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Site-specific incorporation of μ-N-crotonyllysine into histones

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dc.contributor.authorKim, C.H.-
dc.contributor.authorKang, M.-
dc.contributor.authorKim, H.J.-
dc.contributor.authorChatterjee, A.-
dc.contributor.authorSchultz, P.G.-
dc.date.accessioned2021-09-07T04:21:42Z-
dc.date.available2021-09-07T04:21:42Z-
dc.date.created2021-06-17-
dc.date.issued2012-
dc.identifier.issn1433-7851-
dc.identifier.urihttps://scholar.korea.ac.kr/handle/2021.sw.korea/110718-
dc.description.abstractA novel post-translationally modified amino acid, crotonyllysine (Kcr), was genetically incorporated into proteins in bacterial and mammalian cells using an evolved pyrrolysyl-tRNA/synthetase-tRNA pair. The ability to produce histones with homogenous, site-specific Kcr modifications will be valuable in elucidating the biological role of this recently identified post-translational modification. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.-
dc.languageEnglish-
dc.language.isoen-
dc.subjectCrotonylations-
dc.subjectHistones-
dc.subjectMammalian cells-
dc.subjectModified amino acids-
dc.subjectNon natural amino acids-
dc.subjectPost-translational modifications-
dc.subjectSite-specific-
dc.subjectAmino acids-
dc.subjectProteins-
dc.subjectamino acid transfer RNA ligase-
dc.subjectdrug derivative-
dc.subjectepsilon N crotonyllysine-
dc.subjectepsilon-N-crotonyllysine-
dc.subjecthistone-
dc.subjectlysine-
dc.subjectrecombinant protein-
dc.subjectarticle-
dc.subjectcell line-
dc.subjectchemistry-
dc.subjectEscherichia coli-
dc.subjectgenetics-
dc.subjecthuman-
dc.subjectmetabolism-
dc.subjectmutation-
dc.subjectprotein engineering-
dc.subjectprotein processing-
dc.subjectAmino Acyl-tRNA Synthetases-
dc.subjectCell Line-
dc.subjectEscherichia coli-
dc.subjectHistones-
dc.subjectHumans-
dc.subjectLysine-
dc.subjectMutation-
dc.subjectProtein Engineering-
dc.subjectProtein Processing, Post-Translational-
dc.subjectRecombinant Proteins-
dc.titleSite-specific incorporation of μ-N-crotonyllysine into histones-
dc.typeArticle-
dc.contributor.affiliatedAuthorKim, H.J.-
dc.identifier.doi10.1002/anie.201203349-
dc.identifier.scopusid2-s2.0-84863837242-
dc.identifier.bibliographicCitationAngewandte Chemie - International Edition, v.51, no.29, pp.7246 - 7249-
dc.relation.isPartOfAngewandte Chemie - International Edition-
dc.citation.titleAngewandte Chemie - International Edition-
dc.citation.volume51-
dc.citation.number29-
dc.citation.startPage7246-
dc.citation.endPage7249-
dc.type.rimsART-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.subject.keywordPlusCrotonylations-
dc.subject.keywordPlusHistones-
dc.subject.keywordPlusMammalian cells-
dc.subject.keywordPlusModified amino acids-
dc.subject.keywordPlusNon natural amino acids-
dc.subject.keywordPlusPost-translational modifications-
dc.subject.keywordPlusSite-specific-
dc.subject.keywordPlusAmino acids-
dc.subject.keywordPlusProteins-
dc.subject.keywordPlusamino acid transfer RNA ligase-
dc.subject.keywordPlusdrug derivative-
dc.subject.keywordPlusepsilon N crotonyllysine-
dc.subject.keywordPlusepsilon-N-crotonyllysine-
dc.subject.keywordPlushistone-
dc.subject.keywordPluslysine-
dc.subject.keywordPlusrecombinant protein-
dc.subject.keywordPlusarticle-
dc.subject.keywordPluscell line-
dc.subject.keywordPluschemistry-
dc.subject.keywordPlusEscherichia coli-
dc.subject.keywordPlusgenetics-
dc.subject.keywordPlushuman-
dc.subject.keywordPlusmetabolism-
dc.subject.keywordPlusmutation-
dc.subject.keywordPlusprotein engineering-
dc.subject.keywordPlusprotein processing-
dc.subject.keywordPlusAmino Acyl-tRNA Synthetases-
dc.subject.keywordPlusCell Line-
dc.subject.keywordPlusEscherichia coli-
dc.subject.keywordPlusHistones-
dc.subject.keywordPlusHumans-
dc.subject.keywordPlusLysine-
dc.subject.keywordPlusMutation-
dc.subject.keywordPlusProtein Engineering-
dc.subject.keywordPlusProtein Processing, Post-Translational-
dc.subject.keywordPlusRecombinant Proteins-
dc.subject.keywordAuthorCrotonylations-
dc.subject.keywordAuthorHistones-
dc.subject.keywordAuthorNonnatural amino acids-
dc.subject.keywordAuthorPost-translational modifications-
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