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dc.contributor.authorMolina-Serrano, D.en
dc.contributor.authorSchiza, V.en
dc.contributor.authorKirmizis, Antonisen
dc.creatorMolina-Serrano, D.en
dc.creatorSchiza, V.en
dc.creatorKirmizis, Antonisen
dc.date.accessioned2019-11-04T12:52:22Z
dc.date.available2019-11-04T12:52:22Z
dc.date.issued2013
dc.identifier.urihttp://gnosis.library.ucy.ac.cy/handle/7/53257
dc.description.abstractEpigenetic modifications, including those occurring on DNA and on histone proteins, control gene expression by establishing and maintaining different chromatin states. In recent years, it has become apparent that epigenetic modifications do not function alone, but work together in various combinations, and crossregulate each other in a manner that diversifies their functional states. Arginine methylation is one of the numerous PTMs (post-translational modifications) occurring on histones, catalysed by a family of PRMTs (protein arginine methyltransferases). This modification is involved in the regulation of the epigenome largely by controlling the recruitment of effector molecules to chromatin. Histone arginine methylation associates with both active and repressed chromatin states depending on the residue involved and the configuration of the deposited methyl groups. The present review focuses on the increasing number of cross-talks between histone arginine methylation and other epigenetic modifications, and describe how these cross-talks influence factor binding to regulate transcription. Furthermore, we present models of general cross-talk mechanisms that emerge from the examples of histone arginine methylation and allude to various techniques that help decipher the interplay among epigenetic modifications. © 2013 Biochemical Society.en
dc.sourceBiochemical Society transactionsen
dc.source.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-84878342895&doi=10.1042%2fBST20130003&partnerID=40&md5=08a0471f2fb5865f8a242bae58a10693
dc.subjecthumanen
dc.subjectHumansen
dc.subjectpriority journalen
dc.subjectconference paperen
dc.subjectnonhumanen
dc.subjectsignal transductionen
dc.subjectgene expressionen
dc.subjectAnimalsen
dc.subjecttranscription regulationen
dc.subjectarginineen
dc.subjectDNA binding proteinen
dc.subjectprotein processingen
dc.subjectProtein Processing, Post-Translationalen
dc.subjecthistone H3en
dc.subjectHistonesen
dc.subjectEpigenesis, Geneticen
dc.subjectchromatinen
dc.subjectMethylationen
dc.subjecthistone modificationen
dc.subjecttranscription initiationen
dc.subjecthistone H4en
dc.subjectChromatin Assembly and Disassemblyen
dc.subjectchromatin immunoprecipitationen
dc.subjectDNA methylationen
dc.subjectEpigeneticsen
dc.subjectHistone arginine methylationen
dc.subjecthistone methylationen
dc.subjecthistone methyltransferaseen
dc.subjectModification cross-talken
dc.subjectPost-translational modificationen
dc.subjectProtein arginine methyltransferaseen
dc.subjectProtein-Arginine N-Methyltransferasesen
dc.subjectRAG2 proteinen
dc.subjectRING finger motifen
dc.subjecttranscription initiation siteen
dc.titleCross-talk among epigenetic modifications: Lessons from histone arginine methylationen
dc.typeinfo:eu-repo/semantics/article
dc.identifier.doi10.1042/BST20130003
dc.description.volume41
dc.description.startingpage751
dc.description.endingpage759
dc.author.facultyΣχολή Θετικών και Εφαρμοσμένων Επιστημών / Faculty of Pure and Applied Sciences
dc.author.departmentΤμήμα Βιολογικών Επιστημών / Department of Biological Sciences
dc.type.uhtypeArticleen
dc.description.notes<p>Cited By :24</p>en
dc.source.abbreviationBiochem.Soc.Trans.en
dc.contributor.orcidKirmizis, Antonis [0000-0002-3748-8711]
dc.gnosis.orcid0000-0002-3748-8711


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