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dc.contributor.authorYe, Wenjie
dc.contributor.authorSeneviratne, Uthpala I.
dc.contributor.authorChao, Ming-Wei
dc.contributor.authorWogan, Gerald N.
dc.contributor.authorSkipper, Paul L.
dc.contributor.authorKodihalli, Ravindra
dc.contributor.authorTannenbaum, Steven Robert
dc.date.accessioned2013-11-13T18:00:06Z
dc.date.available2013-11-13T18:00:06Z
dc.date.issued2012-11
dc.date.submitted2012-11
dc.identifier.issn0893-228X
dc.identifier.issn1520-5010
dc.identifier.urihttp://hdl.handle.net/1721.1/82110
dc.description.abstractAminophenols can redox cycle through the corresponding quinone imines to generate ROS. The electrophilic quinone imine intermediate can react with protein thiols as a mechanism of immobilization in vivo. Here, we describe the previously unkown transimination of a quinone imine by lysine as an alternative anchoring mechanism. The redox properties of the condensation product remain largely unchanged because the only structural change to the redox nucleus is the addition of an alkyl substituent to the imine nitrogen. Transimination enables targeting of histone proteins since histones are lysine-rich but nearly devoid of cysteines. Consequently, quinone imines can be embedded in the nucleosome and may be expected to produce ROS in maximal proximity to the genome.en_US
dc.description.sponsorshipAgilent Technologiesen_US
dc.language.isoen_US
dc.publisherAmerican Chemical Society (ACS)en_US
dc.relation.isversionofhttp://dx.doi.org/10.1021/tx3004517en_US
dc.rightsArticle is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.en_US
dc.sourcePMCen_US
dc.titleTransimination of Quinone Imines: A Mechanism for Embedding Exogenous Redox Activity into the Nucleosomeen_US
dc.typeArticleen_US
dc.identifier.citationYe, Wenjie, Uthpala I. Seneviratne, Ming-Wei Chao, Kodihalli C. Ravindra, Gerald N. Wogan, Steven R. Tannenbaum, and Paul L. Skipper. “Transimination of Quinone Imines: A Mechanism for Embedding Exogenous Redox Activity into the Nucleosome.” Chemical Research in Toxicology 25, no. 12 (December 17, 2012): 2627-2629. © 2012 American Chemical Societyen_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Biological Engineeringen_US
dc.contributor.departmentMassachusetts Institute of Technology. Department of Chemistryen_US
dc.contributor.mitauthorYe, Wenjieen_US
dc.contributor.mitauthorSeneviratne, Uthpala I.en_US
dc.contributor.mitauthorChao, Ming-Weien_US
dc.contributor.mitauthorKodihalli, Ravindraen_US
dc.contributor.mitauthorWogan, Gerald N.en_US
dc.contributor.mitauthorTannenbaum, Steven Roberten_US
dc.contributor.mitauthorSkipper, Paul L.en_US
dc.relation.journalChemical Research in Toxicologyen_US
dc.eprint.versionFinal published versionen_US
dc.type.urihttp://purl.org/eprint/type/JournalArticleen_US
eprint.statushttp://purl.org/eprint/status/PeerRevieweden_US
dspace.orderedauthorsYe, Wenjie; Seneviratne, Uthpala I.; Chao, Ming-Wei; Ravindra, Kodihalli C.; Wogan, Gerald N.; Tannenbaum, Steven R.; Skipper, Paul L.en_US
dc.identifier.orcidhttps://orcid.org/0000-0001-6774-9639
dc.identifier.orcidhttps://orcid.org/0000-0003-0771-9889
mit.licensePUBLISHER_POLICYen_US


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