compounds
- Proteasome
- Antineoplastic Agents
- Auranofin
- Biocatalysis
- Coordination Complexes
- Cytotoxins
- Humans
- Inhibitory Concentration 50
- Organogold Compounds
- Proteasome Endopeptidase Complex
- Proteasome Inhibitors
- Structure-Activity Relationship
- Sprache
- eng
- Country
- United States
- Paginierung
- 79 - 82
- PII
- S0162-0134(14)00221-9
- Datum der Veröffentlichung
- 2014
- Status
- Published
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2015
- Titel
- Selected cytotoxic gold compounds cause significant inhibition of 20S proteasome catalytic activities.
- Sub types
- Journal Article
- Research Support, Non-U.S. Gov't
- Ausgabe der Zeitschrift
- 141
Datenquelle: PubMed
- Beziehungen:
- Eigentum von