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dc.creatorBarnham, Kevin J.es
dc.creatorDjuran, Milos I.es
dc.creatorMurdoch, Piedad del Socorroes
dc.creatorSadler, Peter J.es
dc.date.accessioned2016-05-05T07:56:59Z
dc.date.available2016-05-05T07:56:59Z
dc.date.issued1994
dc.identifier.issn0022-4936es
dc.identifier.urihttp://hdl.handle.net/11441/40764
dc.description.abstractNMR investigations of the kinetics and thermodynamics of the competitive binding of L-methionine (Met), L-histidine (His), and 5′-monophosphates of guanosine (5′-GMP), adenosine (5′-AMP), thymidine (5′-TMP) and cytidine (5′-CMP) to [Pt(dien)Cl]+ (dien = 1,5-diamino-3-azapentane) in aqueous solution show that 5′-GMP selectively displaces S-bound Met, a finding which has implications for DNA platination by anticancer drugs in vivo.es
dc.formatapplication/pdfes
dc.language.isoenges
dc.publisherChemical Societyes
dc.relation.ispartofJournal of the Chemical Society - Series Chemical Communications, 6, 721-722es
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectAdenosine phosphatees
dc.subjectAntineoplastic agentes
dc.subjectCytidine phosphatees
dc.subjectGuanosine phosphatees
dc.subjectHistidinees
dc.subjectMethioninees
dc.subjectPlatinum derivativees
dc.subjectThymidine phosphatees
dc.titleIntermolecular displacement of S-bound L-methionine on platinum(II) by guanosine 5′-monophosphate: Implications for the mechanism of action of anticancer drugses
dc.typeinfo:eu-repo/semantics/articlees
dc.type.versioninfo:eu-repo/semantics/publishedVersiones
dc.rights.accessrightsinfo:eu-repo/semantics/openAccesses
dc.contributor.affiliationUniversidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Moleculares
dc.relation.publisherversion10.1039/C39940000721es
dc.identifier.doihttp://dx.doi.org/10.1039/C39940000721es
idus.format.extent2 p.es
dc.identifier.idushttps://idus.us.es/xmlui/handle/11441/40764

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Attribution-NonCommercial-NoDerivatives 4.0 Internacional
Except where otherwise noted, this item's license is described as: Attribution-NonCommercial-NoDerivatives 4.0 Internacional