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Article: Chemical proteomics approaches to examine novel histone posttranslational modifications

TitleChemical proteomics approaches to examine novel histone posttranslational modifications
Authors
Issue Date2014
Citation
Current Opinion in Chemical Biology, 2014, v. 24, p. 80-90 How to Cite?
AbstractHistone posttranslational modifications (PTMs) play key roles in the regulation of many fundamental cellular processes, such as gene transcription, DNA damage repair and chromosome segregation. Significant progress has been made on the detection of a large variety of PTMs on histones. However, the identification of these PTMs’ regulating enzymes (i.e. ‘writers’ and ‘erasers’) and functional binding partners (i.e. ‘readers’) have been a relatively slow-paced process. As a result, cellular functions and regulatory mechanisms of many histone PTMs, particularly the newly identified ones, remain poorly understood. This review focuses on the recent progress in developing chemical proteomics approaches to profile readers, erasers and writers of histone PTMs. One of such efforts involves the development of the Cross-Linking-Assisted and SILAC-based Protein Identification (CLASPI) approach to examine PTM-mediated protein–protein interactions.
Persistent Identifierhttp://hdl.handle.net/10722/222463

 

DC FieldValueLanguage
dc.contributor.authorLI, X-
dc.contributor.authorLi, X-
dc.date.accessioned2016-01-18T07:40:52Z-
dc.date.available2016-01-18T07:40:52Z-
dc.date.issued2014-
dc.identifier.citationCurrent Opinion in Chemical Biology, 2014, v. 24, p. 80-90-
dc.identifier.urihttp://hdl.handle.net/10722/222463-
dc.description.abstractHistone posttranslational modifications (PTMs) play key roles in the regulation of many fundamental cellular processes, such as gene transcription, DNA damage repair and chromosome segregation. Significant progress has been made on the detection of a large variety of PTMs on histones. However, the identification of these PTMs’ regulating enzymes (i.e. ‘writers’ and ‘erasers’) and functional binding partners (i.e. ‘readers’) have been a relatively slow-paced process. As a result, cellular functions and regulatory mechanisms of many histone PTMs, particularly the newly identified ones, remain poorly understood. This review focuses on the recent progress in developing chemical proteomics approaches to profile readers, erasers and writers of histone PTMs. One of such efforts involves the development of the Cross-Linking-Assisted and SILAC-based Protein Identification (CLASPI) approach to examine PTM-mediated protein–protein interactions.-
dc.languageeng-
dc.relation.ispartofCurrent Opinion in Chemical Biology-
dc.titleChemical proteomics approaches to examine novel histone posttranslational modifications-
dc.typeArticle-
dc.identifier.emailLi, X: xiangli@hku.hk-
dc.identifier.authorityLi, X=rp01562-
dc.identifier.doi10.1016/j.cbpa.2014.10.015-
dc.identifier.hkuros256646-
dc.identifier.volume24-
dc.identifier.spage80-
dc.identifier.epage90-

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