Proteomic characterization of novel histone post-translational modifications

被引：120

作者：

Arnaudo, Anna M. ^{[1
,2
]}

Garcia, Benjamin A. ^{[1
]}

机构：

[1] Univ Penn, Perelman Sch Med, Dept Biochem & Biophys, Epigenet Program, Philadelphia, PA 19104 USA

[2] Princeton Univ, Dept Mol Biol, Princeton, NJ 08544 USA

来源：

EPIGENETICS & CHROMATIN | 2013年 / 6卷

基金：

美国国家科学基金会;

关键词：

Histone post-translational modifications; Mass spectrometry; Proteomics; Epigenetics; O-GLCNAC; LYSINE; IDENTIFICATION; PROTEINS; CHROMATIN; H3; PHOSPHORYLATION; RESIDUES; PEPTIDE; FRAGMENTATION;

D O I：

10.1186/1756-8935-6-24

中图分类号：

Q3 [遗传学];

学科分类号：

071007 [遗传学];

摘要：

Histone post-translational modifications (PTMs) have been linked to a variety of biological processes and disease states, thus making their characterization a critical field of study. In the last 5 years, a number of novel sites and types of modifications have been discovered, greatly expanding the histone code. Mass spectrometric methods are essential for finding and validating histone PTMs. Additionally, novel proteomic, genomic and chemical biology tools have been developed to probe PTM function. In this snapshot review, proteomic tools for PTM identification and characterization will be discussed and an overview of PTMs found in the last 5 years will be provided.

引用

页数：7

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