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- W2000948892 abstract "Histone 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." @default.
- W2000948892 created "2016-06-24" @default.
- W2000948892 creator A5022526821 @default.
- W2000948892 date "2015-02-01" @default.
- W2000948892 modified "2023-10-18" @default.
- W2000948892 title "Chemical proteomics approaches to examine novel histone posttranslational modifications" @default.
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- W2000948892 doi "https://doi.org/10.1016/j.cbpa.2014.10.015" @default.
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