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dc.contributor.author
Venturi, Veronica
dc.contributor.author
Davies, Carolina
dc.contributor.author
Singh, Jonathan A.
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Matthews, James H.
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Bellows, David S.
dc.contributor.author
Northcote, Peter T.
dc.contributor.author
Keyzers, Robert A.
dc.contributor.author
Teesdale Spittle, Paul
dc.date.available
2017-05-19T14:42:25Z
dc.date.issued
2012-03-20
dc.identifier.citation
Venturi, Veronica; Davies, Carolina; Singh, Jonathan A.; Matthews, James H.; Bellows, David S.; et al.; The protein synthesis inhibitors mycalamides A and E have limited susceptibility toward the drug efflux network; John Wiley & Sons Inc; Journal Of Biochemical And Molecular Toxicology; 26; 3; 20-3-2012; 94-100
dc.identifier.issn
1095-6670
dc.identifier.uri
http://hdl.handle.net/11336/16714
dc.description.abstract
The mycalamides belong to a family of protein synthesis inhibitors noted for antifungal, antitumour, antiviral, immunosuppressive, and nematocidal activities. Here we report a systematic analysis of the role of drug efflux pumps in mycalamide resistance and the first isolation ofmycalamide E. In human cell lines, neither P-glycoprotein overexpression nor the use of efflux pump inhibitors significantly modulated mycalamide A toxicity in the systems tested. In Saccharomyces cerevisiae, it appears thatmycalamide A is subject to efflux by the principle mediator of xenobiotic efflux, Pdr5p alongwith the major facilitator superfamily pump Tpo1p. Mycalamide E showed a similar efflux profile. These results suggest that future drugs based on the mycalamides are likely to be valuable in situations where efflux pump?based resistance leads to failure of other chemotherapeutic approaches, although efflux may be a mediator of resistance in antifungal applications.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
John Wiley & Sons Inc
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Mycalamide
dc.subject
Efflux
dc.subject
Pdr
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Resistance
dc.subject.classification
Otras Ciencias Naturales y Exactas
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Otras Ciencias Naturales y Exactas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
The protein synthesis inhibitors mycalamides A and E have limited susceptibility toward the drug efflux network
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-05-02T18:19:08Z
dc.journal.volume
26
dc.journal.number
3
dc.journal.pagination
94-100
dc.journal.pais
Estados Unidos
dc.journal.ciudad
Nueva York
dc.description.fil
Fil: Venturi, Veronica. Victoria University of Wellington. Centre for Biodiscovery; Nueva Zelanda
dc.description.fil
Fil: Davies, Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Salta. Instituto de Patología Experimental. Universidad Nacional de Salta. Facultad de Cs.de la Salud. Instituto de Patología Experimental; Argentina. Victoria University of Wellington. Centre for Biodiscovery; Nueva Zelanda
dc.description.fil
Fil: Singh, Jonathan A.. Victoria University of Wellington. Centre for Biodiscovery; Nueva Zelanda
dc.description.fil
Fil: Matthews, James H.. Victoria University of Wellington. Centre for Biodiscovery; Nueva Zelanda
dc.description.fil
Fil: Bellows, David S.. Victoria University of Wellington. Centre for Biodiscovery; Nueva Zelanda
dc.description.fil
Fil: Northcote, Peter T.. Victoria University of Wellington. Centre for Biodiscovery; Nueva Zelanda
dc.description.fil
Fil: Keyzers, Robert A.. Victoria University of Wellington. Centre for Biodiscovery; Nueva Zelanda
dc.description.fil
Fil: Teesdale Spittle, Paul. Victoria University of Wellington. Centre for Biodiscovery; Nueva Zelanda
dc.journal.title
Journal Of Biochemical And Molecular Toxicology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1002/jbt.20414/full
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1002/jbt.20414
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