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Article: Roles of histone ubiquitylation in DNA damage signaling

TitleRoles of histone ubiquitylation in DNA damage signaling
Authors
KeywordsDna Damage
Histone Ubiquitylation
Rnf168
Rnf8
Ubiquitin Ligase
Issue Date2011
Citation
Frontiers In Biology, 2011, v. 6 n. 5, p. 390-397 How to Cite?
AbstractHistone ubiquitylation has emerged as an important chromatin modification associated with DNA damage signaling and repair pathways. These histone marks, laid down by E3 ubiquitin ligases that include RNF8 and RNF168, decorate chromatin domains surrounding DNA double-strand breaks (DSBs). Recent work implicated ubiquitylated histones in orchestrating cell cycle checkpoints, DNA repair and gene transcription. Here we summarize recent advances that contribute to our current knowledge of the highly dynamic nature of DSB-associated histone ubiquitylation, and discuss major challenges ahead in understanding the versatility of ubiquitin conjugation in maintaining genome stability. © 2011 Higher Education Press and Springer-Verlag Berlin Heidelberg.
Persistent Identifierhttp://hdl.handle.net/10722/149769
ISSN
References

 

DC FieldValueLanguage
dc.contributor.authorDong, SSen_US
dc.contributor.authorHuen, MSYen_US
dc.date.accessioned2012-06-26T05:58:19Z-
dc.date.available2012-06-26T05:58:19Z-
dc.date.issued2011en_US
dc.identifier.citationFrontiers In Biology, 2011, v. 6 n. 5, p. 390-397en_US
dc.identifier.issn1674-7984en_US
dc.identifier.urihttp://hdl.handle.net/10722/149769-
dc.description.abstractHistone ubiquitylation has emerged as an important chromatin modification associated with DNA damage signaling and repair pathways. These histone marks, laid down by E3 ubiquitin ligases that include RNF8 and RNF168, decorate chromatin domains surrounding DNA double-strand breaks (DSBs). Recent work implicated ubiquitylated histones in orchestrating cell cycle checkpoints, DNA repair and gene transcription. Here we summarize recent advances that contribute to our current knowledge of the highly dynamic nature of DSB-associated histone ubiquitylation, and discuss major challenges ahead in understanding the versatility of ubiquitin conjugation in maintaining genome stability. © 2011 Higher Education Press and Springer-Verlag Berlin Heidelberg.en_US
dc.languageengen_US
dc.relation.ispartofFrontiers in Biologyen_US
dc.subjectDna Damageen_US
dc.subjectHistone Ubiquitylationen_US
dc.subjectRnf168en_US
dc.subjectRnf8en_US
dc.subjectUbiquitin Ligaseen_US
dc.titleRoles of histone ubiquitylation in DNA damage signalingen_US
dc.typeArticleen_US
dc.identifier.emailHuen, MSY:huen.michael@hku.hken_US
dc.identifier.authorityHuen, MSY=rp01336en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1007/s11515-011-1135-5en_US
dc.identifier.scopuseid_2-s2.0-80053638243en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-80053638243&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume6en_US
dc.identifier.issue5en_US
dc.identifier.spage390en_US
dc.identifier.epage397en_US
dc.identifier.scopusauthoridDong, SS=35788109500en_US
dc.identifier.scopusauthoridHuen, MSY=23004751500en_US

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