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dc.contributor.authorIsmail, HMSen_US
dc.contributor.authorHurd, PJen_US
dc.contributor.authorKhalil, MIMen_US
dc.contributor.authorKouzarides, Ten_US
dc.contributor.authorBannister, Aen_US
dc.contributor.authorGout, Ien_US
dc.date.accessioned2016-01-27T11:19:24Z
dc.date.available2013-03-28en_US
dc.date.issued2014-06en_US
dc.identifier.issn0730-2312en_US
dc.identifier.urihttp://qmro.qmul.ac.uk/xmlui/handle/123456789/10934
dc.description.sponsorshipThis work was supported by a project grant from the Association for International Cancer Research (AICR 09-0787). We would like to thank Dr. A. Zhyvoloup for advice and for providing recombinant S6Ks.en_US
dc.format.extent1048 - 1062en_US
dc.relation.ispartofJOURNAL OF CELLULAR BIOCHEMISTRYen_US
dc.rightsThis is the peer reviewed version of the following article: Ismail, Heba, et al. "S6 Kinase 2 Is Bound to Chromatin‐Nuclear Matrix Cellular Fractions and Is Able to Phosphorylate Histone H3 at Threonine 45 In Vitro and In Vivo." Journal of cellular biochemistry 115.6 (2014): 1048-1062., which has been published in final form at http://dx.doi.org/10.1002/jcb.24566. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.
dc.subjectS6K2en_US
dc.subjectH3 PHOSPHORYLATIONen_US
dc.subjectCHROMATINen_US
dc.titleS6 Kinase 2 Is Bound to Chromatin-Nuclear Matrix Cellular Fractions and Is Able to Phosphorylate Histone H3 at Threonine 45 In Vitro and In Vivoen_US
dc.typeArticle
dc.rights.holder© 2014 Wiley Periodicals, Inc.
dc.identifier.doi10.1002/jcb.24566en_US
pubs.author-urlhttp://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000334523300005&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=612ae0d773dcbdba3046f6df545e9f6aen_US
pubs.issue6en_US
pubs.notesNot knownen_US
pubs.publication-statusPublisheden_US
pubs.volume115en_US


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